{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,13]],"date-time":"2026-03-13T15:10:29Z","timestamp":1773414629806,"version":"3.50.1"},"reference-count":100,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[1998,2,1]],"date-time":"1998-02-01T00:00:00Z","timestamp":886291200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Current Opinion in Cell Biology"],"published-print":{"date-parts":[[1998,2]]},"DOI":"10.1016\/s0955-0674(98)80083-5","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T10:32:55Z","timestamp":1027593175000},"page":"23-34","source":"Crossref","is-referenced-by-count":110,"title":["The modular structure of actin-regulatory proteins"],"prefix":"10.1016","volume":"10","author":[{"given":"Yoram A","family":"Puius","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nicole M","family":"Mahoney","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Steven C","family":"Almo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S0955-0674(98)80083-5_BIB1","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0955-0674(97)80152-4","article-title":"Actin dynamics in vivo","volume":"9","author":"Welch","year":"1997","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB2","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/0955-0674(95)80041-7","article-title":"New horizons for cytokinesis","volume":"7","author":"Fishkind","year":"1995","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB3","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/S0955-0674(97)80155-X","article-title":"Molecular interactions in cell adhesion complexes","volume":"9","author":"Yamada","year":"1997","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB4","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/S0962-8924(97)01127-6","article-title":"Focal adhesion assembly","volume":"7","author":"Burridge","year":"1997","journal-title":"Trends Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB5","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/S0955-0674(97)80159-7","article-title":"mRNA and cytoskeletal filaments","volume":"9","author":"Bassell","year":"1997","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB6","first-page":"169","article-title":"Elongation factor 1\u03b1, translation and the cytoskeleton","volume":"20","author":"Condeelis","year":"1997","journal-title":"Trends Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB7","doi-asserted-by":"crossref","first-page":"2855","DOI":"10.1002\/j.1460-2075.1993.tb05947.x","article-title":"Actin and fimbrin are required for the internalization step of endocytosis in yeast","volume":"12","author":"Kubler","year":"1993","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB8","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/0955-0674(95)80048-4","article-title":"Actin- and microtubule-dependent organelle motors: interrelationships between the two mobility systems","volume":"7","author":"Langford","year":"1995","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB9","first-page":"82","article-title":"Modular organization of actin cross-linking proteins","volume":"16","author":"Matsudaira","year":"1991","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB10","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1006\/scel.1994.1021","article-title":"Actin cross-linking proteins at the leading edge","volume":"5","author":"Matsudaira","year":"1994","journal-title":"Sem Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB11","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1146\/annurev.bi.55.070186.005011","article-title":"Actin and actin-binding proteins. A critical analysis of mechanisms and functions","volume":"55","author":"Pollard","year":"1986","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB12","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1002\/cm.970100116","article-title":"The organization and regulation of the macrophage actin cytoskeleton","volume":"10","author":"Hartwig","year":"1988","journal-title":"Cell Motil Cytoskeleton"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB13","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.1083\/jcb.110.6.2013","article-title":"Bundling of actin filaments by \u03b1-actinin depends on its molecular length","volume":"110","author":"Meyer","year":"1990","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB14_1","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1038\/nsb0997-708","article-title":"The structure of an actin-cross-linking domain from human fimbrin","volume":"4","author":"Goldsmith","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB15","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/0014-5793(95)01098-Y","article-title":"Does Vav bind to F-actin through a CH domain?","volume":"374","author":"Castresana","year":"1995","journal-title":"FEBS Lett"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB16","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1038\/301209a0","article-title":"Role of fimbrin and villin in determining the interfilament distances of actin bundles","volume":"301","author":"Matsudaira","year":"1983","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB17","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1038\/287291a0","article-title":"Actin in the inner ear: the remarkable structure of the stereocilium","volume":"287","author":"DeRosier","year":"1980","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB18","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1101\/SQB.1982.046.01.049","article-title":"How actin filaments pack into bundles","volume":"46","author":"DeRosier","year":"1982","journal-title":"Cold Spring Harb Symp Quant Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB19","doi-asserted-by":"crossref","first-page":"2027","DOI":"10.1126\/science.8266097","article-title":"Crystal Structure of the repetitive segments of