[ { "key": "H5BSSHD3", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/H5BSSHD3", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/H5BSSHD3", "type": "text/html" } }, "meta": { "createdByUser": { "id": 250761, "username": "npattara", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/npattara", "type": "text/html" } } }, "creatorSummary": "O'Quinn et al.", "parsedDate": "2001-06", "numChildren": 0 }, "data": { "key": "H5BSSHD3", "version": 1, "itemType": "journalArticle", "title": "Burkholderia pseudomallei kills the nematode Caenorhabditis elegans using an endotoxin-mediated paralysis", "creators": [ { "creatorType": "author", "firstName": "A L", "lastName": "O'Quinn" }, { "creatorType": "author", "firstName": "E M", "lastName": "Wiegand" }, { "creatorType": "author", "firstName": "J A", "lastName": "Jeddeloh" } ], "abstractNote": "We investigated a non-mammalian host model system for fitness in genetic screening for virulence-attenuating mutations in the potential biowarfare agents Burkholderia pseudomallei and Burkholderia mallei. We determined that B. pseudomallei is able to cause 'disease-like' symptoms and kill the nematode Caenorhabditis elegans. Analysis of killing in the surrogate disease model with B. pseudomallei mutants indicated that killing did not require lipopolysaccharide (LPS) O-antigen, aminoglycoside/macrolide efflux pumping, type II pathway-secreted exoenzymes or motility. Burkholderia thailandensis and some strains of Burkholderia cepacia also killed nematodes. Manipulation of the nematode host genotype suggests that the neuromuscular intoxication caused by both B. pseudomallei and B. thailandensis acts in part through a disruption of normal Ca2+ signal transduction. Both species produce a UV-sensitive, gamma-irradiation-resistant, limited diffusion, paralytic agent as part of their nematode pathogenic mechanism. The results of this investigation suggest that killing by B. pseudomallei is an active process in C. elegans, and that the C. elegans model might be useful for the identification of vertebrate animal virulence factors in B. pseudomallei.", "publicationTitle": "Cellular Microbiology", "publisher": "", "place": "", "date": "Jun 2001", "volume": "3", "issue": "6", "section": "", "partNumber": "", "partTitle": "", "pages": "381-393", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Cell. Microbiol.", "DOI": "", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/11422081", "accessDate": "2011-09-29T01:52:42Z", "PMID": "", "PMCID": "", "ISSN": "1462-5814", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 11422081", "tags": [ { "tag": "Animals", "type": 1 }, { "tag": "Bacterial Toxins", "type": 1 }, { "tag": "Biological Warfare", "type": 1 }, { "tag": "Burkholderia", "type": 1 }, { "tag": "Burkholderia pseudomallei", "type": 1 }, { "tag": "Caenorhabditis elegans", "type": 1 }, { "tag": "Endotoxins", "type": 1 }, { "tag": "Mutation", "type": 1 }, { "tag": "Paralysis", "type": 1 } ], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-09-29T01:52:42Z", "dateModified": "2011-09-29T01:52:42Z" } }, { "key": "2SG537S8", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/2SG537S8", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/2SG537S8", "type": "text/html" } }, "meta": { "createdByUser": { "id": 250761, "username": "npattara", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/npattara", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "2SG537S8", "version": 1, "itemType": "journalArticle", "title": "", "creators": [], "abstractNote": "", "publicationTitle": "", "publisher": "", "place": "", "date": "", "volume": "", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": "", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-09-29T01:49:49Z", "dateModified": "2011-09-29T01:49:49Z" } }, { "key": "D9RPP7Z9", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/D9RPP7Z9", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/D9RPP7Z9", "type": "text/html" } }, "meta": { "createdByUser": { "id": 250761, "username": "npattara", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/npattara", "type": "text/html" } } }, "creatorSummary": "Uccelletti et al.", "parsedDate": "2010-09", "numChildren": 0 }, "data": { "key": "D9RPP7Z9", "version": 1, "itemType": "journalArticle", "title": "Anti-Pseudomonas activity of frog skin antimicrobial peptides in a Caenorhabditis elegans infection model: a plausible mode of action in vitro and in vivo", "creators": [ { "creatorType": "author", "firstName": "Daniela", "lastName": "Uccelletti" }, { "creatorType": "author", "firstName": "Elena", "lastName": "Zanni" }, { "creatorType": "author", "firstName": "Ludovica", "lastName": "Marcellini" }, { "creatorType": "author", "firstName": "Claudio", "lastName": "Palleschi" }, { "creatorType": "author", "firstName": "Donatella", "lastName": "Barra" }, { "creatorType": "author", "firstName": "Maria Luisa", "lastName": "Mangoni" } ], "abstractNote": "The emergence of multidrug-resistant (MDR) microorganisms makes it increasingly difficult to treat infections. These infections include those associated with Pseudomonas aeruginosa, which are hard to eradicate, especially in patients with a compromised immune system. Naturally occurring membrane-active cationic antimicrobial peptides (CAMPs) serve as attractive candidates for the development of new therapeutic agents. Amphibian skin is one of the richest sources for such peptides, but only a few studies on their in vivo activities and modes of action have been reported. We investigated (i) the activity and mechanism underlying the killing of short CAMPs from frog skin (e.g., temporins and esculentin fragments) on an MDR clinical isolate of P. aeruginosa and (ii) their in vivo antibacterial activities and modes of action, using the minihost model of Caenorhabditis elegans. Our data revealed that in vivo, both temporin-1Tb and esculentin(1-18) were highly active in promoting the survival of Pseudomonas-infected nematodes, although temporin-1Tb did not show significant activity in vitro under the experimental conditions used. Importantly, esculentin(1-18) permeated the membrane of Pseudomonas cells within the infected nematode. To the best of our knowledge, this is the first report showing the ability of a CAMP to permeate the microbial membrane within a living organism. Besides shedding light on a plausible mode of action of frog skin CAMPs in vivo, our data suggest that temporins and esculentins would be attractive molecules as templates for the development of new therapeutics against life-threatening infections.", "publicationTitle": "Antimicrobial Agents and Chemotherapy", "publisher": "", "place": "", "date": "Sep 2010", "volume": "54", "issue": "9", "section": "", "partNumber": "", "partTitle": "", "pages": "3853-3860", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Antimicrob. Agents Chemother.", "DOI": "10.1128/AAC.00154-10", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/20606068", "accessDate": "2011-09-29T01:49:04Z", "PMID": "", "PMCID": "", "ISSN": "1098-6596", "archive": "", "archiveLocation": "", "shortTitle": "Anti-Pseudomonas activity of frog skin antimicrobial peptides in a Caenorhabditis elegans infection model", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 20606068", "tags": [ { "tag": "Amphibian Proteins", "type": 1 }, { "tag": "Animals", "type": 1 }, { "tag": "Antimicrobial Cationic Peptides", "type": 