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"creatorType": "author", "firstName": "Robbin D.", "lastName": "Eppinga" }, { "creatorType": "author", "firstName": "Yan", "lastName": "Li" }, { "creatorType": "author", "firstName": "Jenny L.-C.", "lastName": "Lin" }, { "creatorType": "author", "firstName": "Jim J.-C.", "lastName": "Lin" } ], "abstractNote": "The contractile ring and the cell cortex generate force to divide the cell while maintaining symmetrical shape. This requires temporal and spatial regulation of the actin cytoskeleton at these areas. We force-expressed misregulated versions of actin-binding proteins, tropomyosin and caldesmon, into cells and analyzed their effects on cell division. Cells expressing proteins that increase actomyosin ATPase, such as human tropomyosin chimera (hTM5/3), significantly speed up division, whereas cells expressing proteins that inhibit actomyosin, such as caldesmon mutants defective in Ca2+/calmodulin binding (CaD39-AB) and in cdk1 phosphorylation sites (CaD39-6F), divide slowly. hTM5 and hTM5/3-expressing cells lift one daughter cell off the substrate and twist. Furthermore, CaD39-AB- and CaD39-6F-expressing cells are sensitive to hypotonic swelling and show severe blebbing during division, whereas hTM5/3-expressing cells are resistant to hypotonic swelling and produce membrane bulges. These results support a model where Ca2+/calmodulin and cdk1 dynamically control caldesmon inhibition of tropomyosin-activated actomyosin to regulate division speed and to suppress membrane blebs.", "publicationTitle": "Archives of Biochemistry and Biophysics", "publisher": "", "place": "", "date": "December 15, 2006", "volume": "456", "issue": "2", "section": "", "partNumber": "", "partTitle": "", "pages": "161-174", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Archives of Biochemistry and Biophysics", "DOI": "10.1016/j.abb.2006.06.015", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S0003986106002268", "accessDate": "2013-02-27T01:32:04Z", "PMID": "", "PMCID": "", "ISSN": "0003-9861", "archive": "", "archiveLocation": "", "shortTitle": "Highlight Issue on Contractile Proteins", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Ca2+/calmodulin", "type": 1 }, { "tag": "Cell cortex", "type": 1 }, { "tag": "Contractile ring", "type": 1 }, { "tag": "Cytokinesis", "type": 1 }, { "tag": "Membrane bleb", "type": 1 }, { "tag": "Membrane bulge", "type": 1 }, { "tag": "cdk1/cdc2", "type": 1 }, { "tag": "p21-Activated kinase", "type": 1 } ], "collections": [ "QVA8NHM5" ], "relations": {}, "dateAdded": "2013-02-27T01:46:17Z", "dateModified": "2013-02-27T01:46:17Z" } }, { "key": "SZGTSBCA", "version": 3, "library": { "type": "group", "id": 151271, "name": "MolecBioPaper", "links": { "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/151271/items/SZGTSBCA", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper/items/SZGTSBCA", "type": "text/html" } }, "meta": { "createdByUser": { "id": 1291166, "username": "rpg3jb", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/rpg3jb", "type": "text/html" } } }, "creatorSummary": "Zhu et al.", "parsedDate": "2007-05-11", "numChildren": 1 }, "data": { "key": "SZGTSBCA", "version": 3, "itemType": "journalArticle", "title": "MicroRNA-21 targets the tumor suppressor gene tropomyosin 1 (TPM1)", "creators": [ { "creatorType": "author", "firstName": "Shuomin", "lastName": "Zhu" }, { "creatorType": "author", "firstName": "Min-Liang", "lastName": "Si" }, { "creatorType": "author", "firstName": "Hailong", "lastName": "Wu" }, { "creatorType": "author", "firstName": "Yin-Yuan", "lastName": "Mo" } ], "abstractNote": "MicroRNAs are small noncoding RNA molecules that control expression of target genes. Our previous studies show that mir-21 is overexpressed in tumor tissues compared with the matched normal tissues. Moreover, suppression of mir-21 by antisense oligonucleotides inhibits tumor cell growth both in vitro and in vivo. However, it remains largely unclear as to how mir-21 affects tumor growth, because our understanding of mir-21 targets is limited. In this study, we performed two-dimensional differentiation in-gel electrophoresis of tumors treated with anti-mir-21 and identified the tumor suppressor tropomyosin 1 (TPM1) as a potential mir-21 target. In agreement with this, there is a putative mir-21 binding site at the 3'-untranslated region (3'-UTR) of TPM1 variants V1 and V5. Thus, we cloned the 3'-UTR of TPM1 into a luciferase reporter and found that although mir-21 down-regulated the