spectrin","volume":"262","author":"Yan","year":"1993","journal-title":"Science"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB20_1","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1006\/jmbi.1997.1344","article-title":"Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil","volume":"273","author":"Pascual","year":"1997","journal-title":"J Mol Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB21_1","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1038\/nsb0397-223","article-title":"The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold","volume":"4","author":"Fucini","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB22","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1083\/jcb.111.3.1069","article-title":"Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation protein","volume":"111","author":"De Arruda","year":"1980","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB23","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1083\/jcb.94.2.466","article-title":"A calcium- and pH-regulated protein from Dictyostelium discoideum that cross-links actin filaments","volume":"94","author":"Condeelis","year":"1982","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB24","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1083\/jcb.121.3.599","article-title":"The Ca2+-binding domains in non-muscle type \u03b1-actinin: biochemical and genetic analysis","volume":"121","author":"Witke","year":"1993","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB25_1","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1083\/jcb.139.2.387","article-title":"Evidence for a conformational change in actin induced by fimbrin (N375) binding","volume":"139","author":"Hanein","year":"1997","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB26","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1083\/jcb.126.2.433","article-title":"Determination of the alpha-actinin binding site on actin by cryo-electron microscopy and image analysis","volume":"126","author":"McGough","year":"1994","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB27","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1083\/jcb.119.4.835","article-title":"Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: implications for the requirements of severing and capping","volume":"119","author":"Way","year":"1992","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB28","doi-asserted-by":"crossref","first-page":"15943","DOI":"10.1016\/S0021-9258(19)49625-7","article-title":"Mapping of the functional domains in the amino-terminal region of calponin","volume":"267","author":"Mezgueldi","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB29_1","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1038\/nsb0397-175","article-title":"Crystal structure of a calponin homology domain","volume":"4","author":"Carugo","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB30","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1146\/annurev.cb.11.110195.002433","article-title":"Control of actin assembly at filament ends","volume":"11","author":"Schafer","year":"1995","journal-title":"Annu Rev Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB31","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0955-0674(05)80009-2","article-title":"F-actin capping proteins","volume":"5","author":"Weeds","year":"1993","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB32","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1091\/mbc.6.11.1423","article-title":"The ADF\/cofilin proteins: stimulus-responsive modulators of actin dynamics","volume":"6","author":"Moon","year":"1995","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB33","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/0092-8674(88)90542-9","article-title":"Pieces in the actin-severing protein puzzle","volume":"54","author":"Matsudaira","year":"1988","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB34","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/S0021-9258(19)35412-2","article-title":"Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains","volume":"263","author":"Andr\u00e9","year":"1988","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB35","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/281583a0","article-title":"Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein","volume":"281","author":"Yin","year":"1979","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB36","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1111\/j.1432-1033.1991.tb16480.x","article-title":"Rate constants and equilibrium constants for binding of actin to the 1:1 gelsolin-actin complex","volume":"202","author":"Schoepper","year":"1991","journal-title":"Eur J Biochem"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB37","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1038\/325362a0","article-title":"Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate","volume":"325","author":"Janmey","year":"1987","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB38","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/0014-5793(90)80769-F","article-title":"Severin is a gelsolin prototype","volume":"264","author":"Yin","year":"1990","journal-title":"FEBS Lett"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB39","doi-asserted-by":"crossref","first-page":"4103","DOI":"10.1002\/j.1460-2075.1990.tb07632.x","article-title":"Identification of a region in segment 1 of gelsolin critical for actin binding","volume":"9","author":"Way","year":"1990","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB40","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1083\/jcb.112.4.665","article-title":"Domain structure in actin-binding proteins: expression and functional characterization of truncated severin","volume":"112","author":"Eichinger","year":"1991","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB41","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1083\/jcb.119.4.835","article-title":"Evidence for functional homology in the F-actin binding