1 }, { "tag": "Anura", "type": 1 }, { "tag": "Caenorhabditis elegans", "type": 1 }, { "tag": "Cells, Cultured", "type": 1 }, { "tag": "Glycosides", "type": 1 }, { "tag": "Hemolysis", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Pregnenolone", "type": 1 }, { "tag": "Proteins", "type": 1 }, { "tag": "Pseudomonas Infections", "type": 1 }, { "tag": "Pseudomonas aeruginosa", "type": 1 }, { "tag": "Skin", "type": 1 } ], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-09-29T01:49:04Z", "dateModified": "2011-09-29T01:49:04Z" } }, { "key": "TT5WAZTR", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/TT5WAZTR", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/TT5WAZTR", "type": "text/html" } }, "meta": { "createdByUser": { "id": 698151, "username": "wuddy", "name": "Santi Chanmanee", "links": { "alternate": { "href": "https://www.zotero.org/wuddy", "type": "text/html" } } }, "creatorSummary": "Mouhat et al.", "parsedDate": "2008", "numChildren": 0 }, "data": { "key": "TT5WAZTR", "version": 1, "itemType": "journalArticle", "title": "Animal toxins acting on voltage-gated potassium channels", "creators": [ { "creatorType": "author", "firstName": "Stéphanie", "lastName": "Mouhat" }, { "creatorType": "author", "firstName": "Nicolas", "lastName": "Andreotti" }, { "creatorType": "author", "firstName": "Besma", "lastName": "Jouirou" }, { "creatorType": "author", "firstName": "Jean-Marc", "lastName": "Sabatier" } ], "abstractNote": "Animal venoms are rich natural sources of bioactive compounds, including peptide toxins acting on the various types of ion channels, i.e. K(+), Na(+), Cl(-) and Ca(2+). Among K+ channel-acting toxins, those selective for voltage-gated K(+) (Kv) channels are widely represented and have been isolated from the venoms of numerous animal species, such as scorpions, sea anemones, snakes, marine cone snails and spiders. The toxins characterized hitherto contain between 22 and 60 amino acid residues, and are cross-linked by two to four disulfide bridges. Depending on their types of fold, toxins can be classified in eight structural categories, which showed a combination of beta-strands, helices, or a mixture of both. The main architectural motifs thereof are referred to as alpha/beta scaffold and inhibitor cystine knot (ICK). A detailed analysis of toxin structures and pharmacological selectivities indicates that toxins exhibiting a similar type of fold can exert their action on several subtypes of Kv channels, whereas a particular Kv channel can be targeted by toxins that possess unrelated folds. Therefore, it appears that the ability of structurally divergent toxins to interact with a particular Kv channel relies onto a similar spatial distribution of amino acid residues that are key to the toxin-channel interaction (rather than the type of toxin fold). The diversity of Kv channel blockers and their therapeutic value in the potential treatment of a number of specific human diseases, especially autoimmune disorders, inflammatory neuropathies and cancer, are reviewed.", "publicationTitle": "Current Pharmaceutical Design", "publisher": "", "place": "", "date": "2008", "volume": "14", "issue": "24", "section": "", "partNumber": "", "partTitle": "", "pages": "2503-2518", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Curr. Pharm. Des", "DOI": "", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/18781998", "accessDate": "2011-08-23T15:08:37Z", "PMID": "", "PMCID": "", "ISSN": "1873-4286", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 18781998", "tags": [ { "tag": "Amino Acid Sequence", "type": 1 }, { "tag": "Animals", "type": 1 }, { "tag": "Drug Design", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Models, Molecular", "type": 1 }, { "tag": "Molecular Sequence Data", "type": 1 }, { "tag": "Peptides", "type": 1 }, { "tag": "Potassium Channel Blockers", "type": 1 }, { "tag": "Potassium Channels, Voltage-Gated", "type": 1 }, { "tag": "Protein Conformation", "type": 1 }, { "tag": "Sequence Alignment", "type": 1 }, { "tag": "Venoms", "type": 1 } ], "collections": [ "2FHV34DU" ], "relations": {}, "dateAdded": "2011-08-23T15:08:37Z", "dateModified": "2011-08-23T15:08:37Z" } }, { "key": "VSBDNGAX", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/VSBDNGAX", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/VSBDNGAX", "type": "text/html" } }, "meta": { "createdByUser": { "id": 251914, "username": "ranna", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/ranna", "type": "text/html" } } }, "creatorSummary": "Becke", "parsedDate": "1988", "numChildren": 0 }, "data": { "key": "VSBDNGAX", "version": 1, "itemType": "journalArticle", "title": "Density-functional exchange-energy approximation with correct asymptotic behavior", "creators": [ { "creatorType": "author", "firstName": "A. D", "lastName": "Becke" } ], "abstractNote": "", "publicationTitle": "Physical Review A", "publisher": "", "place": "", "date": "1988", "volume": "38", "issue": "6", "section": "", "partNumber": "", "partTitle": "", "pages": "3098", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Google Scholar", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-08-23T15:03:40Z", "dateModified": "2011-08-23T15:03:40Z" } }, { "key": "AGVHTRGU", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/AGVHTRGU", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/AGVHTRGU", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254842, "username": "onanong", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/onanong", "type": "text/html" } } }, "creatorSummary": "Zhang et al.", "parsedDate": "2011-07-14", "numChildren": 0 }, "data": { "key": "AGVHTRGU", "version": 1, "itemType": "journalArticle", "title": "Vitamin D Status and Expression of Vitamin D Receptor and LL-37 in Patients with Spontaneous Bacterial Peritonitis", "creators": [ { "creatorType": "author", "firstName": "Chong", "lastName": "Zhang" }, { "creatorType": "author", "firstName": "Lianrong", "lastName": "Zhao" }, { "creatorType": "author", "firstName": "Li", "lastName": "Ma" }, { "creatorType": "author", "firstName": "Cheng", "lastName": "Lv" }, { "creatorType": "author", "firstName": "Yang", "lastName": "Ding" }, { "creatorType": "author", "firstName": "Tingting", "lastName": "Xia" }, { "creatorType": "author", "firstName": "Jingyan", "lastName": "Wang" }, { "creatorType": "author", "firstName": "Xiaoguang", "lastName": "Dou" } ], "abstractNote": "BACKGROUND: Vitamin D, which exerts its effect through vitamin D receptor (VDR), and LL-37, a vitamin D-dependent antimicrobial peptide, are involved in many infectious diseases. AIM: The objective of this study was to evaluate whether vitamin D status and expressions of VDR and LL-37 are involved in the pathogenesis of spontaneous bacterial peritonitis (SBP). METHODS: Serum and ascitic fluid 25-dihydroxyvitamin D [25(OH)D] concentrations and levels of VDR and LL-37 in peritoneal leukocytes were measured by ELISA and real-time PCR methods in cirrhotic patients with SBP (n = 19) and cirrhotic patients with simple ascites (n = 28). The correlations between these levels and clinical variables were evaluated. RESULTS: Cirrhotic patients with ascites showed low vitamin D concentrations in both serum and ascitic fluid. Lower serum vitamin D concentrations were observed in cirrhotic patients with Child-Pugh C class. 