Full text
PDF














Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- ASAKURA S. The interaction between G-actin and ATP. Arch Biochem Biophys. 1961 Jan;92:140–149. doi: 10.1016/0003-9861(61)90228-4. [DOI] [PubMed] [Google Scholar]
- Adam L., Laroche A., Barden A., Lemieux G., Pallotta D. An unusual actin-encoding gene in Physarum polycephalum. Gene. 1991 Sep 30;106(1):79–86. doi: 10.1016/0378-1119(91)90568-v. [DOI] [PubMed] [Google Scholar]
- Aktories K., Bärmann M., Ohishi I., Tsuyama S., Jakobs K. H., Habermann E. Botulinum C2 toxin ADP-ribosylates actin. Nature. 1986 Jul 24;322(6077):390–392. doi: 10.1038/322390a0. [DOI] [PubMed] [Google Scholar]
- Aktories K., Wegner A. ADP-ribosylation of actin by clostridial toxins. J Cell Biol. 1989 Oct;109(4 Pt 1):1385–1387. doi: 10.1083/jcb.109.4.1385. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Aktories K., Wille M., Just I. Clostridial actin-ADP-ribosylating toxins. Curr Top Microbiol Immunol. 1992;175:97–113. doi: 10.1007/978-3-642-76966-5_5. [DOI] [PubMed] [Google Scholar]
- Anderson P. Molecular genetics of nematode muscle. Annu Rev Genet. 1989;23:507–525. doi: 10.1146/annurev.ge.23.120189.002451. [DOI] [PubMed] [Google Scholar]
- Aspenström P., Engkvist H., Lindberg U., Karlsson R. Characterization of yeast-expressed beta-actins, site-specifically mutated at the tumor-related residue Gly245. Eur J Biochem. 1992 Jul 1;207(1):315–320. doi: 10.1111/j.1432-1033.1992.tb17052.x. [DOI] [PubMed] [Google Scholar]
- Aspenström P., Karlsson R. Interference with myosin subfragment-1 binding by site-directed mutagenesis of actin. Eur J Biochem. 1991 Aug 15;200(1):35–41. doi: 10.1111/j.1432-1033.1991.tb21045.x. [DOI] [PubMed] [Google Scholar]
- Aspenström P., Lindberg U., Karlsson R. Site-specific amino-terminal mutants of yeast-expressed beta-actin. Characterization of the interaction with myosin and tropomyosin. FEBS Lett. 1992 May 25;303(1):59–63. doi: 10.1016/0014-5793(92)80477-x. [DOI] [PubMed] [Google Scholar]
- Baird W. V., Meagher R. B. A complex gene superfamily encodes actin in petunia. EMBO J. 1987 Nov;6(11):3223–3231. doi: 10.1002/j.1460-2075.1987.tb02639.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ball E., Karlik C. C., Beall C. J., Saville D. L., Sparrow J. C., Bullard B., Fyrberg E. A. Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate. Cell. 1987 Oct 23;51(2):221–228. doi: 10.1016/0092-8674(87)90149-8. [DOI] [PubMed] [Google Scholar]
- Bleasby A. J., Wootton J. C. Construction of validated, non-redundant composite protein sequence databases. Protein Eng. 1990 Jan;3(3):153–159. doi: 10.1093/protein/3.3.153. [DOI] [PubMed] [Google Scholar]
- Burdon R. H. Heat shock and the heat shock proteins. Biochem J. 1986 Dec 1;240(2):313–324. doi: 10.1042/bj2400313. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Campos A., Bernard P., Fauconnier A., Landa A., Gómez E., Hernández R., Willms K., Laclette J. P. Cloning and sequencing of two actin genes from Taenia solium (Cestoda). Mol Biochem Parasitol. 1990 Apr;40(1):87–93. doi: 10.1016/0166-6851(90)90082-w. [DOI] [PubMed] [Google Scholar]
- Carlier M. F. Actin: protein structure and filament dynamics. J Biol Chem. 1991 Jan 5;266(1):1–4. [PubMed] [Google Scholar]
- Chothia C., Lesk A. M. The relation between the divergence of sequence and structure in proteins. EMBO J. 1986 Apr;5(4):823–826. doi: 10.1002/j.1460-2075.1986.tb04288.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Clark S. W., Meyer D. I. Centractin is an actin homologue associated with the centrosome. Nature. 1992 Sep 17;359(6392):246–250. doi: 10.1038/359246a0. [DOI] [PubMed] [Google Scholar]
- Cook R. K., Blake W. T., Rubenstein P. A. Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo. J Biol Chem. 1992 May 5;267(13):9430–9436. [PubMed] [Google Scholar]
- Cooke R. Force generation in muscle. Curr Opin Cell Biol. 1990 Feb;2(1):62–66. doi: 10.1016/s0955-0674(05)80032-8. [DOI] [PubMed] [Google Scholar]
- Cupples C. G., Pearlman R. E. Isolation and characterization of the actin gene from Tetrahymena thermophila. Proc Natl Acad Sci U S A. 1986 Jul;83(14):5160–5164. doi: 10.1073/pnas.83.14.5160. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DasGupta G., Reisler E. Actomyosin interactions in the presence of ATP and the N-terminal segment of actin. Biochemistry. 1992 Feb 18;31(6):1836–1841. doi: 10.1021/bi00121a036. [DOI] [PubMed] [Google Scholar]
- DasGupta G., White J., Cheung P., Reisler E. Interactions between G-actin and myosin subfragment 1: immunochemical probing of the NH2-terminal segment on actin. Biochemistry. 1990 Sep 11;29(36):8503–8508. doi: 10.1021/bi00488a043. [DOI] [PubMed] [Google Scholar]
- DasGupta G., White J., Phillips M., Bulinski J. C., Reisler E. Immunochemical probing of the N-terminal segment on actin: the polymerization reaction. Biochemistry. 1990 Apr 3;29(13):3319–3324. doi: 10.1021/bi00465a024. [DOI] [PubMed] [Google Scholar]