domains of gelsolin and \u03b1-actinin: implications for the requirements of severing and capping","volume":"119","author":"Way","year":"1992","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB42","doi-asserted-by":"crossref","first-page":"4779","DOI":"10.1021\/bi00135a006","article-title":"Characterization of actin- and lipid-binding domains in severin, a Ca2+-dependent F-actin fragmenting protein","volume":"31","author":"Eichinger","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB43","doi-asserted-by":"crossref","first-page":"1717","DOI":"10.1083\/jcb.108.5.1717","article-title":"Identification of critical functional and regulatory domains in gelsolin","volume":"108","author":"Kwiatkowski","year":"1989","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB44","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1038\/364685a0","article-title":"Structure of gelsolin segment 1-actin complex and the mechanism of filament severing","volume":"364","author":"McLaughlin","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB45_1","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1002\/pro.5560060608","article-title":"Refined structure of villin 14T and a detailed comparison with other actin-severing proteins","volume":"6","author":"Markus","year":"1997","journal-title":"Protein Sci"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB46","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1006\/jmbi.1994.0118","article-title":"Structure of severin domain 2 in solution","volume":"247","author":"Schnuchel","year":"1995","journal-title":"J Mol Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB47_1","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1016\/S0092-8674(00)80527-9","article-title":"The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation","volume":"90","author":"Burtnick","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB48","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/S0014-5793(96)01086-1","article-title":"Evidence for an actin binding helix in gelsolin segment 2: have homologous sequences in segments 1 and 2 of gelsolin evolved to divergent actin binding functions?","volume":"397","author":"Van Troys","year":"1996","journal-title":"FEBS Lett"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB49","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1083\/jcb.116.5.1145","article-title":"In vivo analysis of functional domains from villin and gelsolin","volume":"116","author":"Finidori","year":"1992","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB50","doi-asserted-by":"crossref","first-page":"16738","DOI":"10.1016\/S0021-9258(18)37453-2","article-title":"Functional comparison of villin and gelsolin","volume":"263","author":"Janmey","year":"1988","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB51","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/0014-5793(94)80116-9","article-title":"Characterization of the F-actin binding domains of villin: classification of F-actin binding proteins into two groups according to their binding sites on actin","volume":"338","author":"Pope","year":"1994","journal-title":"FEBS Lett"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB52","doi-asserted-by":"crossref","first-page":"6651","DOI":"10.1073\/pnas.90.14.6651","article-title":"Cloning of human erythroid dematin reveals another member of the villin family","volume":"90","author":"Rana","year":"1994","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB53","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1083\/jcb.138.3.575","article-title":"Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein","volume":"138","author":"Roof","year":"1997","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB54","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1038\/nsb0397-180","article-title":"NMR structure of the 35-residue villin headpiece subdomain","volume":"4","author":"McKnight","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB55","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1083\/jcb.136.6.1307","article-title":"Actin depolymerization factor (ADF\/cofilin) enhances the rate of filament turnover: implications in actin-based motility","volume":"136","author":"Carlier","year":"1997","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB56","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.1083\/jcb.136.6.1323","article-title":"Xenopus actin depolymerizing factor\/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails","volume":"136","author":"Rosenblatt","year":"1997","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB57","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1083\/jcb.120.2.421","article-title":"Cofilin is an essential component of the yeast cortical cytoskeleton","volume":"120","author":"Moon","year":"1993","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB58_1","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1016\/S0092-8674(00)81305-7","article-title":"Tertiary structure of destrin and structural similarity between two actin-regulating protein families","volume":"85","author":"Hatanaka","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB59_1","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1038\/nsb0597-366","article-title":"Structure determination of yeast cofilin","volume":"4","author":"Fedorov","year":"1997","journal-title":"Nature Struct Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB60_1","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1038\/nsb0597-369","article-title":"Crystal structure of the actin-binding protein actophorin from Acanthamoeba","volume":"4","author":"Leonard","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB61_1","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1083\/jcb.138.4.771","article-title":"Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function","volume":"138","author":"McGough","year":"1997","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB62_1","doi-asserted-by":"crossref","first-page":"5520","DOI":"10.1093\/emboj\/16.18.5520","article-title":"Essential