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Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Abe H., Endo T., Yamamoto K., Obinata T. Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic chicken skeletal muscle: two functionally distinct actin-regulatory proteins exhibit high structural homology. Biochemistry. 1990 Aug 14;29(32):7420–7425. doi: 10.1021/bi00484a010. [DOI] [PubMed] [Google Scholar]
- Abe H., Nagaoka R., Obinata T. Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes. Exp Cell Res. 1993 May;206(1):1–10. doi: 10.1006/excr.1993.1113. [DOI] [PubMed] [Google Scholar]
- Adams M. E., Minamide L. S., Duester G., Bamburg J. R. Nucleotide sequence and expression of a cDNA encoding chick brain actin depolymerizing factor. Biochemistry. 1990 Aug 14;29(32):7414–7420. doi: 10.1021/bi00484a009. [DOI] [PubMed] [Google Scholar]
- Agnew B. J., Minamide L. S., Bamburg J. R. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J Biol Chem. 1995 Jul 21;270(29):17582–17587. doi: 10.1074/jbc.270.29.17582. [DOI] [PubMed] [Google Scholar]
- Aizawa H., Sutoh K., Tsubuki S., Kawashima S., Ishii A., Yahara I. Identification, characterization, and intracellular distribution of cofilin in Dictyostelium discoideum. J Biol Chem. 1995 May 5;270(18):10923–10932. doi: 10.1074/jbc.270.18.10923. [DOI] [PubMed] [Google Scholar]
- Bamburg J. R., Harris H. E., Weeds A. G. Partial purification and characterization of an actin depolymerizing factor from brain. FEBS Lett. 1980 Nov 17;121(1):178–182. doi: 10.1016/0014-5793(80)81292-0. [DOI] [PubMed] [Google Scholar]
- Baorto D. M., Mellado W., Shelanski M. L. Astrocyte process growth induction by actin breakdown. J Cell Biol. 1992 Apr;117(2):357–367. doi: 10.1083/jcb.117.2.357. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bearer E. L. Direct observation of actin filament severing by gelsolin and binding by gCap39 and CapZ. J Cell Biol. 1991 Dec;115(6):1629–1638. doi: 10.1083/jcb.115.6.1629. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bernstein B. W., Bamburg J. R. Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil. 1982;2(1):1–8. doi: 10.1002/cm.970020102. [DOI] [PubMed] [Google Scholar]
- Cao L. G., Babcock G. G., Rubenstein P. A., Wang Y. L. Effects of profilin and profilactin on actin structure and function in living cells. J Cell Biol. 1992 Jun;117(5):1023–1029. doi: 10.1083/jcb.117.5.1023. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Carlier M. F., Jean C., Rieger K. J., Lenfant M., Pantaloni D. Modulation of the interaction between G-actin and thymosin beta 4 by the ATP/ADP ratio: possible implication in the regulation of actin dynamics. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5034–5038. doi: 10.1073/pnas.90.11.5034. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Carlier M. F., Pantaloni D. Binding of phosphate to F-ADP-actin and role of F-ADP-Pi-actin in ATP-actin polymerization. J Biol Chem. 1988 Jan 15;263(2):817–825. [PubMed] [Google Scholar]
- Carlsson L., Nyström L. E., Sundkvist I., Markey F., Lindberg U. Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J Mol Biol. 1977 Sep 25;115(3):465–483. doi: 10.1016/0022-2836(77)90166-8. [DOI] [PubMed] [Google Scholar]
- Cooper J. A., Blum J. D., Williams R. C., Jr, Pollard T. D. Purification and characterization of actophorin, a new 15,000-dalton actin-binding protein from Acanthamoeba castellanii. J Biol Chem. 1986 Jan 5;261(1):477–485. [PubMed] [Google Scholar]
- Davidson M. M., Haslam R. J. Dephosphorylation of cofilin in stimulated platelets: roles for a GTP-binding protein and Ca2+. Biochem J. 1994 Jul 1;301(Pt 1):41–47. doi: 10.1042/bj3010041. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Drubin D. G., Mulholland J., Zhu Z. M., Botstein D. Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I. Nature. 1990 Jan 18;343(6255):288–290. doi: 10.1038/343288a0. [DOI] [PubMed] [Google Scholar]