25(OH)D concentrations in ascitic fluid were positive correlated with that in serum (r = 0.74, P < 0.001). The SBP group showed significantly higher levels of both VDR and LL-37 mRNA expressions in peritoneal leukocytes than the simple ascites group (P = 0.005 and P = 0.003, respectively). In the SBP group, VDR and LL-37 expressions in peritoneal leukocytes were positively correlated (r = 0.70, P = 0.001). CONCLUSIONS: Vitamin D insufficiency was universal among cirrhotic patients with ascites, and the situation was more severe with more serious cirrhosis. Expressions of peritoneal leukocytes VDR and LL-37 genes were simultaneously up-regulated in cirrhotic patients with SBP when compared with cirrhotic patients with simple ascites. It is indicated that the vitamin D-VDR system and its downstream gene, LL-37, are involved in the pathogenesis and antibacterial immune response to SBP.", "publicationTitle": "Digestive Diseases and Sciences", "publisher": "", "place": "", "date": "Jul 14, 2011", "volume": "", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": "", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Dig Dis Sci", "DOI": "10.1007/s10620-011-1824-6", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/21755299", "accessDate": "2011-08-23T07:21:35Z", "PMID": "", "PMCID": "", "ISSN": "1573-2568", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 21755299", "tags": [], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-08-23T07:21:35Z", "dateModified": "2011-08-23T07:21:35Z" } }, { "key": "ZN8SSRAM", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/ZN8SSRAM", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/ZN8SSRAM", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254842, "username": "onanong", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/onanong", "type": "text/html" } } }, "creatorSummary": "Morizane et al.", "parsedDate": "2011-08-18", "numChildren": 0 }, "data": { "key": "ZN8SSRAM", "version": 1, "itemType": "journalArticle", "title": "Cathelicidin Antimicrobial Peptide LL-37 in Psoriasis Enables Keratinocyte Reactivity against TLR9 Ligands", "creators": [ { "creatorType": "author", "firstName": "Shin", "lastName": "Morizane" }, { "creatorType": "author", "firstName": "Kenshi", "lastName": "Yamasaki" }, { "creatorType": "author", "firstName": "Beda", "lastName": "Mühleisen" }, { "creatorType": "author", "firstName": "Paul F", "lastName": "Kotol" }, { "creatorType": "author", "firstName": "Masamoto", "lastName": "Murakami" }, { "creatorType": "author", "firstName": "Yumi", "lastName": "Aoyama" }, { "creatorType": "author", "firstName": "Keiji", "lastName": "Iwatsuki" }, { "creatorType": "author", "firstName": "Tissa", "lastName": "Hata" }, { "creatorType": "author", "firstName": "Richard L", "lastName": "Gallo" } ], "abstractNote": "Here we show that keratinocytes in psoriatic lesional skin express increased Toll-like receptor (TLR) 9 that similarly localizes with elevated expression of the cathelicidin antimicrobial peptide LL-37. In culture, normal human keratinocytes exposed to LL-37 increased TLR9 expression. Furthermore, when keratinocytes were exposed to LL-37 and subsequently treated with TLR9 ligands, such as CpG or genomic DNA, they greatly increased production of type I IFNs. This response mimicked observations in the epidermis of psoriatic lesional skin as keratinocytes in psoriatic lesions produce greater amounts of IFN-β than normal skin lacking LL-37. The mechanism for induction of type I IFNs in keratinocytes was dependent on TLR9 expression but not on a DNA-LL-37 complex. These findings suggest that keratinocytes recognize and respond to DNA and can actively participate in contributing to the immunological environment that characterizes psoriasis.Journal of Investigative Dermatology advance online publication, 18 August 2011; doi:10.1038/jid.2011.259.", "publicationTitle": "The Journal of Investigative Dermatology", "publisher": "", "place": "", "date": "Aug 18, 2011", "volume": "", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": "", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J Invest Dermatol", "DOI": "10.1038/jid.2011.259", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/21850017", "accessDate": "2011-08-23T07:21:35Z", "PMID": "", "PMCID": "", "ISSN": "1523-1747", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 21850017", "tags": [], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-08-23T07:21:35Z", "dateModified": "2011-08-23T07:21:35Z" } }, { "key": "TUPEUP7Q", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/TUPEUP7Q", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/TUPEUP7Q", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254842, "username": "onanong", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/onanong", "type": "text/html" } } }, "creatorSummary": "Kim et al.", "parsedDate": "2011-07-07", "numChildren": 0 }, "data": { "key": "TUPEUP7Q", "version": 1, "itemType": "journalArticle", "title": "LL-37 suppresses sodium nitroprusside-induced apoptosis of systemic sclerosis dermal fibroblasts", "creators": [ { "creatorType": "author", "firstName": "Hee Jung", "lastName": "Kim" }, { "creatorType": "author", "firstName": "Dae Ho", "lastName": "Cho" }, { "creatorType": "author", "firstName": "Kyung Jin", "lastName": "Lee" }, { "creatorType": "author", "firstName": "Chul Soo", "lastName": "Cho" }, { "creatorType": "author", "firstName": "Sa Ik", "lastName": "Bang" }, { "creatorType": "author", "firstName": "Baik Kee", "lastName": "Cho" }, { "creatorType": "author", "firstName": "Hyun Jeong", "lastName": "Park" } ], "abstractNote": "The human cathelicidin antimicrobial peptide LL-37 regulates apoptosis of several cell types. Defective apoptosis of skin fibroblasts may contribute to systemic sclerosis (SSc). Here, we show that LL-37 inhibited apoptosis of SSc fibroblasts and identified the signalling pathways by which LL-37 mediates apoptosis. Immunohistochemistry showed that cathelicidin expression was enhanced in SSc patients compared with healthy controls. In addition, LL-37 decreased sodium nitroprusside (SNP)-induced apoptosis of SSc fibroblasts. LL-37 significantly increased expression of Bcl-2 and decreased levels of BAX protein. Pretreatment with LL-37 decreased activation of caspase-3 following SNP-treatment. Moreover, exposure of SSc fibroblasts to LL-37 resulted in increased expression of COX-2 and stimulation of prostaglandin E(2) (PGE(2) ). Furthermore, LL-37 induced phosphorylation of ERK and the ERK inhibitor PD98059 blocked the inhibitory effect of LL-37 on apoptosis. Our data indicate that LL-37 may be associated with skin sclerosis by inhibiting apoptosis of dermal fibroblasts.", "publicationTitle": "Experimental Dermatology", "publisher": "", "place": "", "date": "Jul 7, 2011", "volume": "", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": "", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Exp Dermatol", "DOI": "10.1111/j.1600-0625.2011.01327.x", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/21732986", "accessDate": "2011-08-23T07:21:35Z", "PMID": "", "PMCID": "", "ISSN": "1600-0625", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 21732986", "tags": [], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-08-23T07:21:35Z", "dateModified": "2011-08-23T07:21:35Z" } }, { "key": "8MVPCMTD", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/8MVPCMTD", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/8MVPCMTD", "type": "text/html" } }, "meta": { "createdByUser": { "id": 