functions of actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis","volume":"16","author":"Lappalainen","year":"1997","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB63","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1083\/jcb.110.1.105","article-title":"Purification of profilin from Saccharomyces cerevisiae and analysis of profilin-deficient cells","volume":"110","author":"Haarer","year":"1997","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB64","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/0092-8674(92)90128-Y","article-title":"chickadee encodes a profilin required for intercellular cytoplasm transport during Drosophila oogenesis","volume":"69","author":"Cooley","year":"1992","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB65","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1083\/jcb.125.6.1289","article-title":"The Schizosaccharomyces pombe cdc3+ gene encodes a profilin essential for cytokinesis","volume":"125","author":"Balasubramanian","year":"1994","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB66","doi-asserted-by":"crossref","first-page":"1510","DOI":"10.1073\/pnas.91.4.1510","article-title":"Dynamic actin structures stabilized by profilin","volume":"91","author":"Finkel","year":"1994","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB67","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1091\/mbc.3.9.1015","article-title":"The control of actin nucleotide exchange by thymosin \u03b2-4 and profilin: a potential regulatory mechanism for actin polymerization in cells","volume":"33","author":"Goldschmidt-Clermont","year":"1992","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB68","doi-asserted-by":"crossref","first-page":"5034","DOI":"10.1073\/pnas.90.11.5034","article-title":"Modulation of the interaction between G-actin and \u03b2-4 by the ATP\/ADP ratio","volume":"903","author":"Carlier","year":"1993","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB69","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1016\/0092-8674(93)90544-Z","article-title":"How profilin promotes actin filament assembly in the presence of thymosin \u03b2-4","volume":"753","author":"Pantaloni","year":"1993","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB70","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1038\/365810a0","article-title":"The structure of crystalline profilin-beta-actin","volume":"365","author":"Schutt","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB71","doi-asserted-by":"crossref","first-page":"8636","DOI":"10.1073\/pnas.91.18.8636","article-title":"X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates","volume":"91","author":"Fedorov","year":"1994","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB72","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1006\/jmbi.1994.1461","article-title":"Crystallization and structure determination of bovine profilin at 2.0 \u00c5 resolution","volume":"240","author":"Cedergren-Zeppezauer","year":"1994","journal-title":"J Mol Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB73_1","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/S0969-2126(97)00163-9","article-title":"The crystal structure of a major allergen from plants","volume":"5","author":"Thorn","year":"1997","journal-title":"Structure"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB74_1","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/S0969-2126(97)00164-0","article-title":"The molecular basis for allergen cross-reactivity: crystal structure and IgE-epitope mapping of birch pollen profilin","volume":"5","author":"Fedorov","year":"1996","journal-title":"Structure"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB75_1","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1006\/jmbi.1996.0602","article-title":"The structure of an open state of beta-actin at 2.65 \u00c5 resolution","volume":"263","author":"Chik","year":"1996","journal-title":"J Mol Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB76","doi-asserted-by":"crossref","first-page":"16535","DOI":"10.1021\/bi961498d","article-title":"Structural requirements and thermodynamics of the interaction of proline peptides with profilin","volume":"35","author":"Petrella","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB77","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/S0092-8674(00)81341-0","article-title":"Mena, a relative of VASP and Drosophila Enabled is implicated in the control of microfilament dynamics","volume":"87","author":"Gertler","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB78","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1002\/j.1460-2075.1995.tb07117.x","article-title":"A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin based cytoskeleton of mamalian cells","volume":"14","author":"Chakraborty","year":"1995","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB79","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1002\/j.1460-2075.1995.tb07146.x","article-title":"The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilin","volume":"14","author":"Reinhard","year":"1995","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB80","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1126\/science.276.5309.118","article-title":"Bni1p, a yeast Formin linking Cdc42p and the actin cytoskeleton during polarized morphogenesis","volume":"276","author":"Evangalista","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB81","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1083\/jcb.137.1.169","article-title":"cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin","volume":"137","author":"Chang","year":"1997","journal-title":"J Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB82","doi-asserted-by":"crossref","first-page":"3044","DOI":"10.1093\/emboj\/16.11.3044","article-title":"p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin","volume":"16","author":"Watanabe","year":"1997","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB83","doi-asserted-by":"crossref","first-page":"3697","DOI":"10.1128\/MCB.15.7.3697","article-title":"Characterization