- De Lozanne A., Spudich J. A. Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science. 1987 May 29;236(4805):1086–1091. doi: 10.1126/science.3576222. [DOI] [PubMed] [Google Scholar]
- DeNofrio D., Hoock T. C., Herman I. M. Functional sorting of actin isoforms in microvascular pericytes. J Cell Biol. 1989 Jul;109(1):191–202. doi: 10.1083/jcb.109.1.191. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Denning G. M., Kim I. S., Fulton A. B. Shedding of cytoplasmic actins by developing muscle cells. J Cell Sci. 1988 Feb;89(Pt 2):273–282. doi: 10.1242/jcs.89.2.273. [DOI] [PubMed] [Google Scholar]
- Drummond D. R., Hennessey E. S., Sparrow J. C. Stability of mutant actins. Biochem J. 1991 Feb 15;274(Pt 1):301–303. doi: 10.1042/bj2740301. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Drummond D. R., Hennessey E. S., Sparrow J. C. The binding of mutant actins to profilin, ATP and DNase I. Eur J Biochem. 1992 Oct 1;209(1):171–179. doi: 10.1111/j.1432-1033.1992.tb17274.x. [DOI] [PubMed] [Google Scholar]
- Drummond D. R., Peckham M., Sparrow J. C., White D. C. Alteration in crossbridge kinetics caused by mutations in actin. Nature. 1990 Nov 29;348(6300):440–442. doi: 10.1038/348440a0. [DOI] [PubMed] [Google Scholar]
- Elce J. S., Elbrecht A. S., Middlestadt M. U., McIntyre E. J., Anderson P. J. Actin from pig and rat uterus. Biochem J. 1981 Mar 1;193(3):891–898. doi: 10.1042/bj1930891. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Faulstich H., Merkler I., Blackholm H., Stournaras C. Nucleotide in monomeric actin regulates the reactivity of the thiol groups. Biochemistry. 1984 Apr 10;23(8):1608–1612. doi: 10.1021/bi00303a004. [DOI] [PubMed] [Google Scholar]
- Fidel S., Doonan J. H., Morris N. R. Aspergillus nidulans contains a single actin gene which has unique intron locations and encodes a gamma-actin. Gene. 1988 Oct 30;70(2):283–293. doi: 10.1016/0378-1119(88)90200-4. [DOI] [PubMed] [Google Scholar]
- Fire A. Integrative transformation of Caenorhabditis elegans. EMBO J. 1986 Oct;5(10):2673–2680. doi: 10.1002/j.1460-2075.1986.tb04550.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Flaherty K. M., McKay D. B., Kabsch W., Holmes K. C. Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):5041–5045. doi: 10.1073/pnas.88.11.5041. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Frankel S., Sohn R., Leinwand L. The use of sarkosyl in generating soluble protein after bacterial expression. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1192–1196. doi: 10.1073/pnas.88.4.1192. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Friedman E., Verderame M., Winawer S., Pollack R. Actin cytoskeletal organization loss in the benign-to-malignant tumor transition in cultured human colonic epithelial cells. Cancer Res. 1984 Jul;44(7):3040–3050. [PubMed] [Google Scholar]
- Fulton C., Lai E. Y., Lamoyi E., Sussman D. J. Naegleria actin elicits species-specific antibodies. J Protozool. 1986 Aug;33(3):322–327. doi: 10.1111/j.1550-7408.1986.tb05618.x. [DOI] [PubMed] [Google Scholar]
- Fyrberg E. A., Mahaffey J. W., Bond B. J., Davidson N. Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner. Cell. 1983 May;33(1):115–123. doi: 10.1016/0092-8674(83)90340-9. [DOI] [PubMed] [Google Scholar]
- Gallwitz D., Sures I. Structure of a split yeast gene: complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1980 May;77(5):2546–2550. doi: 10.1073/pnas.77.5.2546. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Garner I., Minty A. J., Alonso S., Barton P. J., Buckingham M. E. A 5' duplication of the alpha-cardiac actin gene in BALB/c mice is associated with abnormal levels of alpha-cardiac and alpha-skeletal actin mRNAs in adult cardiac tissue. EMBO J. 1986 Oct;5(10):2559–2567. doi: 10.1002/j.1460-2075.1986.tb04535.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Geeves M. A. The dynamics of actin and myosin association and the crossbridge model of muscle contraction. Biochem J. 1991 Feb 15;274(Pt 1):1–14. doi: 10.1042/bj2740001. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Geipel U., Just I., Aktories K. Inhibition of cytochalasin D-stimulated G-actin ATPase by ADP-ribosylation with Clostridium perfringens iota toxin. Biochem J. 1990 Mar 1;266(2):335–339. doi: 10.1042/bj2660335. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gerisch G., Segall J. E., Wallraff E. Isolation and behavioral analysis of mutants defective in cytoskeletal proteins. Cell Motil Cytoskeleton. 1989;14(1):75–79. doi: 10.1002/cm.970140115. [DOI] [PubMed] [Google Scholar]
- Goldstein D., Leavitt J. Expression of neoplasia-related proteins of chemically transformed HuT fibroblasts in human osteosarcoma HOS fibroblasts and modulation of actin expression upon elevation of tumorigenic potential. Cancer Res. 1985 Jul;45(7):3256–3261. [PubMed] [Google Scholar]