251914, "username": "ranna", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/ranna", "type": "text/html" } } }, "creatorSummary": "Voss and Siems", "parsedDate": "2006", "numChildren": 0 }, "data": { "key": "8MVPCMTD", "version": 1, "itemType": "journalArticle", "title": "Clinical oxidation parameters of aging", "creators": [ { "creatorType": "author", "firstName": "Peter", "lastName": "Voss" }, { "creatorType": "author", "firstName": "Werner", "lastName": "Siems" } ], "abstractNote": "", "publicationTitle": "Free Radical Research", "publisher": "", "place": "", "date": "01/2006", "volume": "40", "issue": "12", "section": "", "partNumber": "", "partTitle": "", "pages": "1339-1349", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Free Radic Res", "DOI": "10.1080/10715760600953859", "citationKey": "", "url": "http://informahealthcare.com/doi/abs/10.1080/10715760600953859?journalCode=fra", "accessDate": "2011-08-23T07:20:56Z", "PMID": "", "PMCID": "", "ISSN": "1071-5762", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "CrossRef", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-08-23T07:20:56Z", "dateModified": "2011-08-23T07:20:56Z" } }, { "key": "TVWQMAZH", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/TVWQMAZH", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/TVWQMAZH", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254842, "username": "onanong", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/onanong", "type": "text/html" } } }, "creatorSummary": "Schittek et al.", "parsedDate": "2008-09", "numChildren": 0 }, "data": { "key": "TVWQMAZH", "version": 1, "itemType": "journalArticle", "title": "The role of antimicrobial peptides in human skin and in skin infectious diseases", "creators": [ { "creatorType": "author", "firstName": "Birgit", "lastName": "Schittek" }, { "creatorType": "author", "firstName": "Maren", "lastName": "Paulmann" }, { "creatorType": "author", "firstName": "Ilknur", "lastName": "Senyürek" }, { "creatorType": "author", "firstName": "Heiko", "lastName": "Steffen" } ], "abstractNote": "Antimicrobial peptides or proteins (AMPs) represent an ancient and efficient innate defense mechanism which protects interfaces from infection with pathogenic microorganisms. In human skin AMPs are produced mainly by keratinocytes, neutrophils, sebocytes or sweat glands and are either expressed constitutively or after an inflammatory stimulus. In several human skin diseases there is an inverse correlation between severity of the disease and the level of AMP production. Skin lesions of patients with atopic dermatitis show a diminished expression of the beta-defensins and the cathelicidin LL-37. Furthermore, these patients have a reduced amount of the AMP dermcidin in their sweat which correlates with an impaired innate defense of human skin in vivo. In addition, decreased levels of AMPs are associated with burns and chronic wounds. In contrast, overexpression of AMPs can lead to increased protection against skin infections as seen in patients with psoriasis and rosacea, inflammatory skin-diseases which rarely result in superinfection. In other skin diseases, e.g. in patients with acne vulgaris, increased levels of AMPs are often found in inflamed or infected skin areas indicating a role of these peptides in the protection from infection. These data indicate that AMPs have a therapeutical potential as topical anti-infectives in several skin diseases. The broad spectrum of antimicrobial activity, the low incidence of bacterial resistance and their function as immunomodulatory agents are attractive features of AMPs for their clinical use.", "publicationTitle": "Infectious Disorders Drug Targets", "publisher": "", "place": "", "date": "Sep 2008", "volume": "8", "issue": "3", "section": "", "partNumber": "", "partTitle": "", "pages": "135-143", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Infect Disord Drug Targets", "DOI": "", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/18782030", "accessDate": "2011-08-23T07:20:41Z", "PMID": "", "PMCID": "", "ISSN": "1871-5265", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 18782030", "tags": [ { "tag": "Anti-Infective Agents", "type": 1 }, { "tag": "Antimicrobial Cationic Peptides", "type": 1 }, { "tag": "Drug Resistance", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Immunologic Factors", "type": 1 }, { "tag": "Severity of Illness Index", "type": 1 }, { "tag": "Signal Transduction", "type": 1 }, { "tag": "Skin", "type": 1 }, { "tag": "Skin Diseases, Infectious", "type": 1 } ], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-08-23T07:20:41Z", "dateModified": "2011-08-23T07:20:41Z" } }, { "key": "CPXR8PEK", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/CPXR8PEK", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/CPXR8PEK", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254842, "username": "onanong", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/onanong", "type": "text/html" } } }, "creatorSummary": "Nijnik and Hancock", "parsedDate": "2009-01", "numChildren": 0 }, "data": { "key": "CPXR8PEK", "version": 1, "itemType": "journalArticle", "title": "The roles of cathelicidin LL-37 in immune defences and novel clinical applications", "creators": [ { "creatorType": "author", "firstName": "Anastasia", "lastName": "Nijnik" }, { "creatorType": "author", "firstName": "Robert E W", "lastName": "Hancock" } ], "abstractNote": "PURPOSE OF REVIEW LL-37 is the only member of the cathelicidin family of host defence peptides expressed in humans. It is primarily produced by phagocytic leucocytes and epithelial cells, and mediates a wide range of biological responses: direct killing of microorganisms, chemotaxis and chemokine induction, regulation of inflammatory responses, as well as adjuvant, angiogenic and wound healing effects. In this review we will cover the recent advances in the understanding of LL-37 biology: its activities, the mechanisms of its induction and roles in immune defence. RECENT FINDINGS Recent studies advanced our understanding of the mechanisms controlling LL-37 expression, demonstrating the key involvement of the vitamin D3 and the hypoxia response pathways, and the impacts of commensal and pathogenic microorganisms on its production. The synergistic and antagonistic interactions between LL-37 and other immune mediators have been further elucidated. Furthermore, studies in animal models and human patients further characterized the roles of cathelicidins in immunity, with roles in infectious and inflammatory conditions. The underlying properties of LL-37 have been exploited to create innate defence regulator peptides that represent a novel immunomodulatory approach to treating infections. SUMMARY The understanding of the biological properties and functions of LL-37 and other host defence peptides advances our knowledge of innate immunity, the interactions of the host with pathogens and the microflora, as well as the pathology of infectious and inflammatory diseases, creating many strategies and opportunities for therapeutic intervention.", "publicationTitle": "Current Opinion in Hematology", "publisher": "", "place": "", "date": "Jan 2009", "volume": "16", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "41-47", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Curr. Opin. Hematol", "DOI": "", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/19068548", "accessDate": "2011-08-23T07:20:41Z", "PMID": "", "PMCID": "", "ISSN": "1531-7048", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 