DOI: 10.1083/jcb.138.3.559. A Correlative Analysis of Actin Filament Assembly, Structure, and Dynamics

A Correlative Analysis of Actin Filament Assembly, Structure, and Dynamics

10.1083/jcb.138.3.559

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

The effect of the type of metal ion (i.e., Ca2+, Mg2+, or none) bound to the high-affinity divalent cation binding site (HAS) of actin on filament assembly, structure, and dynamics was investigated in the absence and presence of the mushroom toxin phalloidin. In agreement with earlier reports, we found the polymerization reaction of G-actin into F-actin filaments to be tightly controlled by the type of divalent cation residing in its HAS. Moreover, novel polymerization data are presented indicating that LD, a dimer unproductive by itself, does incorporate into growing F-actin filaments. This observation suggests that during actin filament formation, in addition to the obligatory nucleation– condensation pathway involving UD, a productive filament dimer, a facultative, LD-based pathway is implicated whose abundance strongly depends on the exact polymerization conditions chosen. The “ragged” and “branched” filaments observed during the early stages of assembly represent a hallmark of LD incorporation and might be key to producing an actin meshwork capable of rapidly assembling and disassembling in highly motile cells. Hence, LD incorporation into growing actin filaments might provide an additional level of regulation of actin cytoskeleton dynamics. Regarding the structure and mechanical properties of the F-actin filament at steady state, no significant correlation with the divalent cation residing in its HAS was found. However, compared to native filaments, phalloidin-stabilized filaments were stiffer and yielded subtle but significant structural changes. Together, our data indicate that whereas the G-actin conformation is tightly controlled by the divalent cation in its HAS, the F-actin conformation appears more robust than this variation. Hence, we conclude that the structure and dynamics of the Mg–F-actin moiety within the thin filament are not significantly modulated by the cyclic Ca2+ release as it occurs in muscle contraction to regulate the actomyosin interaction via troponin.

Bibliography

Steinmetz, M. O., Goldie, K. N., & Aebi, U. (1997). A Correlative Analysis of Actin Filament Assembly, Structure, and Dynamics. The Journal of Cell Biology, 138(3), 559â574.

Authors 3

Michel O. Steinmetz (first)
Kenneth N. Goldie (additional)
Ueli Aebi (additional)