- Gordon D. J., Boyer J. L., Korn E. D. Comparative biochemistry of non-muscle actins. J Biol Chem. 1977 Nov 25;252(22):8300–8309. [PubMed] [Google Scholar]
- Gordon D. J., Eisenberg E., Korn E. D. Characterization of cytoplasmic actin isolated from Acanthamoeba castellanii by a new method. J Biol Chem. 1976 Aug 10;251(15):4778–4786. [PubMed] [Google Scholar]
- Greer C., Schekman R. Actin from Saccharomyces cerevisiae. Mol Cell Biol. 1982 Oct;2(10):1270–1278. doi: 10.1128/mcb.2.10.1270. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gunning P., Ponte P., Kedes L., Hickey R. J., Skoultchi A. I. Expression of human cardiac actin in mouse L cells: a sarcomeric actin associates with a nonmuscle cytoskeleton. Cell. 1984 Mar;36(3):709–715. doi: 10.1016/0092-8674(84)90351-9. [DOI] [PubMed] [Google Scholar]
- Hartwig J. H., Kwiatkowski D. J. Actin-binding proteins. Curr Opin Cell Biol. 1991 Feb;3(1):87–97. doi: 10.1016/0955-0674(91)90170-4. [DOI] [PubMed] [Google Scholar]
- Haymer D. S., Anleitner J. E., He M., Thanaphum S., Saul S. H., Ivy J., Houtchens K., Arcangeli L. Actin genes in the Mediterranean fruit fly, Ceratitis capitata. Genetics. 1990 May;125(1):155–160. doi: 10.1093/genetics/125.1.155. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hennessey E. S., Drummond D. R., Sparrow J. C. Post-translational processing of the amino terminus affects actin function. Eur J Biochem. 1991 Apr 23;197(2):345–352. doi: 10.1111/j.1432-1033.1991.tb15917.x. [DOI] [PubMed] [Google Scholar]
- Hennessey E. S., Harrison A., Drummond D. R., Sparrow J. C. Mutant actin: a dead end? J Muscle Res Cell Motil. 1992 Apr;13(2):127–131. doi: 10.1007/BF01874149. [DOI] [PubMed] [Google Scholar]
- Higgins D. G., Sharp P. M. Fast and sensitive multiple sequence alignments on a microcomputer. Comput Appl Biosci. 1989 Apr;5(2):151–153. doi: 10.1093/bioinformatics/5.2.151. [DOI] [PubMed] [Google Scholar]
- Hightower L. E. Heat shock, stress proteins, chaperones, and proteotoxicity. Cell. 1991 Jul 26;66(2):191–197. doi: 10.1016/0092-8674(91)90611-2. [DOI] [PubMed] [Google Scholar]
- Hightower R. C., Meagher R. B. The molecular evolution of actin. Genetics. 1986 Sep;114(1):315–332. doi: 10.1093/genetics/114.1.315. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hiromi Y., Hotta Y. Actin gene mutations in Drosophila; heat shock activation in the indirect flight muscles. EMBO J. 1985 Jul;4(7):1681–1687. doi: 10.1002/j.1460-2075.1985.tb03837.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hiromi Y., Okamoto H., Gehring W. J., Hotta Y. Germline transformation with Drosophila mutant actin genes induces constitutive expression of heat shock genes. Cell. 1986 Jan 31;44(2):293–301. doi: 10.1016/0092-8674(86)90763-4. [DOI] [PubMed] [Google Scholar]
- Hirono M., Kumagai Y., Numata O., Watanabe Y. Purification of Tetrahymena actin reveals some unusual properties. Proc Natl Acad Sci U S A. 1989 Jan;86(1):75–79. doi: 10.1073/pnas.86.1.75. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Holmes K. C., Popp D., Gebhard W., Kabsch W. Atomic model of the actin filament. Nature. 1990 Sep 6;347(6288):44–49. doi: 10.1038/347044a0. [DOI] [PubMed] [Google Scholar]
- Hue H. K., Labbé J. P., Harricane M. C., Cavadore J. C., Benyamin Y., Roustan C. Structural and functional variations in skeletal-muscle and scallop muscle actins. Biochem J. 1988 Dec 15;256(3):853–859. doi: 10.1042/bj2560853. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Huffaker T. C., Hoyt M. A., Botstein D. Genetic analysis of the yeast cytoskeleton. Annu Rev Genet. 1987;21:259–284. doi: 10.1146/annurev.ge.21.120187.001355. [DOI] [PubMed] [Google Scholar]
- Johannes F. J., Gallwitz D. Site-directed mutagenesis of the yeast actin gene: a test for actin function in vivo. EMBO J. 1991 Dec;10(12):3951–3958. doi: 10.1002/j.1460-2075.1991.tb04965.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Johara M., Toyoshima Y. Y., Ishijima A., Kojima H., Yanagida T., Sutoh K. Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2127–2131. doi: 10.1073/pnas.90.6.2127. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Just I., Hennessey E. S., Drummond D. R., Aktories K., Sparrow J. C. ADP-ribosylation of Drosophila indirect-flight-muscle actin and arthrin by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. Biochem J. 1993 Apr 15;291(Pt 2):409–412. doi: 10.1042/bj2910409. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KASAI M., NAKANO E., OOSAWA F. POLYMERIZATION OF ACTIN FREE FROM NUCLEOTIDES AND DIVALENT CATIONS. Biochim Biophys Acta. 1965 Mar 29;94:494–503. doi: 10.1016/0926-6585(65)90058-0. [DOI] [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]
- Kabsch W., Vandekerckhove J. Structure and function of actin. Annu Rev Biophys Biomol Struct. 1992;21:49–76. doi: 10.1146/annurev.bb.21.060192.000405. [DOI] [PubMed] [Google Scholar]