- Edwards K. A., Montague R. A., Shepard S., Edgar B. A., Erikson R. L., Kiehart D. P. Identification of Drosophila cytoskeletal proteins by induction of abnormal cell shape in fission yeast. Proc Natl Acad Sci U S A. 1994 May 10;91(10):4589–4593. doi: 10.1073/pnas.91.10.4589. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fechheimer M., Zigmond S. H. Focusing on unpolymerized actin. J Cell Biol. 1993 Oct;123(1):1–5. doi: 10.1083/jcb.123.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gieselmann R., Mann K. ASP-56, a new actin sequestering protein from pig platelets with homology to CAP, an adenylate cyclase-associated protein from yeast. FEBS Lett. 1992 Feb 24;298(2-3):149–153. doi: 10.1016/0014-5793(92)80043-g. [DOI] [PubMed] [Google Scholar]
- Goldschmidt-Clermont P. J., Furman M. I., Wachsstock D., Safer D., Nachmias V. T., Pollard T. D. The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol Biol Cell. 1992 Sep;3(9):1015–1024. doi: 10.1091/mbc.3.9.1015. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Harwell O. D., Sweeney M. L., Kirkpatrick F. H. Conformation changes of actin during formation of filaments and paracrystals and upon interaction with DNase I, cytochalasin B, and phalloidin. J Biol Chem. 1980 Feb 10;255(3):1210–1220. [PubMed] [Google Scholar]
- Hawkins M., Pope B., Maciver S. K., Weeds A. G. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry. 1993 Sep 28;32(38):9985–9993. doi: 10.1021/bi00089a014. [DOI] [PubMed] [Google Scholar]
- Hayden S. M., Miller P. S., Brauweiler A., Bamburg J. R. Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry. 1993 Sep 28;32(38):9994–10004. doi: 10.1021/bi00089a015. [DOI] [PubMed] [Google Scholar]
- Iida K., Moriyama K., Matsumoto S., Kawasaki H., Nishida E., Yahara I. Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein. Gene. 1993 Feb 14;124(1):115–120. doi: 10.1016/0378-1119(93)90770-4. [DOI] [PubMed] [Google Scholar]
- Ingber D. E., Prusty D., Frangioni J. V., Cragoe E. J., Jr, Lechene C., Schwartz M. A. Control of intracellular pH and growth by fibronectin in capillary endothelial cells. J Cell Biol. 1990 May;110(5):1803–1811. doi: 10.1083/jcb.110.5.1803. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Isambert H., Venier P., Maggs A. C., Fattoum A., Kassab R., Pantaloni D., Carlier M. F. Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J Biol Chem. 1995 May 12;270(19):11437–11444. doi: 10.1074/jbc.270.19.11437. [DOI] [PubMed] [Google Scholar]
- Ishikawa R., Hayashi K., Shirao T., Xue Y., Takagi T., Sasaki Y., Kohama K. Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments. J Biol Chem. 1994 Nov 25;269(47):29928–29933. [PubMed] [Google Scholar]
- Kabsch W., Mannherz H. G., Suck D., Pai E. F., Holmes K. C. Atomic structure of the actin:DNase I complex. Nature. 1990 Sep 6;347(6288):37–44. doi: 10.1038/347037a0. [DOI] [PubMed] [Google Scholar]
- Kanamori T., Hayakawa T., Suzuki M., Titani K. Identification of two 17-kDa rat parotid gland phosphoproteins, subjects for dephosphorylation upon beta-adrenergic stimulation, as destrin- and cofilin-like proteins. J Biol Chem. 1995 Apr 7;270(14):8061–8067. doi: 10.1074/jbc.270.14.8061. [DOI] [PubMed] [Google Scholar]
- Kim S. R., Kim Y., An G. Molecular cloning and characterization of anther-preferential cDNA encoding a putative actin-depolymerizing factor. Plant Mol Biol. 1993 Jan;21(1):39–45. doi: 10.1007/BF00039616. [DOI] [PubMed] [Google Scholar]
- Kojima N., Kato Y., Shirao T., Obata K. Nucleotide sequences of two embryonic drebrins, developmentally regulated brain proteins, and developmental change in their mRNAs. Brain Res. 1988 Nov;464(3):207–215. doi: 10.1016/0169-328x(88)90027-7. [DOI] [PubMed] [Google Scholar]