luciferase activity, anti-mir-21 up-regulated it. Moreover, deletion of the mir-21 binding site abolished the effect of mir-21 on the luciferase activity, suggesting that this mir-21 binding site is critical. Western blot with the cloned TPM1-V1 plus the 3'-UTR indicated that TPM1 protein level was also regulated by mir-21, whereas real-time quantitative reverse transcription-PCR revealed no difference at the mRNA level, suggesting translational regulation. Finally, overexpression of TPM1 in breast cancer MCF-7 cells suppressed anchorage-independent growth. Thus, down-regulation of TPM1 by mir-21 may explain, at least in part, why suppression of mir-21 can inhibit tumor growth, further supporting the notion that mir-21 functions as an oncogene.", "publicationTitle": "The Journal of biological chemistry", "publisher": "", "place": "", "date": "May 11, 2007", "volume": "282", "issue": "19", "section": "", "partNumber": "", "partTitle": "", "pages": "14328-14336", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Biol. Chem.", "DOI": "10.1074/jbc.M611393200", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0021-9258", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 17363372", "tags": [ { "tag": "3' Untranslated Regions", "type": 1 }, { "tag": "Animals", "type": 1 }, { "tag": "Breast Neoplasms", "type": 1 }, { "tag": "Cell Adhesion", "type": 1 }, { "tag": "Cell Line, Tumor", "type": 1 }, { "tag": "Cell Proliferation", "type": 1 }, { "tag": "Female", "type": 1 }, { "tag": "Gene Expression Regulation, Neoplastic", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Luciferases", "type": 1 }, { "tag": "Mice", "type": 1 }, { "tag": "Mice, Nude", "type": 1 }, { "tag": "MicroRNAs", "type": 1 }, { "tag": "Oligonucleotides, Antisense", "type": 1 }, { "tag": "RNA Processing, Post-Transcriptional", "type": 1 }, { "tag": "RNA, Messenger", "type": 1 }, { "tag": "Tumor Stem Cell Assay", "type": 1 }, { "tag": "tropomyosin", "type": 1 } ], "collections": [ "QVA8NHM5" ], "relations": {}, "dateAdded": "2013-02-27T01:46:17Z", "dateModified": "2013-02-27T01:46:17Z" } }, { "key": "VQNWCFAD", "version": 3, "library": { "type": "group", "id": 151271, "name": "MolecBioPaper", "links": { "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/151271/items/VQNWCFAD", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper/items/VQNWCFAD", "type": "text/html" } }, "meta": { "createdByUser": { "id": 1291166, "username": "rpg3jb", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/rpg3jb", "type": "text/html" } } }, "creatorSummary": "MacDonald et al.", "parsedDate": "2001-07-06", "numChildren": 2 }, "data": { "key": "VQNWCFAD", "version": 3, "itemType": "journalArticle", "title": "Endostatin Binds Tropomyosin A POTENTIAL MODULATOR OF THE ANTITUMOR ACTIVITY OF ENDOSTATIN", "creators": [ { "creatorType": "author", "firstName": "Nicholas J.", "lastName": "MacDonald" }, { "creatorType": "author", "firstName": "Wanda Y.", "lastName": "Shivers" }, { "creatorType": "author", "firstName": "David L.", "lastName": "Narum" }, { "creatorType": "author", "firstName": "Stacy M.", "lastName": "Plum" }, { "creatorType": "author", "firstName": "Jennifer N.", "lastName": "Wingard" }, { "creatorType": "author", "firstName": "Steven R.", "lastName": "Fuhrmann" }, { "creatorType": "author", "firstName": "Hong", "lastName": "Liang" }, { "creatorType": "author", "firstName": "Janel", "lastName": "Holland-Linn" }, { "creatorType": "author", "firstName": "D. H. Tom", "lastName": "Chen" }, { "creatorType": "author", "firstName": "B. Kim Lee", "lastName": "Sim" } ], "abstractNote": "The mechanism of action of Endostatin, an endogenous inhibitor of angiogenesis and tumor growth, remains unknown. We utilized phage-display technology to identify polypeptides that mimic the binding domains of proteins with which Endostatin interacts. A conformed peptide (E37) was identified that shares an epitope with human tropomyosin implicating tropomyosin as an Endostatin-binding protein. We show that recombinant human Endostatin binds tropomyosin in vitro and to tropomyosin-associated microfilaments in a variety of endothelial cell types. The most compelling evidence that tropomyosin modulates the activity of Endostatin was demonstrated when E37 blocked greater than 84% of the tumor-growth inhibitory activity of Endostatin in the B16-BL6 metastatic melanoma model. We conclude that the E37 peptide mimics the Endostatin-binding epitope of tropomyosin and blocks the antitumor activity of Endostatin by competing for Endostatin binding. We