- Karlik C. C., Coutu M. D., Fyrberg E. A. A nonsense mutation within the act88F actin gene disrupts myofibril formation in Drosophila indirect flight muscles. Cell. 1984 Oct;38(3):711–719. doi: 10.1016/0092-8674(84)90266-6. [DOI] [PubMed] [Google Scholar]
- Karlik C. C., Saville D. L., Fyrberg E. A. Two missense alleles of the Drosophila melanogaster act88F actin gene are strongly antimorphic but only weakly induce synthesis of heat shock proteins. Mol Cell Biol. 1987 Sep;7(9):3084–3091. doi: 10.1128/mcb.7.9.3084. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Karlsson R., Aspenström P., Byström A. S. A chicken beta-actin gene can complement a disruption of the Saccharomyces cerevisiae ACT1 gene. Mol Cell Biol. 1991 Jan;11(1):213–217. doi: 10.1128/mcb.11.1.213. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Karlsson R. Expression of chicken beta-actin in Saccharomyces cerevisiae. Gene. 1988 Sep 7;68(2):249–257. doi: 10.1016/0378-1119(88)90027-3. [DOI] [PubMed] [Google Scholar]
- Kasai M., Oosawa F. The exchangeability of actin-bound calcium with various divalent cations. Biochim Biophys Acta. 1968 Apr 9;154(3):520–528. doi: 10.1016/0005-2795(68)90012-3. [DOI] [PubMed] [Google Scholar]
- Kenyon C. The nematode Caenorhabditis elegans. Science. 1988 Jun 10;240(4858):1448–1453. doi: 10.1126/science.3287621. [DOI] [PubMed] [Google Scholar]
- Khaitlina SYu Polymerization of beta-like actin from scallop adductor muscle. FEBS Lett. 1986 Mar 31;198(2):221–224. doi: 10.1016/0014-5793(86)80409-4. [DOI] [PubMed] [Google Scholar]
- Korn E. D. Actin polymerization and its regulation by proteins from nonmuscle cells. Physiol Rev. 1982 Apr;62(2):672–737. doi: 10.1152/physrev.1982.62.2.672. [DOI] [PubMed] [Google Scholar]
- Korn E. D., Carlier M. F., Pantaloni D. Actin polymerization and ATP hydrolysis. Science. 1987 Oct 30;238(4827):638–644. doi: 10.1126/science.3672117. [DOI] [PubMed] [Google Scholar]
- Krause M., Wild M., Rosenzweig B., Hirsh D. Wild-type and mutant actin genes in Caenorhabditis elegans. J Mol Biol. 1989 Aug 5;208(3):381–392. doi: 10.1016/0022-2836(89)90503-2. [DOI] [PubMed] [Google Scholar]
- Kron S. J., Drubin D. G., Botstein D., Spudich J. A. Yeast actin filaments display ATP-dependent sliding movement over surfaces coated with rabbit muscle myosin. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4466–4470. doi: 10.1073/pnas.89.10.4466. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kron S. J., Spudich J. A. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6272–6276. doi: 10.1073/pnas.83.17.6272. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kögler H., Moir A. J., Trayer I. P., Rüegg J. C. Peptide competition of actin activation of myosin-subfragment 1 ATPase by an amino terminal actin fragment. FEBS Lett. 1991 Dec 2;294(1-2):31–34. doi: 10.1016/0014-5793(91)81336-7. [DOI] [PubMed] [Google Scholar]
- Larsson H., Lindberg U. The effect of divalent cations on the interaction between calf spleen profilin and different actins. Biochim Biophys Acta. 1988 Mar 2;953(1):95–105. doi: 10.1016/0167-4838(88)90013-1. [DOI] [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]
- Leavitt J., Bushar G., Kakunaga T., Hamada H., Hirakawa T., Goldman D., Merril C. Variations in expression of mutant beta actin accompanying incremental increases in human fibroblast tumorigenicity. Cell. 1982 Feb;28(2):259–268. doi: 10.1016/0092-8674(82)90344-0. [DOI] [PubMed] [Google Scholar]
- Leavitt J., Gunning P., Kedes L., Jariwalla R. Smooth muscle alpha-action is a transformation-sensitive marker for mouse NIH 3T3 and Rat-2 cells. 1985 Aug 29-Sep 4Nature. 316(6031):840–842. doi: 10.1038/316840a0. [DOI] [PubMed] [Google Scholar]
- Leavitt J., Kakunaga T. Expression of a variant form of actin and additional polypeptide changes following chemical-induced in vitro neoplastic transformation of human fibroblasts. J Biol Chem. 1980 Feb 25;255(4):1650–1661. [PubMed] [Google Scholar]
- Leavitt J., Ng S. Y., Aebi U., Varma M., Latter G., Burbeck S., Kedes L., Gunning P. Expression of transfected mutant beta-actin genes: alterations of cell morphology and evidence for autoregulation in actin pools. Mol Cell Biol. 1987 Jul;7(7):2457–2466. doi: 10.1128/mcb.7.7.2457. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lees-Miller J. P., Helfman D. M., Schroer T. A. A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility. Nature. 1992 Sep 17;359(6392):244–246. doi: 10.1038/359244a0. [DOI] [PubMed] [Google Scholar]
- Lees-Miller J. P., Henry G., Helfman D. M. Identification of act2, an essential gene in the fission yeast Schizosaccharomyces pombe that encodes a protein related to actin. Proc Natl Acad Sci U S A. 1992 Jan 1;89(1):80–83. doi: 10.1073/pnas.89.1.80. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lindquist S., Craig E. A. The heat-shock proteins. Annu Rev Genet. 1988;22:631–677. doi: 10.1146/annurev.ge.22.120188.003215. [DOI] [PubMed] [Google Scholar]