of fus1 of Schizosaccharomyces pombe: A developmentally controlled function needed for conjugation","volume":"15","author":"Petersen","year":"1995","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB84","doi-asserted-by":"crossref","first-page":"2109","DOI":"10.1242\/dev.122.7.2109","article-title":"Profilin is required for posterior patterning of the Drosophila oocyte","volume":"122","author":"Manseau","year":"1996","journal-title":"Development"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB85","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1093\/genetics\/139.2.537","article-title":"Identification of developmental regulatory genes in Aspergillus nidulans by overexpression","volume":"139","author":"Marhoul","year":"1995","journal-title":"Genetics"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB86_1","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1038\/nsb1197-953","article-title":"Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation","volume":"43","author":"Mahoney","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB87","doi-asserted-by":"crossref","first-page":"8472","DOI":"10.1021\/bi00194a011","article-title":"Interaction of profilin with G-actin and poly-L-proline","volume":"333","author":"Perelroizen","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB88","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1126\/science.8438166","article-title":"Identification of a ten-amino acid proline-rich SH3 binding site","volume":"259","author":"Ren","year":"1993","journal-title":"Science"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB89","doi-asserted-by":"crossref","first-page":"7819","DOI":"10.1073\/pnas.92.17.7819","article-title":"The WW domain of YES-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules","volume":"92","author":"Chen","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB90","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1016\/0092-8674(94)90367-0","article-title":"Structural basis for the binding of proline-rich peptides to SH3 domains","volume":"76","author":"Yu","year":"1994","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB91_1","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1038\/382646a0","article-title":"Structure of the WW domain of a kinase associated protein complexed with a proline-rich peptide","volume":"382","author":"Macias","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB92","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1002\/j.1460-2075.1996.tb00442.x","article-title":"Formin binding proteins bear WWP\/WW domains that bind proline-rich peptides and functionally resemble SH3 domains","volume":"15","author":"Chan","year":"1996","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB93","doi-asserted-by":"crossref","first-page":"3110","DOI":"10.1073\/pnas.92.8.3110","article-title":"Proline-rich sequences that bind to Src homology domains with individual specificities","volume":"92","author":"Alexandropoulos","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB94","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S0968-0004(96)30018-2","article-title":"The WW module competes with the SH3 domain?","volume":"21","author":"Sudol","year":"1996","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB95","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/347037a0","article-title":"Atomic structure of the actin:DNase I complex","volume":"347","author":"Kabsch","year":"1990","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB96","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1006\/jmbi.1993.1628","article-title":"Refinement of the F-actin model against X-ray fiber diffraction data by use of a directed mutation algorithm","volume":"234","author":"Lorenz","year":"1993","journal-title":"J Mol Biol"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB97","doi-asserted-by":"crossref","first-page":"12408","DOI":"10.1073\/pnas.92.26.12408","article-title":"Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands","volume":"92","author":"Feng","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB98","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1107\/S0021889891004399","article-title":"MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures","volume":"24","author":"Kraulis","year":"1991","journal-title":"Appl Crystallog"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB99","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1002\/prot.340110407","article-title":"Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons","volume":"11","author":"Nicholls","year":"1991","journal-title":"Proteins"},{"key":"10.1016\/S0955-0674(98)80083-5_BIB100","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/0263-7855(93)87009-T","article-title":"SETOR: hardware-lighted three-dimensional solid model representation of macromolecules","volume":"11","author":"Evans","year":"1993","journal-title":"J Mol Graph"}],"container-title":["Current Opinion in Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0955067498800835?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0955067498800835?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,5,4]],"date-time":"2021-05-04T12:39:13Z","timestamp":1620131953000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0955067498800835"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,2]]},"references-count":100,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1998,2]]}},"alternative-id":["S0955067498800835"],"URL":"https:\/\/doi.org\/10.1016\/s0955-0674(98)80083-5","relation":{},"ISSN":["0955-0674"],"issn-type":[{"value":"0955-0674","type":"print"}],"subject":[],"published":{"date-parts":[[1998,2]]}}}