References 81 Referenced 105

10.1083/jcb.91.2.340 / J Cell Biol / Crystalline actin sheets: their structure and polymorphism by Aebi (1981)
10.1111/j.1749-6632.1986.tb34502.x / Ann NY Acad Sci / The three-dimensional structure of the actin filament revisited by Aebi (1986)
{'key': '2023072823055175900_B3'}
10.1083/jcb.115.3.689 / J Cell Biol / The structural basis for the intrinsic disorder of the F-actin filament: the lateral slipping model by Bremer (1991)
10.1006/jmbi.1994.1617 / J Mol Biol / Towards atomic interpretation of F-actin filament three-dimensional reconstruction by Bremer (1994)
10.1016/S0021-9258(18)47290-0 / J Biol Chem / Actobindin binds with high- affinity to a covalently crosslinked actin dimer by Bubb (1994)
10.1016/S0021-9258(18)47291-2 / J Biol Chem / Actobindin induces the accumulation of actin dimers that neither nucleate polymerization nor self-associate by Bubb (1994)
10.1074/jbc.270.8.3463 / J Biol Chem / Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments by Bubb (1995)
10.1016/S0021-9258(18)52391-7 / J Biol Chem / Actin: protein structure and filament dynamics by Carlier (1991)
10.1016/S0021-9258(18)67454-X / J Biol Chem / Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin by Carlier (1986)
10.1016/S0021-9258(18)67455-1 / J Biol Chem / The effect of Mg2+at the high-affinity and low-affinity sites on the polymerization of actin and associated ATP hydrolysis by Carlier (1986)
10.1006/jsbi.1993.1006 / J Struct Biol / A rotational offset model for two-stranded F-actin by Censullo (1993)
10.1083/jcb.99.2.529 / J Cell Biol / Phalloidin enhances actin assembly by preventing monomer dissociation by Coluccio (1984)
10.1021/bi00278a021 / Biochemistry / Kinetic evidence for a monomer activation step in actin polymerization by Cooper (1983)
10.1007/BF00712034 / J Musc Res Cell Motil / Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization by Cooper (1983)
10.1016/0022-2836(70)90036-7 / J Mol Biol / Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry by DeRosier (1970)
{'key': '2023072823055175900_B17', 'first-page': '172', 'article-title': 'New insights into actin filament dynamics', 'volume': '5', 'author': 'Egelman', 'year': '1995', 'journal-title': 'Curr Opin Cell Biol'} / Curr Opin Cell Biol / New insights into actin filament dynamics by Egelman (1995)
10.1038/307056a0 / Nature (Lond) / X–ray evidence that actin is a 100 Å filament by Egelman (1984)
10.1038/298131a0 / Nature (Lond) / F-actin is a helix with a random variable twist by Egelman (1982)
10.1073/pnas.81.21.6599 / Proc Natl Acad Sci USA / F-actin is intermolecularly crosslinked by N,N′-p-phenylenedimaleimide through Lysine 191 and Cysteine 374 by Elzinga (1984)
10.1016/0958-1669(93)90005-H / Curr Opin Biotechnol / Application of scanning transmission electron microscopy to the study of biological structure by Engel (1993)
10.1038/259686a0 / Nature (Lond) / Effect of temperature and pressure on polymerisation equilibrium of neuronal microtubules by Engelborghs (1976)
10.1021/bi00507a006 / Biochemistry / Mechanism of action of phalloidin on the polymerization of muscle actin by Estes (1981)
10.1016/S0021-9258(18)61137-8 / J Biol Chem / Tight binding of divalent cations to monomeric actin. Binding kinetics support a simplified model by Estes (1987)
10.1007/BF01766455 / J Musc Res Cell Motil / Tightly-bound divalent cation of actin by Estes (1992)
10.1021/bi00305a015 / Biochemistry / Bound-cation exchange affects the lag phase in actin polymerization by Gershman (1984)
10.1016/0167-4838(89)90068-X / Biochim Biophys Acta / Preparation and polymerization properties of monomeric ADP-actin by Gershman (1989)
10.1016/S0006-3495(97)78776-9 / Biophys J / Calcium regulation of skeletal muscle thin filament motility in vivo by Gordon (1997)
10.1021/bi961159k / Biochemistry / Mobility of the NH2-terminal segment of rabbit skeletal muscle F-actin detected by 1H and 19F nuclear magnetic resonance spectroscopy by Heintz (1996)