postulate that the Endostatin interaction with tropomyosin results in disruption of microfilament integrity leading to inhibition of cell motility, induction of apoptosis, and ultimately inhibition of tumor growth.", "publicationTitle": "Journal of Biological Chemistry", "publisher": "", "place": "", "date": "07/06/2001", "volume": "276", "issue": "27", "section": "", "partNumber": "", "partTitle": "", "pages": "25190-25196", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Biol. Chem.", "DOI": "10.1074/jbc.M100743200", "citationKey": "", "url": "http://www.jbc.org.proxy.its.virginia.edu/content/276/27/25190", "accessDate": "2013-02-23T18:35:44Z", "PMID": "", "PMCID": "", "ISSN": "0021-9258, 1083-351X", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "en", "libraryCatalog": "www.jbc.org.proxy.its.virginia.edu", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [ "QVA8NHM5" ], "relations": {}, "dateAdded": "2013-02-27T01:46:17Z", "dateModified": "2013-02-27T01:46:17Z" } }, { "key": "G22MMDX7", "version": 3, "library": { "type": "group", "id": 151271, "name": "MolecBioPaper", "links": { "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/151271/items/G22MMDX7", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper/items/G22MMDX7", "type": "text/html" }, "up": { "href": 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"contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2013-02-27T01:46:17Z", "dateModified": "2013-02-27T01:46:17Z" } }, { "key": "CEKDKHFG", "version": 3, "library": { "type": "group", "id": 151271, "name": "MolecBioPaper", "links": { "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/151271/items/CEKDKHFG", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper/items/CEKDKHFG", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/151271/items/C9ZH2HNS", "type": "application/json" } }, "meta": { "createdByUser": { "id": 1291166, "username": "rpg3jb", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/rpg3jb", "type": "text/html" } } } }, "data": { "key": "CEKDKHFG", "version": 3, "parentItem": "C9ZH2HNS", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Link", "accessDate": "2013-02-27T01:17:05Z", "url": "http://www.ncbi.nlm.nih.gov/pubmed/17008534", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2013-02-27T01:46:17Z", "dateModified": "2013-02-27T01:46:17Z" } }, { "key": "DRTPNDIM", "version": 3, "library": { "type": "group", "id": 151271, "name": "MolecBioPaper", "links": { "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/151271/items/DRTPNDIM", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper/items/DRTPNDIM", "type": "text/html" } }, "meta": { "createdByUser": { "id": 1291166, "username": "rpg3jb", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/rpg3jb", "type": "text/html" } } }, "creatorSummary": "Ebert et al.", "parsedDate": "2006-11", "numChildren": 2 }, "data": { "key": "DRTPNDIM", "version": 3, "itemType": "journalArticle", "title": "Autoantibodies against human tropomyosin isoform 5 in ulcerative colitis destroys colonic epithelial cells through antibody and complement-mediated lysis", "creators": [ { "creatorType": "author", "firstName": "Ellen C.", "lastName": "Ebert" }, { "creatorType": "author", "firstName": "Xin", "lastName": "Geng" }, { "creatorType": "author", "firstName": "Jim", "lastName": "Lin" }, { "creatorType": "author", "firstName": "Kiron M.", "lastName": "Das" } ], "abstractNote": "Introduction. Patients with ulcerative colitis (UC) have IgG1 antibodies in serum and colon against human tropomyosin isoform 5 (hTM5), a cytoskeletal microfilament protein found intracellularly and on the surface of colonic epithelial cells (EC). These antibodies may be pathogenic in UC. Methods. Sera from patients with UC (n = 110) or Crohn’s disease (CD) (n = 50) and from healthy individuals (Hl) (n = 30) were preincubated with recombinant hTM5 or bovine serum albumin (BSA), then cultured for 4 h with 51Cr-labelled colonic adenocarcinoma cells (LS180). Cytotoxicity was determined by 51Cr release assay. Results. All serum samples lysed up to 36% of LS180 cells regardless of the source of the serum. However, adding hTM5 to UC, but not to CD or HI, sera reduced cytotoxicity by up to 75%. This hTM5-induced inhibition of cytotoxicity was found especially with sera from UC patients with active disease, and was found even after total colectomy. The hTM5-induced inhibition was mediated by purified IgG from UC sera. Complement was involved since hTM5-induced inhibition of cytotoxicity declined with