- Mahaffey J. W., Coutu M. D., Fyrberg E. A., Inwood W. The flightless Drosophila mutant raised has two distinct genetic lesions affecting accumulation of myofibrillar proteins in flight muscles. Cell. 1985 Jan;40(1):101–110. doi: 10.1016/0092-8674(85)90313-7. [DOI] [PubMed] [Google Scholar]
- Mannherz H. G., Gooch J., Way M., Weeds A. G., McLaughlin P. J. Crystallization of the complex of actin with gelsolin segment 1. J Mol Biol. 1992 Aug 5;226(3):899–901. doi: 10.1016/0022-2836(92)90641-v. [DOI] [PubMed] [Google Scholar]
- Manstein D. J., Ruppel K. M., Kubalek L., Spudich J. A. Manipulation and expression of molecular motors in Dictyostelium discoideum. J Cell Sci Suppl. 1991;14:63–65. doi: 10.1242/jcs.1991.supplement_14.13. [DOI] [PubMed] [Google Scholar]
- Manstein D. J., Titus M. A., De Lozanne A., Spudich J. A. Gene replacement in Dictyostelium: generation of myosin null mutants. EMBO J. 1989 Mar;8(3):923–932. doi: 10.1002/j.1460-2075.1989.tb03453.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Masters C. Interactions between glycolytic enzymes and components of the cytomatrix. J Cell Biol. 1984 Jul;99(1 Pt 2):222s–225s. doi: 10.1083/jcb.99.1.222s. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Matsudaira P. Modular organization of actin crosslinking proteins. Trends Biochem Sci. 1991 Mar;16(3):87–92. doi: 10.1016/0968-0004(91)90039-x. [DOI] [PubMed] [Google Scholar]
- Mauss S., Chaponnier C., Just I., Aktories K., Gabbiani G. ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. Eur J Biochem. 1990 Nov 26;194(1):237–241. doi: 10.1111/j.1432-1033.1990.tb19448.x. [DOI] [PubMed] [Google Scholar]
- McElroy D., Rothenberg M., Reece K. S., Wu R. Characterization of the rice (Oryza sativa) actin gene family. Plant Mol Biol. 1990 Aug;15(2):257–268. doi: 10.1007/BF00036912. [DOI] [PubMed] [Google Scholar]
- McKenna N., Meigs J. B., Wang Y. L. Identical distribution of fluorescently labeled brain and muscle actins in living cardiac fibroblasts and myocytes. J Cell Biol. 1985 Jan;100(1):292–296. doi: 10.1083/jcb.100.1.292. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Meagher R. B. Divergence and differential expression of actin gene families in higher plants. Int Rev Cytol. 1991;125:139–163. doi: 10.1016/s0074-7696(08)61218-8. [DOI] [PubMed] [Google Scholar]
- Meza I., Sabanero M., Cazares F., Bryan J. Isolation and characterization of actin from Entamoeba histolytica. J Biol Chem. 1983 Mar 25;258(6):3936–3941. [PubMed] [Google Scholar]
- Miller L. K. Baculoviruses as gene expression vectors. Annu Rev Microbiol. 1988;42:177–199. doi: 10.1146/annurev.mi.42.100188.001141. [DOI] [PubMed] [Google Scholar]
- Mimura N., Asano A. Further characterization of a conserved actin-binding 27-kDa fragment of actinogelin and alpha-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking. J Biol Chem. 1987 Apr 5;262(10):4717–4723. [PubMed] [Google Scholar]
- Miwa T., Manabe Y., Kurokawa K., Kamada S., Kanda N., Bruns G., Ueyama H., Kakunaga T. Structure, chromosome location, and expression of the human smooth muscle (enteric type) gamma-actin gene: evolution of six human actin genes. Mol Cell Biol. 1991 Jun;11(6):3296–3306. doi: 10.1128/mcb.11.6.3296. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mogami K., Hotta Y. Isolation of Drosophila flightless mutants which affect myofibrillar proteins of indirect flight muscle. Mol Gen Genet. 1981;183(3):409–417. doi: 10.1007/BF00268758. [DOI] [PubMed] [Google Scholar]
- Mossakowska M., Strzelecka-Gołaszewska H. Identification of amino acid substitutions differentiating actin isoforms in their interaction with myosin. Eur J Biochem. 1985 Dec 2;153(2):373–381. doi: 10.1111/j.1432-1033.1985.tb09313.x. [DOI] [PubMed] [Google Scholar]
- Mounier N., Gouy M., Mouchiroud D., Prudhomme J. C. Insect muscle actins differ distinctly from invertebrate and vertebrate cytoplasmic actins. J Mol Evol. 1992 May;34(5):406–415. doi: 10.1007/BF00162997. [DOI] [PubMed] [Google Scholar]
- Nairn C. J., Winesett L., Ferl R. J. Nucleotide sequence of an actin gene from Arabidopsis thaliana. Gene. 1988 May 30;65(2):247–257. doi: 10.1016/0378-1119(88)90461-1. [DOI] [PubMed] [Google Scholar]
- Ng R., Abelson J. Isolation and sequence of the gene for actin in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1980 Jul;77(7):3912–3916. doi: 10.1073/pnas.77.7.3912. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Noegel A. A., Leiting B., Witke W., Gurniak C., Harloff C., Hartmann H., Wiesmüller E., Schleicher M. Biological roles of actin-binding proteins in Dictyostelium discoideum examined using genetic techniques. Cell Motil Cytoskeleton. 1989;14(1):69–74. doi: 10.1002/cm.970140114. [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]