{'key': '2023072823055175900_B30', 'first-page': '1729', 'article-title': 'X-ray scattering of F-actin and myosin subfragment-1 complex', 'volume': '39', 'author': 'Hartt', 'year': '1980', 'journal-title': 'Fed Proc'} / Fed Proc / X-ray scattering of F-actin and myosin subfragment-1 complex by Hartt (1980)
10.1006/jsbi.1996.0015 / J Struct Biol / Real-time isocontouring and texture mapping meet new challenges in interactive molecular graphics applications by Henn (1996)
10.1111/j.1432-1033.1993.tb18403.x / Eur J Biochem / The actin monomers in the ternary gelsolin:2 actin complex are in an antiparallel orientation by Hesterkamp (1993)
10.1016/S0006-3495(96)79753-9 / Biophys J / Calcium regulation of thin filament movement in an in vitro motility assay by Homsher (1996)
10.1074/jbc.270.19.11437 / J Biol Chem / Flexibility of actin filaments derived from thermal fluctuations by Isambert (1995)
10.1016/0022-2836(77)90020-1 / J Mol Biol / Kinetic analysis of microtubule self-assembly in vitro. by Johnson (1977)
10.1016/S0006-3495(95)80072-X / Biophys J / Conformational changes in subdomain 2 of G-actin: fluorescence probing by dansyl ethylenediamine attached to Gln-41 by Kim (1995)
10.1042/bj1751023 / Biochem J / p-N,N′-phenylenebismaleimide, a specific crosslinking agent for F-actin by Knight (1978)
10.1111/j.1432-1033.1981.tb06167.x / Eur J Biochem / Fluorimetry study of N-(1-Pyrenyl)iodoacetamide-labeled F-actin by Kouyama (1981)
{'key': '2023072823055175900_B39'}
10.1006/jmbi.1993.1628 / J Mol Biol / Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm by Lorenz (1993)
10.1002/j.1460-2075.1988.tb02821.x / EMBO (Eur Mol Biol Organ) J / Dynamics of the microtubule oscillator: role of nucleotides and tubulin-MAP interactions by Mandelkow (1988)
10.1083/jcb.114.5.977 / J Cell Biol / Microtubule dynamics and microtubule caps: a time resolved cryo-electron microscopy study by Mandelkow (1991)
10.1016/0005-2795(81)90074-X / Biochim Biophys Acta / Effects of trace amounts of Ca2+ and Mg2+on the polymerization of actin by Maruyama (1981)
10.1083/jcb.126.2.433 / J Cell Biol / Determination of the α-actinin binding site on actin filaments by cryoelectron microscopy and image analysis by McGough (1994)
10.1016/S0006-291X(88)80723-X / Biochem Biophys Res Commun / Cation binding sites on actin: a structural relationship between antigenic epitopes and cation exchange by Mejean (1988)
10.1038/348217a0 / Nature (Lond) / Molecular structure of F-actin and location of surface binding sites by Milligan (1990)
10.1083/jcb.106.3.785 / J Cell Biol / Probing actin polymerization by intermolecular crosslinking by Millonig (1988)
10.1016/S0021-9258(18)43413-8 / J Biol Chem / Isolation and characterization of covalently crosslinked actin dimer by Mockrin (1981)
10.1016/S0021-9258(18)32851-5 / J Biol Chem / Kinetics of polymerization and ATP hydrolysis of covalently crosslinked actin dimer by Mockrin (1983)
10.1021/bi00327a038 / Biochemistry / Actin oligomers below the critical concentration detected by fluorescence photobleaching recovery by Mozo-Villarias (1985)
10.1016/0304-3991(92)90022-C / Ultramicroscopy / Factors influencing the precision of quantitative scanning transmission electron microscopy by Müller (1992)
10.1021/bi00327a037 / Biochemistry / Presence of oligomers at subcritical actin concentrations by Newman (1985)
10.1016/0022-2836(92)90520-T / J Mol Biol / Structural basis for the destabilization of F-actin by phosphate release following ATP-hydrolysis by Orlova (1992)
10.1006/jmbi.1993.1393 / J Mol Biol / A conformational change in the actin subunit can change the flexibility of the actin filament by Orlova (1993)
10.1006/jmbi.1996.0761 / J Mol Biol / Cooperativity rigor binding of myosin to actin is a function of F-actin structure by Orlova (1997)
10.1006/jmbi.1994.0049 / J Mol Biol / Structural dynamics of F-actin: II. Cooperativity in structural transitions by Orlova (1995)