- Kwiatkowski D. J., Janmey P. A., Yin H. L. Identification of critical functional and regulatory domains in gelsolin. J Cell Biol. 1989 May;108(5):1717–1726. doi: 10.1083/jcb.108.5.1717. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lal A. A., Korn E. D. Reinvestigation of the inhibition of actin polymerization by profilin. J Biol Chem. 1985 Aug 25;260(18):10132–10138. [PubMed] [Google Scholar]
- Lassing I., Lindberg U. Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin. Nature. 1985 Apr 4;314(6010):472–474. doi: 10.1038/314472a0. [DOI] [PubMed] [Google Scholar]
- Lorenz M., Popp D., Holmes K. C. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J Mol Biol. 1993 Dec 5;234(3):826–836. doi: 10.1006/jmbi.1993.1628. [DOI] [PubMed] [Google Scholar]
- Mabuchi I. An actin-depolymerizing protein (depactin) from starfish oocytes: properties and interaction with actin. J Cell Biol. 1983 Nov;97(5 Pt 1):1612–1621. doi: 10.1083/jcb.97.5.1612. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mabuchi I. Biochemical aspects of cytokinesis. Int Rev Cytol. 1986;101:175–213. doi: 10.1016/s0074-7696(08)60249-1. [DOI] [PubMed] [Google Scholar]
- Mabuchi I. Effects of muscle proteins on the interaction between actin and an actin-depolymerizing protein from starfish oocytes. J Biochem. 1982 Nov;92(5):1439–1447. doi: 10.1093/oxfordjournals.jbchem.a134068. [DOI] [PubMed] [Google Scholar]
- Maciver S. K., Wachsstock D. H., Schwarz W. H., Pollard T. D. The actin filament severing protein actophorin promotes the formation of rigid bundles of actin filaments crosslinked with alpha-actinin. J Cell Biol. 1991 Dec;115(6):1621–1628. doi: 10.1083/jcb.115.6.1621. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Maciver S. K., Weeds A. G. Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: consequences for cell locomotion. FEBS Lett. 1994 Jun 27;347(2-3):251–256. doi: 10.1016/0014-5793(94)00552-4. [DOI] [PubMed] [Google Scholar]
- Maciver S. K., Zot H. G., Pollard T. D. Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J Cell Biol. 1991 Dec;115(6):1611–1620. doi: 10.1083/jcb.115.6.1611. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Magnus K. A., Maciver S. K., Pollard T. D. Crystallization of actophorin, an actin filament-severing protein from Acanthamoeba. J Biol Chem. 1988 Dec 5;263(34):18143–18144. [PubMed] [Google Scholar]
- McKim K. S., Matheson C., Marra M. A., Wakarchuk M. F., Baillie D. L. The Caenorhabditis elegans unc-60 gene encodes proteins homologous to a family of actin-binding proteins. Mol Gen Genet. 1994 Feb;242(3):346–357. doi: 10.1007/BF00280425. [DOI] [PubMed] [Google Scholar]
- Mockrin S. C., Korn E. D. Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5'-triphosphate. Biochemistry. 1980 Nov 11;19(23):5359–5362. doi: 10.1021/bi00564a033. [DOI] [PubMed] [Google Scholar]
- Moolenaar W. H., Tertoolen L. G., de Laat S. W. The regulation of cytoplasmic pH in human fibroblasts. J Biol Chem. 1984 Jun 25;259(12):7563–7569. [PubMed] [Google Scholar]
- Moolenaar W. H., Tsien R. Y., van der Saag P. T., de Laat S. W. Na+/H+ exchange and cytoplasmic pH in the action of growth factors in human fibroblasts. Nature. 1983 Aug 18;304(5927):645–648. doi: 10.1038/304645a0. [DOI] [PubMed] [Google Scholar]
- Moon A. L., Janmey P. A., Louie K. A., Drubin D. G. Cofilin is an essential component of the yeast cortical cytoskeleton. J Cell Biol. 1993 Jan;120(2):421–435. doi: 10.1083/jcb.120.2.421. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morgan T. E., Lockerbie R. O., Minamide L. S., Browning M. D., Bamburg J. R. Isolation and characterization of a regulated form of actin depolymerizing factor. J Cell Biol. 1993 Aug;122(3):623–633. doi: 10.1083/jcb.122.3.623. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Moriyama K., Matsumoto S., Nishida E., Sakai H., Yahara I. Nucleotide sequence of mouse cofilin cDNA. Nucleic Acids Res. 1990 May 25;18(10):3053–3053. doi: 10.1093/nar/18.10.3053. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Moriyama K., Nishida E., Yonezawa N., Sakai H., Matsumoto S., Iida K., Yahara I. Destrin, a mammalian actin-depolymerizing protein, is closely related to cofilin. Cloning and expression of porcine brain destrin cDNA. J Biol Chem. 1990 Apr 5;265(10):5768–5773. [PubMed] [Google Scholar]