- Ohmori H., Toyama S., Toyama S. Direct proof that the primary site of action of cytochalasin on cell motility processes is actin. J Cell Biol. 1992 Feb;116(4):933–941. doi: 10.1083/jcb.116.4.933. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ohshima S., Abe H., Obinata T. Isolation of profilin from embryonic chicken skeletal muscle and evaluation of its interaction with different actin isoforms. J Biochem. 1989 Jun;105(6):855–857. doi: 10.1093/oxfordjournals.jbchem.a122765. [DOI] [PubMed] [Google Scholar]
- Okamoto H., Hiromi Y., Ishikawa E., Yamada T., Isoda K., Maekawa H., Hotta Y. Molecular characterization of mutant actin genes which induce heat-shock proteins in Drosophila flight muscles. EMBO J. 1986 Mar;5(3):589–596. doi: 10.1002/j.1460-2075.1986.tb04251.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Otey C. A., Kalnoski M. H., Bulinski J. C. Immunolocalization of muscle and nonmuscle isoforms of actin in myogenic cells and adult skeletal muscle. Cell Motil Cytoskeleton. 1988;9(4):337–348. doi: 10.1002/cm.970090406. [DOI] [PubMed] [Google Scholar]
- Parker-Thornburg J., Bonner J. J. Mutations that induce the heat shock response of Drosophila. Cell. 1987 Dec 4;51(5):763–772. doi: 10.1016/0092-8674(87)90099-7. [DOI] [PubMed] [Google Scholar]
- Peckham M., Molloy J. E., Sparrow J. C., White D. C. Physiological properties of the dorsal longitudinal flight muscle and the tergal depressor of the trochanter muscle of Drosophila melanogaster. J Muscle Res Cell Motil. 1990 Jun;11(3):203–215. doi: 10.1007/BF01843574. [DOI] [PubMed] [Google Scholar]
- Peng I., Fischman D. A. Post-translational incorporation of actin into myofibrils in vitro: evidence for isoform specificity. Cell Motil Cytoskeleton. 1991;20(2):158–168. doi: 10.1002/cm.970200208. [DOI] [PubMed] [Google Scholar]
- Perriard J. C., von Arx P., Bantle S., Eppenberger H. M., Eppenberger-Eberhardt M., Messerli M., Soldati T. Molecular analysis of protein sorting during biogenesis of muscle cytoarchitecture. Symp Soc Exp Biol. 1992;46:219–235. [PubMed] [Google Scholar]
- Pollard T. D. Actin. Curr Opin Cell Biol. 1990 Feb;2(1):33–40. doi: 10.1016/s0955-0674(05)80028-6. [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]
- Pròchniewicz E., Yanagida T. Comparison of intermonomer interactions within polymers of chicken gizzard and rabbit skeletal muscle actins. J Biochem. 1981 Apr;89(4):1215–1221. [PubMed] [Google Scholar]
- Redman K. L., Martin D. J., Korn E. D., Rubenstein P. A. Lack of NH2-terminal processing of actin from Acanthamoeba castellanii. J Biol Chem. 1985 Nov 25;260(27):14857–14861. [PubMed] [Google Scholar]
- Redman K., Rubenstein P. A. NH2-terminal processing of Dictyostelium discoideum actin in vitro. J Biol Chem. 1981 Dec 25;256(24):13226–13229. [PubMed] [Google Scholar]
- Reedy M. C., Beall C., Fyrberg E. Formation of reverse rigor chevrons by myosin heads. Nature. 1989 Jun 8;339(6224):481–483. doi: 10.1038/339481a0. [DOI] [PubMed] [Google Scholar]
- Rubenstein P. A., Solomon L. R., Solomon T., Gay L. Actin structure-function relationships in vitro using oligodeoxynucleotide-directed site-specific mutagenesis. Cell Motil Cytoskeleton. 1989;14(1):35–39. doi: 10.1002/cm.970140108. [DOI] [PubMed] [Google Scholar]
- Rubenstein P. A. The functional importance of multiple actin isoforms. Bioessays. 1990 Jul;12(7):309–315. doi: 10.1002/bies.950120702. [DOI] [PubMed] [Google Scholar]
- Rubenstein P., Ruppert T., Sandra A. Selective isoactin release from cultured embryonic skeletal muscle cells. J Cell Biol. 1982 Jan;92(1):164–169. doi: 10.1083/jcb.92.1.164. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rubenstein P., Smith P., Deuchler J., Redman K. NH2-terminal acetylation of Dictyostelium discoideum actin in a cell-free protein-synthesizing system. J Biol Chem. 1981 Aug 10;256(15):8149–8155. [PubMed] [Google Scholar]
- Saborío J. L., Palmer E. Brain actin synthesized in vitro undergoes two different and sequential posttranslational modifications. J Neurochem. 1981 May;36(5):1659–1669. doi: 10.1111/j.1471-4159.1981.tb00416.x. [DOI] [PubMed] [Google Scholar]
- Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol. 1987 Jul;4(4):406–425. doi: 10.1093/oxfordjournals.molbev.a040454. [DOI] [PubMed] [Google Scholar]
- Sakai Y., Okamoto H., Mogami K., Matsuo H., Hotta Y. Heat shock gene activation by mutant actin is independent of myofibril degeneration in Drosophila muscle. J Biochem. 1991 May;109(5):670–673. doi: 10.1093/oxfordjournals.jbchem.a123438. [DOI] [PubMed] [Google Scholar]
- Sakai Y., Okamoto H., Mogami K., Yamada T., Hotta Y. Actin with tumor-related mutation is antimorphic in Drosophila muscle: two distinct modes of myofibrillar disruption by antimorphic actins. J Biochem. 1990 Mar;107(3):499–505. doi: 10.1093/oxfordjournals.jbchem.a123074. [DOI] [PubMed] [Google Scholar]