10.1083/jcb.123.2.337 / J Cell Biol / A 13-Å map of the actin-scruin filament from the limulus acrosomal process by Owen (1993)
10.1083/jcb.103.6.2747 / J Cell Biol / Rate constant for the reactions of ATP- and ADP-actin with the ends of actin filaments by Pollard (1986)
10.1016/S0955-0674(05)80028-6 / Curr Opin Cell Biol / Actin by Pollard (1990)
10.1006/jmbi.1996.0435 / J Mol Biol / Cooperativity in F-actin: binding of gelsolin at the barbed end affects structure and dynamics of the whole filament by Prochniewicz (1996)
10.1006/jsbi.1996.0035 / J Struct Biol / Semper: distortion compensation, selective averaging, 3-D reconstruction, and transfer function correction in a highly programmable system by Saxton (1996)
10.1016/0167-4838(95)00186-5 / Biochim Biophys Acta / Mg- and Ca-actin filaments appear virtually identical in steady state as determined by dynamic light scattering by Scharf (1995)
10.1016/0006-291X(83)90548-X / Biochem Biophys Res Commun / The tightly-bound divalent cation regulates actin polymerization by Selden (1983)
10.1007/BF01753554 / J Musc Res Cell Motil / Kinetic comparison between Mg-actin and Ca-actin by Selden (1986)
{'key': '2023072823055175900_B65', 'first-page': '1627', 'article-title': 'Computer generated Fourier transforms of helical particles', 'volume': '7', 'author': 'Smith', 'year': '1974', 'journal-title': 'J Phys A Gen Phys'} / J Phys A Gen Phys / Computer generated Fourier transforms of helical particles by Smith (1974)
10.1006/jsbi.1996.0007 / J Struct Biol / The micrograph data processing program by Smith (1996)
10.1016/0022-2836(76)90083-8 / J Mol Biol / Studies on the structure of the bacteriophage T4 tail sheath. I. The recovery of 3-D structural information from the extended sheath by Smith (1976)
10.1016/0304-3991(84)90062-7 / Ultramicroscopy / Toward an alignment of the actin molecule in the actin filament by Smith (1984)
10.1016/S0021-9258(18)62016-2 / J Biol Chem / The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of tropomyosin-troponin complex with actin and the proteolytic fragments of myosin by Spudich (1971)
10.1016/0022-2836(88)90246-X / J Mol Biol / Molecular substructure of a viral receptor-recognition protein. The gp 17 tail-fibre of bacteriophage T7 by Steven (1988)
10.1083/jcb.104.4.1005 / J Cell Biol / The variable twist of actin and its modulation by actin-binding proteins by Stokes (1987)
10.1111/j.1432-1033.1993.tb17603.x / Eur J Biochem / Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion by Strzelecka-Golaszewska (1993)
10.1042/bj3160713 / Biochem J / Effects of the type of divalent cation, Ca2+ or Mg2+, bound at the high-affinity site and on the ionic composition of the solution on the structure of F-actin by Strzelecka-Golaszewska (1996)
10.1021/bi00256a027 / Biochemistry / Cytochalasin D and platelet gelsolin accelerate actin polymer formation. A model for regulation of the extent of actin polymer formation in vivo. by Tellam (1982)
10.1016/S0021-9258(18)32850-3 / J Biol Chem / The kinetics of actin nucleation and polymerization by Tobacman (1983)
10.1016/S0021-9258(20)89500-3 / J Biol Chem / Role of ATP-bound divalent metal ion in the conformation and function of actin by Valentin-Ranc (1991)
10.3109/10409237809149870 / CRC Crit Rev Biochem / Amatoxins, phallotoxins, phallolysin, and antamanide: the biologically active components of poisonous Amanitamushrooms by Wieland (1978)
10.1016/S0022-5320(68)80048-6 / J Ultrastruct Res / The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy by Wrighley (1968)
10.1016/0022-2836(78)90056-6 / J Mol Biol / Polarized fluorescence from ε-ADP incorporation into F-actin in a myosin-free single fibre: conformation of F-actin and changes induced in it by heavy meromyosin by Yanagida (1978)
10.1006/jmbi.1996.0571 / J Mol Biol / Direct measurement of the torsional rigidity of single actin filaments by Yasuda (1996)
10.1021/bi00420a026 / Biochemistry / pH-induced changes in G-actin conformation and metal affinity by Zimmerle (1988)

Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 12:47 p.m.)
Deposited	2 years, 1 month ago (July 28, 2023, 7:07 p.m.)
Indexed	1 month, 2 weeks ago (July 8, 2025, 7:29 a.m.)
Issued	28 years ago (Aug. 11, 1997)
Published	28 years ago (Aug. 11, 1997)
Published Online	28 years ago (Aug. 11, 1997)
Published Print	28 years ago (Aug. 11, 1997)

Funders 0

None

BibTeX

@article{Steinmetz_1997, title={A Correlative Analysis of Actin Filament Assembly, Structure, and Dynamics}, volume={138}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.138.3.559}, DOI={10.1083/jcb.138.3.559}, number={3}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Steinmetz, Michel O. and Goldie, Kenneth N. and Aebi, Ueli}, year={1997}, month=aug, pages={559–574} }

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  "abstract": "<jats:p>The effect of the type of metal ion (i.e., Ca2+, Mg2+, or none) bound to the high-affinity divalent cation binding site (HAS) of actin on filament assembly, structure, and dynamics was investigated in the absence and presence of the mushroom toxin phalloidin. In agreement with earlier reports, we found the polymerization reaction of G-actin into F-actin filaments to be tightly controlled by the type of divalent cation residing in its HAS. Moreover, novel polymerization data are presented indicating that LD, a dimer unproductive by itself, does incorporate into growing F-actin filaments. This observation suggests that during actin filament formation, in addition to the obligatory nucleation\u2013 condensation pathway involving UD, a productive filament dimer, a facultative, LD-based pathway is implicated whose abundance strongly depends on the exact polymerization conditions chosen. The \u201cragged\u201d and \u201cbranched\u201d filaments observed during the early stages of assembly represent a hallmark of LD incorporation and might be key to producing an actin meshwork capable of rapidly assembling and disassembling in highly motile cells. Hence, LD incorporation into growing actin filaments might provide an additional level of regulation of actin cytoskeleton dynamics. Regarding the structure and mechanical properties of the F-actin filament at steady state, no significant correlation with the divalent cation residing in its HAS was found. However, compared to native filaments, phalloidin-stabilized filaments were stiffer and yielded subtle but significant structural changes. Together, our data indicate that whereas the G-actin conformation is tightly controlled by the divalent cation in its HAS, the F-actin conformation appears more robust than this variation. Hence, we conclude that the structure and dynamics of the Mg\u2013F-actin moiety within the thin filament are not significantly modulated by the cyclic Ca2+ release as it occurs in muscle contraction to regulate the actomyosin interaction via troponin.</jats:p>",
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      "first-page": "340",
      "DOI": "10.1083/jcb.91.2.340",
      "article-title": "Crystalline actin sheets: their structure and polymorphism",
      "volume": "91",
      "author": "Aebi",
      "year": "1981",
      "journal-title": "J Cell Biol"
    },
    {
      "key": "2023072823055175900_B2",
      "doi-asserted-by": "crossref",
      "first-page": "100",
      "DOI": "10.1111/j.1749-6632.1986.tb34502.x",
      "article-title": "The three-dimensional structure of the actin filament revisited",
      "volume": "483",
      "author": "Aebi",
      "year": "1986",
      "journal-title": "Ann NY Acad Sci"
    },
    {
      "key": "2023072823055175900_B3"
    },
    {
      "key": "2023072823055175900_B4",
      "doi-asserted-by": "crossref",
      "first-page": "689",
      "DOI": "10.1083/jcb.115.3.689",
      "article-title": "The structural basis for the intrinsic disorder of the F-actin filament: the lateral slipping model",
      "volume": "115",
      "author": "Bremer",
      "year": "1991",
      "journal-title": "J Cell Biol"
    },
    {
      "key": "2023072823055175900_B5",
      "doi-asserted-by": "crossref",
      "first-page": "683",
      "DOI": "10.1006/jmbi.1994.1617",
      "article-title": "Towards atomic interpretation of F-actin filament three-dimensional reconstruction",
      "volume": "242",
      "author": "Bremer",
      "year": "1994",
      "journal-title": "J Mol Biol"
    },
    {
      "key": "2023072823055175900_B6",
      "doi-asserted-by": "crossref",
      "first-page": "25587",
      "DOI": "10.1016/S0021-9258(18)47290-0",
      "article-title": "Actobindin binds with high- affinity to a covalently crosslinked actin dimer",
      "volume": "269",
      "author": "Bubb",
      "year": "1994",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "2023072823055175900_B7",
      "doi-asserted-by": "crossref",
      "first-page": "25592",
      "DOI": "10.1016/S0021-9258(18)47291-2",
      "article-title": "Actobindin induces the accumulation of actin dimers that neither nucleate polymerization nor self-associate",
      "volume": "269",
      "author": "Bubb",
      "year": "1994",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "2023072823055175900_B8",