- Moriyama K., Yonezawa N., Sakai H., Yahara I., Nishida E. Mutational analysis of an actin-binding site of cofilin and characterization of chimeric proteins between cofilin and destrin. J Biol Chem. 1992 Apr 15;267(11):7240–7244. [PubMed] [Google Scholar]
- Muneyuki E., Nishida E., Sutoh K., Sakai H. Purification of cofilin, a 21,000 molecular weight actin-binding protein, from porcine kidney and identification of the cofilin-binding site in the actin sequence. J Biochem. 1985 Feb;97(2):563–568. doi: 10.1093/oxfordjournals.jbchem.a135091. [DOI] [PubMed] [Google Scholar]
- Nachmias V. T. Small actin-binding proteins: the beta-thymosin family. Curr Opin Cell Biol. 1993 Feb;5(1):56–62. doi: 10.1016/s0955-0674(05)80008-0. [DOI] [PubMed] [Google Scholar]
- Nagaoka R., Abe H., Kusano K., Obinata T. Concentration of cofilin, a small actin-binding protein, at the cleavage furrow during cytokinesis. Cell Motil Cytoskeleton. 1995;30(1):1–7. doi: 10.1002/cm.970300102. [DOI] [PubMed] [Google Scholar]
- Nagaoka R., Kusano K., Abe H., Obinata T. Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action. J Cell Sci. 1995 Feb;108(Pt 2):581–593. doi: 10.1242/jcs.108.2.581. [DOI] [PubMed] [Google Scholar]
- Nishida E., Iida K., Yonezawa N., Koyasu S., Yahara I., Sakai H. Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5262–5266. doi: 10.1073/pnas.84.15.5262. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nishida E., Maekawa S., Muneyuki E., Sakai H. Action of a 19K protein from porcine brain on actin polymerization: a new functional class of actin-binding proteins. J Biochem. 1984 Feb;95(2):387–398. doi: 10.1093/oxfordjournals.jbchem.a134619. [DOI] [PubMed] [Google Scholar]
- Nishida E., Maekawa S., Sakai H. Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry. 1984 Oct 23;23(22):5307–5313. doi: 10.1021/bi00317a032. [DOI] [PubMed] [Google Scholar]
- Nishida E., Muneyuki E., Maekawa S., Ohta Y., Sakai H. An actin-depolymerizing protein (destrin) from porcine kidney. Its action on F-actin containing or lacking tropomyosin. Biochemistry. 1985 Nov 5;24(23):6624–6630. doi: 10.1021/bi00344a049. [DOI] [PubMed] [Google Scholar]
- Nishida E. Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5'-triphosphate. Biochemistry. 1985 Feb 26;24(5):1160–1164. doi: 10.1021/bi00326a015. [DOI] [PubMed] [Google Scholar]
- Novick P., Botstein D. Phenotypic analysis of temperature-sensitive yeast actin mutants. Cell. 1985 Feb;40(2):405–416. doi: 10.1016/0092-8674(85)90154-0. [DOI] [PubMed] [Google Scholar]
- Ohta Y., Nishida E., Sakai H., Miyamoto E. Dephosphorylation of cofilin accompanies heat shock-induced nuclear accumulation of cofilin. J Biol Chem. 1989 Sep 25;264(27):16143–16148. [PubMed] [Google Scholar]
- Pantaloni D., Carlier M. F. How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell. 1993 Dec 3;75(5):1007–1014. doi: 10.1016/0092-8674(93)90544-z. [DOI] [PubMed] [Google Scholar]
- Pollard T. D., Cooper J. A. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu Rev Biochem. 1986;55:987–1035. doi: 10.1146/annurev.bi.55.070186.005011. [DOI] [PubMed] [Google Scholar]
- Pollard T. D. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J Cell Biol. 1986 Dec;103(6 Pt 2):2747–2754. doi: 10.1083/jcb.103.6.2747. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Quirk S., Maciver S. K., Ampe C., Doberstein S. K., Kaiser D. A., VanDamme J., Vandekerckhove J. S., Pollard T. D. Primary structure of and studies on Acanthamoeba actophorin. Biochemistry. 1993 Aug 24;32(33):8525–8533. doi: 10.1021/bi00084a019. [DOI] [PubMed] [Google Scholar]