19068548", "tags": [ { "tag": "Antimicrobial Cationic Peptides", "type": 1 }, { "tag": "Cathelicidins", "type": 1 }, { "tag": "Drug Design", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Immunity, Innate", "type": 1 }, { "tag": "Transcriptional Activation", "type": 1 } ], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-08-23T07:20:41Z", "dateModified": "2011-08-23T07:20:41Z" } }, { "key": "SQNRUTBI", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/SQNRUTBI", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/SQNRUTBI", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254842, "username": "onanong", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/onanong", "type": "text/html" } } }, "creatorSummary": "Doss et al.", "parsedDate": "2010-01", "numChildren": 0 }, "data": { "key": "SQNRUTBI", "version": 1, "itemType": "journalArticle", "title": "Human defensins and LL-37 in mucosal immunity", "creators": [ { "creatorType": "author", "firstName": "Mona", "lastName": "Doss" }, { "creatorType": "author", "firstName": "Mitchell R", "lastName": "White" }, { "creatorType": "author", "firstName": "Tesfaldet", "lastName": "Tecle" }, { "creatorType": "author", "firstName": "Kevan L", "lastName": "Hartshorn" } ], "abstractNote": "Defensins are widespread in nature and have activity against a broad range of pathogens. Defensins have direct antimicrobial effects and also modulate innate and adaptive immune responses. We consider the role of human defensins and the cathelicidin LL-37 in defense of respiratory, gastrointestinal, and genitourinary tracts and the oral cavity, skin, and eye. Human beta-defensins (hBDs) and human defensins 5 and 6 (HD5 and -6) are involved most obviously in mucosal responses, as they are produced principally by epithelial cells. Human alpha-defensins 1-4 (or HNPs 1-4) are produced principally by neutrophils recruited to the mucosa. Understanding the biology of defensins and LL-37 is the beginning to clarify the pathophysiology of mucosal inflammatory and infectious diseases (e.g., Crohn's disease, atopic dermatitis, lung or urinary infections). Challenges for these studies are the redundancy of innate defense mechanisms and the presence and interactions of many innate defense proteins in mucosal secretions.", "publicationTitle": "Journal of Leukocyte Biology", "publisher": "", "place": "", "date": "Jan 2010", "volume": "87", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "79-92", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Leukoc. Biol", "DOI": "10.1189/jlb.0609382", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/19808939", "accessDate": "2011-08-23T07:20:41Z", "PMID": "", "PMCID": "", "ISSN": "1938-3673", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 19808939", "tags": [ { "tag": "Antimicrobial Cationic Peptides", "type": 1 }, { "tag": "Defensins", "type": 1 }, { "tag": "Eye", "type": 1 }, { "tag": "Gastric Mucosa", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Immunity, Innate", "type": 1 }, { "tag": "Immunity, Mucosal", "type": 1 }, { "tag": "Infection", "type": 1 }, { "tag": "Intestinal Mucosa", "type": 1 }, { "tag": "Mouth Mucosa", "type": 1 }, { "tag": "Organ Specificity", "type": 1 }, { "tag": "Respiratory Mucosa", "type": 1 }, { "tag": "Skin", "type": 1 }, { "tag": "Urogenital System", "type": 1 } ], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-08-23T07:20:41Z", "dateModified": "2011-08-23T07:20:41Z" } }, { "key": "C2UBPFNR", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/C2UBPFNR", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/C2UBPFNR", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254842, "username": "onanong", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/onanong", "type": "text/html" } } }, "creatorSummary": "Burton and Steel", "parsedDate": "2009-12", "numChildren": 0 }, "data": { "key": "C2UBPFNR", "version": 1, "itemType": "journalArticle", "title": "The chemistry and biology of LL-37", "creators": [ { "creatorType": "author", "firstName": "Matthew F", "lastName": "Burton" }, { "creatorType": "author", "firstName": "Patrick G", "lastName": "Steel" } ], "abstractNote": "LL-37 is a human host defence peptide that has a wide range of biological functions, including antimicrobial and immunomodulatory properties. This review summarises how molecular structure influences the balance between the immunomodulatory and antimicrobial functions of LL-37.", "publicationTitle": "Natural Product Reports", "publisher": "", "place": "", "date": "Dec 2009", "volume": "26", "issue": "12", "section": "", "partNumber": "", "partTitle": "", "pages": "1572-1584", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Nat Prod Rep", "DOI": "10.1039/b912533g", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/19936387", "accessDate": "2011-08-23T07:20:41Z", "PMID": "", "PMCID": "", "ISSN": "1460-4752", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 19936387", "tags": [ { "tag": "Amino Acid Sequence", "type": 1 }, { "tag": "Antimicrobial Cationic Peptides", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Molecular Sequence Data", "type": 1 } ], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-08-23T07:20:41Z", "dateModified": "2011-08-23T07:20:41Z" } }, { "key": "KPTUUGPE", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/KPTUUGPE", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/KPTUUGPE", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254842, "username": "onanong", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/onanong", "type": "text/html" } } }, "creatorSummary": "Wu et al.", "parsedDate": "2010-10-15", "numChildren": 0 }, "data": { "key": "KPTUUGPE", "version": 1, "itemType": "journalArticle", "title": "Emerging roles of the host defense peptide LL-37 in human cancer and its potential therapeutic applications", "creators": [ { "creatorType": "author", "firstName": "William K K", "lastName": "Wu" }, { "creatorType": "author", "firstName": "Guangshun", "lastName": "Wang" }, { "creatorType": "author", "firstName": "Seth B", "lastName": "Coffelt" }, { "creatorType": "author", "firstName": "Aline M", "lastName": "Betancourt" }, { "creatorType": "author", "firstName": "Chung W", "lastName": "Lee" }, { "creatorType": "author", "firstName": "Daiming", "lastName": "Fan" }, { "creatorType": "author", "firstName": "Kaichun", "lastName": "Wu" }, { "creatorType": "author", "firstName": "Jun", "lastName": "Yu" }, { "creatorType": "author", "firstName": "Joseph J Y", "lastName": "Sung" }, { "creatorType": "author", "firstName": "Chi H", "lastName": "Cho" } ], "abstractNote": "Human cathelicidin LL-37, a host defense peptide derived from leukocytes and epithelial cells, plays a crucial role in innate and adaptive immunity. Not only does LL-37 eliminate pathogenic microbes directly but also modulates host immune responses. Emerging evidence from tumor biology studies indicates that LL-37 plays a prominent and complex role in carcinogenesis. Although overexpression of LL-37 has been implicated in the development or progression of many human malignancies, including breast, ovarian and lung cancers, LL-37 suppresses tumorigenesis in gastric cancer. These data are beginning to unveil the intricate and contradictory functions of LL-37. The reasons for