either heat inactivation of the sera or premixing sera with Fc fragments. Conclusions. This study shows that hTM5-specific IgG autoantibodies present in UC sera destroy LS180 cells by antibody and complement-mediated lysis. Such a phenomenon was not seen in CD or HI. This suggests an autoantigenic role of hTM5 and anti-hTM5 antibodies in the pathogenesis of UC. This observation may lead to novel diagnostic and therapeutic possibilities.", "publicationTitle": "Cellular Immunology", "publisher": "", "place": "", "date": "November 2006", "volume": "244", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "43-49", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Cellular Immunology", "DOI": "10.1016/j.cellimm.2007.02.004", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S0008874907000214", "accessDate": "2013-02-27T01:34:17Z", "PMID": "", "PMCID": "", "ISSN": "0008-8749", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Antibodies", "type": 1 }, { "tag": "Inflammatory bowel disease", "type": 1 }, { "tag": "Ulcerative colitis", "type": 1 }, { "tag": "tropomyosin", "type": 1 } ], "collections": [ "QVA8NHM5" ], "relations": {}, "dateAdded": "2013-02-27T01:46:17Z", "dateModified": "2013-02-27T01:46:17Z" } }, { "key": "NZFWQBHH", "version": 3, "library": { "type": "group", "id": 151271, "name": "MolecBioPaper", "links": { "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/151271/items/NZFWQBHH", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper/items/NZFWQBHH", "type": "text/html" } }, "meta": { "createdByUser": { "id": 1291166, "username": "rpg3jb", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/rpg3jb", "type": "text/html" } } }, "creatorSummary": "Schevzov et al.", "parsedDate": "2005-05", "numChildren": 1 }, "data": { "key": "NZFWQBHH", "version": 3, "itemType": "journalArticle", "title": "Tissue-specific tropomyosin isoform composition", "creators": [ { "creatorType": "author", "firstName": "Galina", "lastName": "Schevzov" }, { "creatorType": "author", "firstName": "Bernadette", "lastName": "Vrhovski" }, { "creatorType": "author", "firstName": "Nicole S", "lastName": "Bryce" }, { "creatorType": "author", "firstName": "Sarah", "lastName": "Elmir" }, { "creatorType": "author", "firstName": "Min Ru", "lastName": "Qiu" }, { "creatorType": "author", "firstName": "Geraldine M", "lastName": "O'neill" }, { "creatorType": "author", "firstName": "Nan", "lastName": "Yang" }, { "creatorType": "author", "firstName": "Nicole M", "lastName": "Verrills" }, { "creatorType": "author", "firstName": "Maria", "lastName": "Kavallaris" }, { "creatorType": "author", "firstName": "Peter W", "lastName": "Gunning" } ], "abstractNote": "Four distinct genes encode tropomyosin (Tm) proteins, integral components of the actin microfilament system. In non-muscle cells, over 40 Tm isoforms are derived using alternative splicing. Distinct populations of actin filaments characterized by the composition of these Tm isoforms are found differentially sorted within cells (Gunning et al. 1998b). We hypothesized that these distinct intracellular compartments defined by the association of Tm isoforms may allow for independent regulation of microfilament function. Consequently, to understand the molecular mechanisms that give rise to these different microfilaments and their regulation, a cohort of fully characterized isoform-specific Tm antibodies was required. The characterization protocol initially involved testing the specificity of the antibodies on bacterially produced Tm proteins. We then confirmed that these Tm antibodies can be used to probe the expression and subcellular localization of different Tm isoforms by Western blot analysis, immunofluorescence staining of cells in culture, and immunohistochemistry of paraffin wax-embedded mouse tissues. These Tm antibodies, therefore, have the capacity to monitor specific actin filament populations in a range of experimental systems.", "publicationTitle": "The journal of histochemistry and cytochemistry: official journal of the Histochemistry Society", "publisher": "", "place": "", "date": "May 2005", "volume": "53", "issue": "5", "section": "", "partNumber": "", "partTitle": "", "pages": "557-570", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Histochem. Cytochem.", "DOI": "10.1369/jhc.4A6505.2005", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0022-1554", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 15872049", "tags": [ { "tag": "Actins", "type": 1 }, { "tag": "Animals", "type": 1 }, { "tag": "Antibodies", "type": 