- Schering B., Bärmann M., Chhatwal G. S., Geipel U., Aktories K. ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin. Eur J Biochem. 1988 Jan 15;171(1-2):225–229. doi: 10.1111/j.1432-1033.1988.tb13780.x. [DOI] [PubMed] [Google Scholar]
- Schutt C. E., Lindberg U., Myslik J., Strauss N. Molecular packing in profilin: actin crystals and its implications. J Mol Biol. 1989 Oct 20;209(4):735–746. doi: 10.1016/0022-2836(89)90603-7. [DOI] [PubMed] [Google Scholar]
- Schwob E., Martin R. P. New yeast actin-like gene required late in the cell cycle. Nature. 1992 Jan 9;355(6356):179–182. doi: 10.1038/355179a0. [DOI] [PubMed] [Google Scholar]
- Schwyter D. H., Kron S. J., Toyoshima Y. Y., Spudich J. A., Reisler E. Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin. J Cell Biol. 1990 Aug;111(2):465–470. doi: 10.1083/jcb.111.2.465. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sheetz M. P., Painter R. G., Singer S. J. Relationships of the spectrin complex of human erythrocyte membranes to the actomyosins of muscle cells. Biochemistry. 1976 Oct 5;15(20):4486–4492. doi: 10.1021/bi00665a024. [DOI] [PubMed] [Google Scholar]
- Sheff D. R., Rubenstein P. A. Amino-terminal processing of actins mutagenized at the Cys-1 residue. J Biol Chem. 1992 Feb 5;267(4):2671–2678. [PubMed] [Google Scholar]
- Sheff D. R., Rubenstein P. A. Identification of N-acetylmethionine as the product released during the NH2-terminal processing of a pseudo-class I actin. J Biol Chem. 1989 Jul 5;264(19):11491–11496. [PubMed] [Google Scholar]
- Shires A. K., Rubenstein P. A. Nonuniform behavior of multiple isoactins in the same cell is a cell-dependent phenomenon. Cell Motil Cytoskeleton. 1989;14(2):263–270. doi: 10.1002/cm.970140212. [DOI] [PubMed] [Google Scholar]
- Shortle D., Haber J. E., Botstein D. Lethal disruption of the yeast actin gene by integrative DNA transformation. Science. 1982 Jul 23;217(4557):371–373. doi: 10.1126/science.7046050. [DOI] [PubMed] [Google Scholar]
- Shortle D., Novick P., Botstein D. Construction and genetic characterization of temperature-sensitive mutant alleles of the yeast actin gene. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4889–4893. doi: 10.1073/pnas.81.15.4889. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Skalli O., Gabbiani F., Gabbiani G. Action of general and alpha-smooth muscle-specific actin antibody microinjection on stress fibers of cultured smooth muscle cells. Exp Cell Res. 1990 Mar;187(1):119–125. doi: 10.1016/0014-4827(90)90125-t. [DOI] [PubMed] [Google Scholar]
- Solomon L. R., Rubenstein P. A. Studies on the role of actin's N tau-methylhistidine using oligodeoxynucleotide-directed site-specific mutagenesis. J Biol Chem. 1987 Aug 15;262(23):11382–11388. [PubMed] [Google Scholar]
- Solomon T. L., Solomon L. R., Gay L. S., Rubenstein P. A. Studies on the role of actin's aspartic acid 3 and aspartic acid 11 using oligodeoxynucleotide-directed site-specific mutagenesis. J Biol Chem. 1988 Dec 25;263(36):19662–19669. [PubMed] [Google Scholar]
- Sparrow J. C., Drummond D. R., Hennessey E. S., Clayton J. D., Lindegaard F. B. Drosophila actin mutants and the study of myofibrillar assembly and function. Symp Soc Exp Biol. 1992;46:111–129. [PubMed] [Google Scholar]
- Sparrow J., Drummond D., Peckham M., Hennessey E., White D. Protein engineering and the study of muscle contraction in Drosophila flight muscles. J Cell Sci Suppl. 1991;14:73–78. doi: 10.1242/jcs.1991.supplement_14.15. [DOI] [PubMed] [Google Scholar]
- Sparrow J., Reedy M., Ball E., Kyrtatas V., Molloy J., Durston J., Hennessey E., White D. Functional and ultrastructural effects of a missense mutation in the indirect flight muscle-specific actin gene of Drosophila melanogaster. J Mol Biol. 1991 Dec 20;222(4):963–982. doi: 10.1016/0022-2836(91)90588-w. [DOI] [PubMed] [Google Scholar]
- Stranathan M., Hastings C., Trinh H., Zimmerman J. L. Molecular evolution of two actin genes from carrot. Plant Mol Biol. 1989 Oct;13(4):375–383. doi: 10.1007/BF00015549. [DOI] [PubMed] [Google Scholar]
- Strzelecka-Golaszewska H., Sobieszek A. Activation of smooth muscle myosin by smooth and skeletal muscle actins. FEBS Lett. 1981 Nov 16;134(2):197–202. doi: 10.1016/0014-5793(81)80601-1. [DOI] [PubMed] [Google Scholar]
- Strzelecka-Gołaszewska H., Venyaminov SYu, Zmorzynski S., Mossakowska M. Effects of various amino acid replacements on the conformational stability of G-actin. Eur J Biochem. 1985 Mar 1;147(2):331–342. doi: 10.1111/j.1432-1033.1985.tb08754.x. [DOI] [PubMed] [Google Scholar]
- Strzelecka-Gołaszewska H., Zmorzyński S., Mossakowska M. Bovine aorta actin. Development of an improved purification procedure and comparison of polymerization properties with actins from other types of muscle. Biochim Biophys Acta. 1985 Mar 22;828(1):13–21. doi: 10.1016/0167-4838(85)90003-2. [DOI] [PubMed] [Google Scholar]