      "doi-asserted-by": "crossref",
      "first-page": "3463",
      "DOI": "10.1074/jbc.270.8.3463",
      "article-title": "Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments",
      "volume": "270",
      "author": "Bubb",
      "year": "1995",
      "journal-title": "J Biol Chem"
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      "author": "Carlier",
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      "journal-title": "J Biol Chem"
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      "author": "Coluccio",
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      "volume": "22",
      "author": "Cooper",
      "year": "1983",
      "journal-title": "Biochemistry"
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      "author": "Cooper",
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      "volume": "52",
      "author": "DeRosier",
      "year": "1970",
      "journal-title": "J Mol Biol"
    },
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      "key": "2023072823055175900_B17",
      "first-page": "172",
      "article-title": "New insights into actin filament dynamics",
      "volume": "5",
      "author": "Egelman",
      "year": "1995",
      "journal-title": "Curr Opin Cell Biol"
    },
    {
      "key": "2023072823055175900_B18",
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      "first-page": "56",
      "DOI": "10.1038/307056a0",
      "article-title": "X\u2013ray evidence that actin is a 100 \u00c5 filament",
      "volume": "307",
      "author": "Egelman",
      "year": "1984",
      "journal-title": "Nature (Lond)"
    },
    {
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      "first-page": "131",
      "DOI": "10.1038/298131a0",
      "article-title": "F-actin is a helix with a random variable twist",
      "volume": "298",
      "author": "Egelman",
      "year": "1982",
      "journal-title": "Nature (Lond)"
    },
    {
      "key": "2023072823055175900_B20",
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      "first-page": "6599",
      "DOI": "10.1073/pnas.81.21.6599",
      "article-title": "F-actin is intermolecularly crosslinked by N,N\u2032-p-phenylenedimaleimide through Lysine 191 and Cysteine 374",
      "volume": "81",
      "author": "Elzinga",
      "year": "1984",
      "journal-title": "Proc Natl Acad Sci USA"
    },
    {
      "key": "2023072823055175900_B21",
      "doi-asserted-by": "crossref",
      "first-page": "403",
      "DOI": "10.1016/0958-1669(93)90005-H",
      "article-title": "Application of scanning transmission electron microscopy to the study of biological structure",
      "volume": "4",
      "author": "Engel",
      "year": "1993",
      "journal-title": "Curr Opin Biotechnol"
    },
    {
      "key": "2023072823055175900_B22",
      "doi-asserted-by": "crossref",
      "first-page": "686",
      "DOI": "10.1038/259686a0",
      "article-title": "Effect of temperature and pressure on polymerisation equilibrium of neuronal microtubules",
      "volume": "259",
      "author": "Engelborghs",
      "year": "1976",
      "journal-title": "Nature (Lond)"
    },
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      "key": "2023072823055175900_B23",
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      "first-page": "708",
      "DOI": "10.1021/bi00507a006",
      "article-title": "Mechanism of action of phalloidin on the polymerization of muscle actin",
      "volume": "20",
      "author": "Estes",
      "year": "1981",
      "journal-title": "Biochemistry"
    },
    {
      "key": "2023072823055175900_B24",
      "doi-asserted-by": "crossref",
      "first-page": "4952",
      "DOI": "10.1016/S0021-9258(18)61137-8",
      "article-title": "Tight binding of divalent cations to monomeric actin. Binding kinetics support a simplified model",
      "volume": "262",
      "author": "Estes",
      "year": "1987",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "2023072823055175900_B25",
      "doi-asserted-by": "crossref",
      "first-page": "272",
      "DOI": "10.1007/BF01766455",
      "article-title": "Tightly-bound divalent cation of actin",
      "volume": "13",
      "author": "Estes",
      "year": "1992",
      "journal-title": "J Musc Res Cell Motil"
    },
    {
      "key": "2023072823055175900_B26",
      "doi-asserted-by": "crossref",
      "first-page": "2199",
      "DOI": "10.1021/bi00305a015",
      "article-title": "Bound-cation exchange affects the lag phase in actin polymerization",
      "volume": "23",
      "author": "Gershman",
      "year": "1984",
      "journal-title": "Biochemistry"
    },
    {
      "key": "2023072823055175900_B27",
      "doi-asserted-by": "crossref",
      "first-page": "109",
      "DOI": "10.1016/0167-4838(89)90068-X",
      "article-title": "Preparation and polymerization properties of monomeric ADP-actin",
      "volume": "995",
      "author": "Gershman",
      "year": "1989",
      "journal-title": "Biochim Biophys Acta"
    },
    {
      "key": "2023072823055175900_B28",
      "doi-asserted-by": "crossref",