1 }, { "tag": "Blotting, Western", "type": 1 }, { "tag": "Cells, Cultured", "type": 1 }, { "tag": "Electrophoresis, Gel, Two-Dimensional", "type": 1 }, { "tag": "Embryo, Mammalian", "type": 1 }, { "tag": "Fibroblasts", "type": 1 }, { "tag": "Immunohistochemistry", "type": 1 }, { "tag": "Mice", "type": 1 }, { "tag": "Organ Specificity", "type": 1 }, { "tag": "Protein Isoforms", "type": 1 }, { "tag": "Rabbits", "type": 1 }, { "tag": "Sheep", "type": 1 }, { "tag": "Spleen", "type": 1 }, { "tag": "tropomyosin", "type": 1 } ], "collections": [ "QVA8NHM5" ], "relations": {}, "dateAdded": "2013-02-27T01:46:17Z", "dateModified": "2013-02-27T01:46:17Z" } }, { "key": "78BJ93MS", "version": 3, "library": { "type": "group", "id": 151271, "name": "MolecBioPaper", "links": { "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/151271/items/78BJ93MS", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/molecbiopaper/items/78BJ93MS", "type": "text/html" } }, "meta": { "createdByUser": { "id": 1291166, "username": "rpg3jb", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/rpg3jb", "type": "text/html" } } }, "creatorSummary": "Bryce et al.", "parsedDate": "2003-03", "numChildren": 1 }, "data": { "key": "78BJ93MS", "version": 3, "itemType": "journalArticle", "title": "Specification of actin filament function and molecular composition by tropomyosin isoforms", "creators": [ { "creatorType": "author", "firstName": "Nicole S", "lastName": "Bryce" }, { "creatorType": "author", "firstName": "Galina", "lastName": "Schevzov" }, { "creatorType": "author", "firstName": "Vicki", "lastName": "Ferguson" }, { "creatorType": "author", "firstName": "Justin M", "lastName": "Percival" }, { "creatorType": "author", "firstName": "Jim J-C", "lastName": "Lin" }, { "creatorType": "author", "firstName": "Fumio", "lastName": "Matsumura" }, { "creatorType": "author", "firstName": "James R", "lastName": "Bamburg" }, { "creatorType": "author", "firstName": "Peter L", "lastName": "Jeffrey" }, { "creatorType": "author", "firstName": "Edna C", "lastName": "Hardeman" }, { "creatorType": "author", "firstName": "Peter", "lastName": "Gunning" }, { "creatorType": "author", "firstName": "Ron P", "lastName": "Weinberger" } ], "abstractNote": "The specific functions of greater than 40 vertebrate nonmuscle tropomyosins (Tms) are poorly understood. In this article we have tested the ability of two Tm isoforms, TmBr3 and the human homologue of Tm5 (hTM5(NM1)), to regulate actin filament function. We found that these Tms can differentially alter actin filament organization, cell size, and shape. hTm5(NM1) was able to recruit myosin II into stress fibers, which resulted in decreased lamellipodia and cellular migration. In contrast, TmBr3 transfection induced lamellipodial formation, increased cellular migration, and reduced stress fibers. Based on coimmunoprecipitation and colocalization studies, TmBr3 appeared to be associated with actin-depolymerizing factor/cofilin (ADF)-bound actin filaments. Additionally, the Tms can specifically regulate the incorporation of other Tms into actin filaments, suggesting that selective dimerization may also be involved in the control of actin filament organization. We conclude that Tm isoforms can be used to specify the functional properties and molecular composition of actin filaments and that spatial segregation of isoforms may lead to localized specialization of actin filament function.", "publicationTitle": "Molecular biology of the cell", "publisher": "", "place": "", "date": "Mar 2003", "volume": "14", "issue": "3", "section": "", "partNumber": "", "partTitle": "", "pages": "1002-1016", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Mol. Biol. Cell", "DOI": "10.1091/mbc.E02-04-0244", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "1059-1524", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 12631719", "tags": [ { "tag": "Actins", "type": 1 }, { "tag": "Animals", "type": 1 }, { "tag": "Cell Line", "type": 1 }, { "tag": "Cell Movement", "type": 1 }, { "tag": "Cell Size", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Mice", "type": 1 }, { "tag": "Mice, Transgenic", "type": 1 }, { "tag": "Myosin Type II", "type": 1 }, { "tag": "Neurons", "type": 1 }, { "tag": "Protein Isoforms", "type": 1 }, { "tag": "Pseudopodia", "type": 1 }, { "tag": "Rats", "type": 1 }, { "tag": "Stress Fibers", "type": 1 }, { "tag": "tropomyosin", "type": 1 } ], "collections": [ "QVA8NHM5" ], "relations": {}, "dateAdded": "2013-02-27T01:46:17Z", "dateModified": "2013-02-27T01:46:17Z" } } ]