the tissue-specific function of LL-37 in carcinogenesis remain to be elucidated. Here, we review the relationship between LL-37, its fragments and cancer progression as well as discuss the potential therapeutic implications of targeting this peptide.", "publicationTitle": "International Journal of Cancer. Journal International Du Cancer", "publisher": "", "place": "", "date": "Oct 15, 2010", "volume": "127", "issue": "8", "section": "", "partNumber": "", "partTitle": "", "pages": "1741-1747", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Int. J. Cancer", "DOI": "10.1002/ijc.25489", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/20521250", "accessDate": "2011-08-23T07:05:43Z", "PMID": "", "PMCID": "", "ISSN": "1097-0215", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 20521250", "tags": [ { "tag": "Antimicrobial Cationic Peptides", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Lipopolysaccharides", "type": 1 }, { "tag": "Neoplasms", "type": 1 } ], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-08-23T07:05:43Z", "dateModified": "2011-08-23T07:05:43Z" } }, { "key": "ZN5BRNDU", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/ZN5BRNDU", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/ZN5BRNDU", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254842, "username": "onanong", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/onanong", "type": "text/html" } } }, "creatorSummary": "Bucki et al.", "parsedDate": "2010-02", "numChildren": 0 }, "data": { "key": "ZN5BRNDU", "version": 1, "itemType": "journalArticle", "title": "Cathelicidin LL-37: a multitask antimicrobial peptide", "creators": [ { "creatorType": "author", "firstName": "Robert", "lastName": "Bucki" }, { "creatorType": "author", "firstName": "Katarzyna", "lastName": "Leszczyńska" }, { "creatorType": "author", "firstName": "Andrzej", "lastName": "Namiot" }, { "creatorType": "author", "firstName": "Wojciech", "lastName": "Sokołowski" } ], "abstractNote": "The antimicrobial peptide LL-37 is the only known member of the cathelicidin family of peptides expressed in humans. LL-37 is a multifunctional host defense molecule essential for normal immune responses to infection and tissue injury. LL-37 peptide is a potent killer of different microorganisms with the ability to prevent immunostimulatory effects of bacterial wall molecules such as lipopolysaccharide and can therefore protect against lethal endotoxemia. Additional reported activities of LL-37 include chemoattractant function, inhibition of neutrophil apoptosis, and stimulation of angiogenesis, tissue regeneration, and cytokine release (e.g. IL-8). Cellular production of LL-37 is affected by multiple factors, including bacterial products, host cytokines, availability of oxygen, and sun exposure through the activation of CAP-18 gene expression by vitamin D(3). At infection sites, the function of LL-37 can be inhibited by charge-driven interactions with DNA and F-actin released from dead neutrophils and other cells lysed as the result of inflammation. A better understanding of LL-37's biological properties is necessary for its possible therapeutic application for immunomodulatory purposes as well as in treating bacterial infection.", "publicationTitle": "Archivum Immunologiae Et Therapiae Experimentalis", "publisher": "", "place": "", "date": "Feb 2010", "volume": "58", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "15-25", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Arch. Immunol. Ther. Exp. (Warsz.)", "DOI": "10.1007/s00005-009-0057-2", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/20049649", "accessDate": "2011-08-23T07:05:43Z", "PMID": "", "PMCID": "", "ISSN": "1661-4917", "archive": "", "archiveLocation": "", "shortTitle": "Cathelicidin LL-37", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 20049649", "tags": [ { "tag": "Antimicrobial Cationic Peptides", "type": 1 }, { "tag": "Bacterial Infections", "type": 1 }, { "tag": "Cytoprotection", "type": 1 }, { "tag": "Gene Expression Regulation", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Hypoxia-Inducible Factor 1, alpha Subunit", "type": 1 }, { "tag": "Interleukin-8", "type": 1 }, { "tag": "Lipopolysaccharides", "type": 1 }, { "tag": "Neutrophils", "type": 1 }, { "tag": "Vitamin D", "type": 1 } ], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-08-23T07:05:43Z", "dateModified": "2011-08-23T07:05:43Z" } }, { "key": "T96G4DQ6", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/T96G4DQ6", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/T96G4DQ6", "type": "text/html" } }, "meta": { "createdByUser": { "id": 694614, "username": "Patrasuda", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/patrasuda", "type": "text/html" } } }, "creatorSummary": "Cota-Gomez et al.", "parsedDate": "2011-08-05", "numChildren": 0 }, "data": { "key": "T96G4DQ6", "version": 1, "itemType": "journalArticle", "title": "HIV-1 Tat increases oxidant burden in the lungs of transgenic mice", "creators": [ { "creatorType": "author", "firstName": "Adela", "lastName": "Cota-Gomez" }, { "creatorType": "author", "firstName": "Ariana C", "lastName": "Flores" }, { "creatorType": "author", "firstName": "Xiaofeng", "lastName": "Ling" }, { "creatorType": "author", "firstName": "Marileila", "lastName": "Varella-Garcia" }, { "creatorType": "author", "firstName": "Sonia C", "lastName": "Flores" } ], "abstractNote": "Chronic human immunodeficiency virus infection is associated with higher incidence of pulmonary complications including hypertension, vasculopathy, lymphocytic alveolitis, and interstitial pneumonitis not attributed to either opportunistic infections or presence of the virus. The Tat (transactivator of transcription) protein, a required transactivator for expression of full-length viral genes, is pleiotropic and influences expression of cellular inflammatory genes. Tat-dependent transactivation of cellular genes requires specific mediators, including NF-κB, widely recognized as sensitive to changes in cellular oxidant burden. We hypothesized that overproduction of Tat leads to increased oxidant burden and to alterations in basal inflammatory status as measured by NF-κB activation. We engineered transgenic mouse lines that express Tat (86-amino-acid isoform) in the lung under the control of the surfactant protein C promoter. Tat-transgenic mice exhibit increased pulmonary cellular infiltration, increased nitrotyrosine and carbonyl protein modifications, and increased levels of NF-κB, MnSOD, and thioredoxin-interacting protein. These data indicate that Tat increases oxidant burden and resets the threshold for inflammation, which may increase susceptibility to secondary injuries.", "publicationTitle": "Free Radical Biology & Medicine", "publisher": "", "place": "", "date": "Aug 5, 2011", "volume": "", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": "", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Free Radic Biol Med", "DOI": "10.1016/j.freeradbiomed.2011.07.023", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/21855628", "accessDate": "2011-08-23T07:03:49Z", "PMID": "", "PMCID": "", "ISSN": "1873-4596", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 21855628", "tags": [], "collections": [ "EBWKR6B6" ], "relations": {}, "dateAdded": "2011-08-23T07:03:49Z", "dateModified": "2011-08-23T07:03:49Z" } }, { "key": "VRWFW85A", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/VRWFW85A", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/VRWFW85A", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/18466/items/PDGHHDRR", "type": "application/json" } }, "meta": { "createdByUser": { "id": 255927, "username": "sawinee", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/sawinee", "type": "text/html" } } } }, "data": { "key": "VRWFW85A", "version": 1, "parentItem": "PDGHHDRR", "itemType": "attachment", "linkMode": "linked_url", "title": "Full Text PDF", "accessDate": "2011-08-23T07:03:35Z", "url": "http://jxb.oxfordjournals.org/content/56/416/1685.full.pdf", "note": "", "contentType": "application/pdf", "charset": "", "tags": [], "relations": {}, "dateAdded": "2011-08-23T07:03:35Z", "dateModified": "2011-08-23T07:03:35Z" } }, { "key": "4FAF4XN6", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/4FAF4XN6", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/4FAF4XN6", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/18466/items/PDGHHDRR", "type": "application/json" } }, "meta": { "createdByUser": { "id": 255927, "username": "sawinee", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/sawinee", "type": "text/html" } } } }, "data": { "key": "4FAF4XN6", "version": 1, "parentItem": "PDGHHDRR", "itemType": "attachment", "linkMode": "linked_url", "title": "Snapshot", "accessDate": "2011-08-23T07:03:35Z", "url": "http://jxb.oxfordjournals.org/content/56/416/1685.short", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2011-08-23T07:03:35Z", "dateModified": "2011-08-23T07:03:35Z" } }, { "key": "PDGHHDRR", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/PDGHHDRR", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/PDGHHDRR", "type": "text/html" } }, "meta": { "createdByUser": { "id": 255927, "username": "sawinee", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/sawinee", "type": "text/html" } } }, "creatorSummary": "Yevtushenko et al.", "parsedDate": "2005-06", "numChildren": 2 }, "data": { "key": "PDGHHDRR", "version": 1, "itemType": "journalArticle", "title": "Pathogen-induced expression of a cecropin A-melittin antimicrobial peptide gene confers antifungal resistance in transgenic tobacco", "creators": [ { "creatorType": "author", "firstName": "Dmytro P.", "lastName": "Yevtushenko" }, { "creatorType": "author", "firstName": "Rafael", "lastName": "Romero" }, { "creatorType": "author", "firstName": "Benjamin S.", "lastName": "Forward" }, { "creatorType": "author", "firstName": "Robert E.", "lastName": "Hancock" }, { "creatorType": "author", "firstName": "William W.", "lastName": "Kay" }, { "creatorType": "author", "firstName": "Santosh", "lastName": "Misra" } ], "abstractNote": "Expression of defensive genes from a promoter that is specifically activated in response to pathogen invasion is highly desirable for engineering disease-resistant plants. A plant transformation vector was constructed with transcriptional fusion between the pathogen-responsive win3.12T promoter from poplar and the gene encoding the novel cecropin A-melittin hybrid peptide (CEMA) with strong antimicrobial activity. This promoter–transgene combination was evaluated in transgenic tobacco (Nicotiana tabacum L. cv. Xanthi) for enhanced plant resistance against a highly virulent pathogenic fungus Fusarium solani. Transgene expression in leaves was strongly increased after fungal infection or mechanical wounding, and the accumulation of CEMA transcripts was found to be systemic and positively correlated with the number of transgene insertions. A simple and efficient in vitro regeneration bioassay for preliminary screening of transgenic lines against pathogenic fungi was developed. CEMA had strong antifungal activity in vitro, inhibiting conidia germination at concentrations that were non-toxic to tobacco protoplasts. Most importantly, the expression level of the CEMA peptide in vivo, regulated by the win3.12T promoter, was sufficient to confer resistance against F. solani in transgenic tobacco. The antifungal resistance of plants with high CEMA expression was strong and reproducible. In addition, leaf tissue extracts from transgenic plants significantly reduced the number of fungal colonies arising from germinated conidia. Accumulation of CEMA peptide in transgenic tobacco had no deleterious effect on plant growth and development. This is the first report showing the application of a heterologous pathogen-inducible promoter to direct the expression of an antimicrobial peptide in plants, and the feasibility of this approach to provide disease resistance in tobacco and, possibly, other crops.", "publicationTitle": "Journal of Experimental Botany", "publisher": "", "place": "", "date": "June 2005", "volume": "56", "issue": "416", "section": "", "partNumber": "", "partTitle": "", "pages": "1685 -1695", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1093/jxb/eri165", "citationKey": "", "url": "http://jxb.oxfordjournals.org/content/56/416/1685.abstract", "accessDate": "2011-08-23T07:03:35Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Highwire 2.0", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [ "D7ZSM3ST" ], "relations": {}, "dateAdded": "2011-08-23T07:03:35Z", "dateModified": "2011-08-23T07:03:35Z" } }, { "key": "BUJ2FASN", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/BUJ2FASN", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/BUJ2FASN", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254795, "username": "Supaluk Pasan", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/supaluk_pasan", "type": "text/html" } } }, "creatorSummary": "Olugbile et al.", "parsedDate": "2011-07-29", "numChildren": 0 }, "data": { "key": "BUJ2FASN", "version": 1, "itemType": "journalArticle", "title": "Malaria vaccine candidate: Design of a multivalent subunit α-helical coiled coil poly-epitope", "creators": [ { "creatorType": "author", "firstName": "Sope", "lastName": "Olugbile" }, { "creatorType": "author", "firstName": "Viviane", "lastName": "Villard" }, { "creatorType": "author", "firstName": "Sylvie", "lastName": "Bertholet" }, { "creatorType": "author", "firstName": "Ali", "lastName": "Jafarshad" }, { "creatorType": "author", "firstName": "Caroline", "lastName": "Kulangara" }, { "creatorType": "author", "firstName": "Christian", "lastName": "Roussilhon" }, { "creatorType": "author", "firstName": "Geraldine", "lastName": "Frank" }, { "creatorType": "author", "firstName": "George W", "lastName": "Agak" }, { "creatorType": "author", "firstName": "Ingrid", "lastName": "Felger" }, { "creatorType": "author", "firstName": "Issa", "lastName": "Nebie" }, { "creatorType": "author", "firstName": "Karidia", "lastName": "Konate" }, { "creatorType": "author", "firstName": "Andrey V", "lastName": "Kajava" }, { "creatorType": "author", "firstName": "Peter", "lastName": "Schuck" }, { "creatorType": "author", "firstName": "Pierre", "lastName": "Druilhe" }, { "creatorType": "author", "firstName": "François", "lastName": "Spertini" }, { "creatorType": "author", "firstName": "Giampietro", "lastName": "Corradin" } ], "abstractNote": "A new strategy for the rapid identification of new malaria antigens based on protein structural motifs was previously described. We identified and evaluated the malaria vaccine potential of fragments of several malaria antigens containing α-helical coiled coil protein motifs. By taking advantage of the relatively short size of these structural fragments, we constructed