- Saito T., Lamy F., Roger P. P., Lecocq R., Dumont J. E. Characterization and identification as cofilin and destrin of two thyrotropin- and phorbol ester-regulated phosphoproteins in thyroid cells. Exp Cell Res. 1994 May;212(1):49–61. doi: 10.1006/excr.1994.1117. [DOI] [PubMed] [Google Scholar]
- Samstag Y., Eckerskorn C., Wesselborg S., Henning S., Wallich R., Meuer S. C. Costimulatory signals for human T-cell activation induce nuclear translocation of pp19/cofilin. Proc Natl Acad Sci U S A. 1994 May 10;91(10):4494–4498. doi: 10.1073/pnas.91.10.4494. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schwartz M. A., Ingber D. E., Lawrence M., Springer T. A., Lechene C. Multiple integrins share the ability to induce elevation of intracellular pH. Exp Cell Res. 1991 Aug;195(2):533–535. doi: 10.1016/0014-4827(91)90407-l. [DOI] [PubMed] [Google Scholar]
- Stossel T. P., Chaponnier C., Ezzell R. M., Hartwig J. H., Janmey P. A., Kwiatkowski D. J., Lind S. E., Smith D. B., Southwick F. S., Yin H. L. Nonmuscle actin-binding proteins. Annu Rev Cell Biol. 1985;1:353–402. doi: 10.1146/annurev.cb.01.110185.002033. [DOI] [PubMed] [Google Scholar]
- Sun H. Q., Kwiatkowska K., Yin H. L. Actin monomer binding proteins. Curr Opin Cell Biol. 1995 Feb;7(1):102–110. doi: 10.1016/0955-0674(95)80051-4. [DOI] [PubMed] [Google Scholar]
- Sutoh K., Mabuchi I. End-label fingerprintings show that an N-terminal segment of depactin participates in interaction with actin. Biochemistry. 1989 Jan 10;28(1):102–106. doi: 10.1021/bi00427a015. [DOI] [PubMed] [Google Scholar]
- Sutoh K., Mabuchi I. Improved method for mapping the binding site of an actin-binding protein in the actin sequence. Use of a site-directed antibody against the N-terminal region of actin as a probe of its N-terminus. Biochemistry. 1986 Oct 7;25(20):6186–6192. doi: 10.1021/bi00368a053. [DOI] [PubMed] [Google Scholar]
- Takagi T., Konishi K., Mabuchi I. Amino acid sequence of starfish oocyte depactin. J Biol Chem. 1988 Mar 5;263(7):3097–3102. [PubMed] [Google Scholar]
- Tilney L. G. Polymerization of actin. V. A new organelle, the actomere, that initates the assembly of actin filaments in Thyone sperm. J Cell Biol. 1978 May;77(2):551–564. [PMC free article] [PubMed] [Google Scholar]
- Way M., Gooch J., Pope B., Weeds A. G. Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis. J Cell Biol. 1989 Aug;109(2):593–605. doi: 10.1083/jcb.109.2.593. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yonezawa N., Nishida E., Iida K., Kumagai H., Yahara I., Sakai H. Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin. J Biol Chem. 1991 Jun 5;266(16):10485–10489. [PubMed] [Google Scholar]
- Yonezawa N., Nishida E., Iida K., Yahara I., Sakai H. Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J Biol Chem. 1990 May 25;265(15):8382–8386. [PubMed] [Google Scholar]
- Yonezawa N., Nishida E., Koyasu S., Maekawa S., Ohta Y., Yahara I., Sakai H. Distribution among tissues and intracellular localization of cofilin, a 21kDa actin-binding protein. Cell Struct Funct. 1987 Oct;12(5):443–452. doi: 10.1247/csf.12.443. [DOI] [PubMed] [Google Scholar]
- Yonezawa N., Nishida E., Ohba M., Seki M., Kumagai H., Sakai H. An actin-interacting heptapeptide in the cofilin sequence. Eur J Biochem. 1989 Jul 15;183(1):235–238. doi: 10.1111/j.1432-1033.1989.tb14918.x. [DOI] [PubMed] [Google Scholar]
- Yonezawa N., Nishida E., Sakai H., Koyasu S., Matsuzaki F., Iida K., Yahara I. Purification and characterization of the 90-kDa heat-shock protein from mammalian tissues. Eur J Biochem. 1988 Oct 15;177(1):1–7. doi: 10.1111/j.1432-1033.1988.tb14337.x. [DOI] [PubMed] [Google Scholar]
- Yonezawa N., Nishida E., Sakai H. pH control of actin polymerization by cofilin. J Biol Chem. 1985 Nov 25;260(27):14410–14412. [PubMed] [Google Scholar]
- de Hostos E. L., Bradtke B., Lottspeich F., Gerisch G. Coactosin, a 17 kDa F-actin binding protein from Dictyostelium discoideum. Cell Motil Cytoskeleton. 1993;26(3):181–191. doi: 10.1002/cm.970260302. [DOI] [PubMed] [Google Scholar]