- Sussman D. J., Sellers J. R., Flicker P., Lai E. Y., Cannon L. E., Szent-Györgyi A. G., Fulton C. Actin of Naegleria gruberi. Absence of N tau-methylhistidine. J Biol Chem. 1984 Jun 10;259(11):7349–7354. [PubMed] [Google Scholar]
- Sutoh K., Ando M., Sutoh K., Toyoshima Y. Y. Site-directed mutations of Dictyostelium actin: disruption of a negative charge cluster at the N terminus. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7711–7714. doi: 10.1073/pnas.88.17.7711. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sutoh K. Identification of myosin-binding sites on the actin sequence. Biochemistry. 1982 Jul 20;21(15):3654–3661. doi: 10.1021/bi00258a020. [DOI] [PubMed] [Google Scholar]
- Taniguchi S., Kawano T., Kakunaga T., Baba T. Differences in expression of a variant actin between low and high metastatic B16 melanoma. J Biol Chem. 1986 May 5;261(13):6100–6106. [PubMed] [Google Scholar]
- Taniguchi S., Sagara J., Kakunaga T. Deficient polymerization in vitro of a point-mutated beta-actin expressed in a transformed human fibroblast cell line. J Biochem. 1988 Apr;103(4):707–713. doi: 10.1093/oxfordjournals.jbchem.a122333. [DOI] [PubMed] [Google Scholar]
- Tobin S. L., Zulauf E., Sánchez F., Craig E. A., McCarthy B. J. Multiple actin-related sequences in the Drosophila melanogaster genome. Cell. 1980 Jan;19(1):121–131. doi: 10.1016/0092-8674(80)90393-1. [DOI] [PubMed] [Google Scholar]
- Trayer I. P., Trayer H. R., Levine B. A. Evidence that the N-terminal region of A1-light chain of myosin interacts directly with the C-terminal region of actin. A proton magnetic resonance study. Eur J Biochem. 1987 Apr 1;164(1):259–266. doi: 10.1111/j.1432-1033.1987.tb11019.x. [DOI] [PubMed] [Google Scholar]
- Uyemura D. G., Brown S. S., Spudich J. A. Biochemical and structural characterization of actin from Dictyostelium discoideum. J Biol Chem. 1978 Dec 25;253(24):9088–9096. [PubMed] [Google Scholar]
- Van Eyk J. E., Hodges R. S. A synthetic peptide of the N-terminus of actin interacts with myosin. Biochemistry. 1991 Dec 17;30(50):11676–11682. doi: 10.1021/bi00114a010. [DOI] [PubMed] [Google Scholar]
- Vandekerckhove J. S., Kaiser D. A., Pollard T. D. Acanthamoeba actin and profilin can be cross-linked between glutamic acid 364 of actin and lysine 115 of profilin. J Cell Biol. 1989 Aug;109(2):619–626. doi: 10.1083/jcb.109.2.619. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vandekerckhove J., Leavitt J., Kakunaga T., Weber K. Coexpression of a mutant beta-actin and the two normal beta- and gamma-cytoplasmic actins in a stably transformed human cell line. Cell. 1980 Dec;22(3):893–899. doi: 10.1016/0092-8674(80)90566-8. [DOI] [PubMed] [Google Scholar]
- Vandekerckhove J., Schering B., Bärmann M., Aktories K. Botulinum C2 toxin ADP-ribosylates cytoplasmic beta/gamma-actin in arginine 177. J Biol Chem. 1988 Jan 15;263(2):696–700. [PubMed] [Google Scholar]
- Vandekerckhove J., Schering B., Bärmann M., Aktories K. Clostridium perfringens iota toxin ADP-ribosylates skeletal muscle actin in Arg-177. FEBS Lett. 1987 Dec 10;225(1-2):48–52. doi: 10.1016/0014-5793(87)81129-8. [DOI] [PubMed] [Google Scholar]
- Vandekerckhove J., Weber K. At least six different actins are expressed in a higher mammal: an analysis based on the amino acid sequence of the amino-terminal tryptic peptide. J Mol Biol. 1978 Dec 25;126(4):783–802. doi: 10.1016/0022-2836(78)90020-7. [DOI] [PubMed] [Google Scholar]
- Vandekerckhove J., Weber K. Vegetative Dictyostelium cells containing 17 actin genes express a single major actin. Nature. 1980 Apr 3;284(5755):475–477. doi: 10.1038/284475a0. [DOI] [PubMed] [Google Scholar]
- Waterston R. H. Molecular genetic approaches to the study of motility in Caenorhabditis elegans. Cell Motil Cytoskeleton. 1989;14(1):136–145. doi: 10.1002/cm.970140123. [DOI] [PubMed] [Google Scholar]
- Weigt C., Schoepper B., Wegner A. Tropomyosin-troponin complex stabilizes the pointed ends of actin filaments against polymerization and depolymerization. FEBS Lett. 1990 Jan 29;260(2):266–268. doi: 10.1016/0014-5793(90)80119-4. [DOI] [PubMed] [Google Scholar]
- Wertman K. F., Drubin D. G. Actin constitution: guaranteeing the right to assemble. Science. 1992 Oct 30;258(5083):759–760. doi: 10.1126/science.1439782. [DOI] [PubMed] [Google Scholar]
- Wertman K. F., Drubin D. G., Botstein D. Systematic mutational analysis of the yeast ACT1 gene. Genetics. 1992 Oct;132(2):337–350. doi: 10.1093/genetics/132.2.337. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Woolley D. E. An actin-like protein from amoebae of dictyostelium discoideum. Arch Biochem Biophys. 1972 Jun;150(2):519–530. doi: 10.1016/0003-9861(72)90070-7. [DOI] [PubMed] [Google Scholar]