different poly-epitopes in which 3 or 4 of these segments were joined together via a non-immunogenic linker. Only peptides that are targets of human antibodies with anti-parasite in vitro biological activities were incorporated. One of the constructs, P181, was well recognized by sera and peripheral blood mononuclear cells (PBMC) of adults living in malaria-endemic areas. Affinity purified antigen-specific human antibodies and sera from P181-immunized mice recognised native proteins on malaria-infected erythrocytes in both immunofluorescence and western blot assays. In addition, specific antibodies inhibited parasite development in an antibody dependent cellular inhibition (ADCI) assay. Naturally induced antigen-specific human antibodies were at high titers and associated with clinical protection from malaria in longitudinal follow-up studies in Senegal.", "publicationTitle": "Vaccine", "publisher": "", "place": "", "date": "Jul 29, 2011", "volume": "", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": "", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Vaccine", "DOI": "10.1016/j.vaccine.2011.06.122", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/21803099", "accessDate": "2011-08-23T07:03:28Z", "PMID": "", "PMCID": "", "ISSN": "1873-2518", "archive": "", "archiveLocation": "", "shortTitle": "Malaria vaccine candidate", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 21803099", "tags": [], "collections": [ "MX8NGHNN" ], "relations": {}, "dateAdded": "2011-08-23T07:03:28Z", "dateModified": "2011-08-23T07:03:28Z" } }, { "key": "JMZ3Q6FU", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/JMZ3Q6FU", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/JMZ3Q6FU", "type": "text/html" } }, "meta": { "createdByUser": { "id": 254842, "username": "onanong", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/onanong", "type": "text/html" } } }, "creatorSummary": "Méndez-Samperio", "parsedDate": "2010-09", "numChildren": 0 }, "data": { "key": "JMZ3Q6FU", "version": 1, "itemType": "journalArticle", "title": "The human cathelicidin hCAP18/LL-37: a multifunctional peptide involved in mycobacterial infections", "creators": [ { "creatorType": "author", "firstName": "Patricia", "lastName": "Méndez-Samperio" } ], "abstractNote": "Antimicrobial peptides are predominantly small cationic polypeptides that are classified together on the basis of these molecules to directly kill or inhibit the growth of microorganisms including mycobacteria, and to activate mechanisms of cellular and adaptive immunity. Various families of antimicrobial peptides have been identified, including the cathelicidins. The cathelicidin family is characterised by a conserved N-terminal cathelin domain and a variable C-terminal antimicrobial domain that can be released from the precursor protein after cleavage by proteinases. LL-37 is the C-terminal part of the only human cathelicidin identified to date called human cationic antimicrobial protein (hCAP18), which is mainly expressed by neutrophils and epithelial cells. The cathelicidin hCAP18/LL-37 is a multifunctional molecule that may mediate various host responses, including bactericidal action, chemotaxis, epithelial cell activation, angiogenesis, epithelial wound repair and activation of chemokine secretion. The antimicrobial peptide LL-37 is produced from human cells during infection of mycobacteria and exerts a microbicidal effect. The discussion will (1) describe recent work on the antimicrobial and immunomodulatory functions of the cathelicidin hCAP18/LL-37, (2) highlight the effectiveness of the cathelicidin hCAP18/LL-37 as a potent component in antimycobacterial immune responses and (3) summarise current progress in the understanding of the therapeutic application of hCAP18/LL-37 and its derivates antimicrobial peptides in mycobacterial infection.", "publicationTitle": "Peptides", "publisher": "", "place": "", "date": "Sep 2010", "volume": "31", "issue": "9", "section": "", "partNumber": "", "partTitle": "", "pages": "1791-1798", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Peptides", "DOI": "10.1016/j.peptides.2010.06.016", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/20600427", "accessDate": "2011-08-23T07:02:54Z", "PMID": "", "PMCID": "", "ISSN": "1873-5169", "archive": "", "archiveLocation": "", "shortTitle": "The human cathelicidin hCAP18/LL-37", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 20600427", "tags": [ { "tag": "Animals", "type": 1 }, { "tag": "Anti-Bacterial Agents", "type": 1 }, { "tag": "Cathelicidins", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Immunity, Innate", "type": 1 }, { "tag": "Immunologic Factors", "type": 1 }, { "tag": "Mycobacterium", "type": 1 }, { "tag": "Mycobacterium Infections", "type": 1 }, { "tag": "Peptide Fragments", "type": 1 } ], "collections": [ "FPE9T7MB" ], "relations": {}, "dateAdded": "2011-08-23T07:02:54Z", "dateModified": "2011-08-23T07:02:54Z" } }, { "key": "DQXM7TUV", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/DQXM7TUV", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/DQXM7TUV", "type": "text/html" } }, "meta": { "createdByUser": { "id": 250761, "username": "npattara", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/npattara", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "DQXM7TUV", "version": 1, "itemType": "webpage", "title": "Zotero | People > Bhorntip > Library > Induction and release of bud dormancy in woody perennials: a science comes of age", "creators": [], "abstractNote": "", "websiteTitle": "", "websiteType": "", "date": "", "publisher": "", "place": "", "DOI": "", "citationKey": "", "url": "http://www.zotero.org/bhorntip/items/133653172", "accessDate": "2010-06-19T08:08:33Z", "shortTitle": "", "language": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2010-06-19T08:08:33Z", "dateModified": "2010-06-19T08:08:33Z" } }, { "key": "MPF9VD4Z", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": 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"DOI": "", "citationKey": "", "url": "http://www.zotero.org/bhorntip/items/133654012", "accessDate": "2010-06-19T08:08:29Z", "shortTitle": "", "language": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2010-06-19T08:08:29Z", "dateModified": "2010-06-19T08:08:29Z" } }, { "key": "6NHPM94B", "version": 1, "library": { "type": "group", "id": 18466, "name": "Rina Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/rina_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/18466/items/6NHPM94B", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/rina_lab/items/6NHPM94B", "type": "text/html" } }, "meta": { "createdByUser": { "id": 250761, "username": "npattara", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/npattara", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "6NHPM94B", "version": 1, "itemType": "webpage", "title": "Zotero | People > Bhorntip > Library > Budbreak with garlic preparations: Effects of garlic preparations and of calcium and hydrogen cyanamides on budbreak of grapevines grown in greenhouses", "creators": [], "abstractNote": "", "websiteTitle": "", "websiteType": "", "date": "", "publisher": "", "place": "", "DOI": "", "citationKey": "", "url": "http://www.zotero.org/bhorntip/items/133654444", "accessDate": "2010-06-19T08:08:16Z", "shortTitle": "", "language": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2010-06-19T08:08:16Z", "dateModified": "2010-06-19T08:08:16Z" } } ]