      "first-page": "1295",
      "DOI": "10.1016/S0006-3495(97)78776-9",
      "article-title": "Calcium regulation of skeletal muscle thin filament motility in vivo",
      "volume": "72",
      "author": "Gordon",
      "year": "1997",
      "journal-title": "Biophys J"
    },
    {
      "key": "2023072823055175900_B29",
      "doi-asserted-by": "crossref",
      "first-page": "12686",
      "DOI": "10.1021/bi961159k",
      "article-title": "Mobility of the NH2-terminal segment of rabbit skeletal muscle F-actin detected by 1H and 19F nuclear magnetic resonance spectroscopy",
      "volume": "35",
      "author": "Heintz",
      "year": "1996",
      "journal-title": "Biochemistry"
    },
    {
      "key": "2023072823055175900_B30",
      "first-page": "1729",
      "article-title": "X-ray scattering of F-actin and myosin subfragment-1 complex",
      "volume": "39",
      "author": "Hartt",
      "year": "1980",
      "journal-title": "Fed Proc"
    },
    {
      "key": "2023072823055175900_B31",
      "doi-asserted-by": "crossref",
      "first-page": "86",
      "DOI": "10.1006/jsbi.1996.0015",
      "article-title": "Real-time isocontouring and texture mapping meet new challenges in interactive molecular graphics applications",
      "volume": "116",
      "author": "Henn",
      "year": "1996",
      "journal-title": "J Struct Biol"
    },
    {
      "key": "2023072823055175900_B32",
      "doi-asserted-by": "crossref",
      "first-page": "507",
      "DOI": "10.1111/j.1432-1033.1993.tb18403.x",
      "article-title": "The actin monomers in the ternary gelsolin:2 actin complex are in an antiparallel orientation",
      "volume": "218",
      "author": "Hesterkamp",
      "year": "1993",
      "journal-title": "Eur J Biochem"
    },
    {
      "key": "2023072823055175900_B33",
      "doi-asserted-by": "crossref",
      "first-page": "1881",
      "DOI": "10.1016/S0006-3495(96)79753-9",
      "article-title": "Calcium regulation of thin filament movement in an in vitro motility assay",
      "volume": "70",
      "author": "Homsher",
      "year": "1996",
      "journal-title": "Biophys J"
    },
    {
      "key": "2023072823055175900_B34",
      "doi-asserted-by": "crossref",
      "first-page": "11437",
      "DOI": "10.1074/jbc.270.19.11437",
      "article-title": "Flexibility of actin filaments derived from thermal fluctuations",
      "volume": "270",
      "author": "Isambert",
      "year": "1995",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "2023072823055175900_B35",
      "doi-asserted-by": "crossref",
      "first-page": "1",
      "DOI": "10.1016/0022-2836(77)90020-1",
      "article-title": "Kinetic analysis of microtubule self-assembly in vitro.",
      "volume": "117",
      "author": "Johnson",
      "year": "1977",
      "journal-title": "J Mol Biol"
    },
    {
      "key": "2023072823055175900_B36",
      "doi-asserted-by": "crossref",
      "first-page": "2024",
      "DOI": "10.1016/S0006-3495(95)80072-X",
      "article-title": "Conformational changes in subdomain 2 of G-actin: fluorescence probing by dansyl ethylenediamine attached to Gln-41",
      "volume": "69",
      "author": "Kim",
      "year": "1995",
      "journal-title": "Biophys J"
    },
    {
      "key": "2023072823055175900_B37",
      "doi-asserted-by": "crossref",
      "first-page": "1023",
      "DOI": "10.1042/bj1751023",
      "article-title": "p-N,N\u2032-phenylenebismaleimide, a specific crosslinking agent for F-actin",
      "volume": "175",
      "author": "Knight",
      "year": "1978",
      "journal-title": "Biochem J"
    },
    {
      "key": "2023072823055175900_B38",
      "doi-asserted-by": "crossref",
      "first-page": "33",
      "DOI": "10.1111/j.1432-1033.1981.tb06167.x",
      "article-title": "Fluorimetry study of N-(1-Pyrenyl)iodoacetamide-labeled F-actin",
      "volume": "114",
      "author": "Kouyama",
      "year": "1981",
      "journal-title": "Eur J Biochem"
    },
    {
      "key": "2023072823055175900_B39"
    },
    {
      "key": "2023072823055175900_B40",
      "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 the use of a directed mutation algorithm",
      "volume": "234",
      "author": "Lorenz",
      "year": "1993",
      "journal-title": "J Mol Biol"
    },
    {
      "key": "2023072823055175900_B41",
      "doi-asserted-by": "crossref",
      "first-page": "357",
      "DOI": "10.1002/j.1460-2075.1988.tb02821.x",
      "article-title": "Dynamics of the microtubule oscillator: role of nucleotides and tubulin-MAP interactions",
      "volume": "7",
      "author": "Mandelkow",
      "year": "1988",
      "journal-title": "EMBO (Eur Mol Biol Organ) J"
    },
    {
      "key": "2023072823055175900_B42",
      "doi-asserted-by": "crossref",
      "first-page": "977",
      "DOI": "10.1083/jcb.114.5.977",
      "article-title": "Microtubule dynamics and microtubule caps: a time resolved cryo-electron microscopy study",
      "volume": "114",
      "author": "Mandelkow",
      "year": "1991",
      "journal-title": "J Cell Biol"
    },
    {
      "key": "2023072823055175900_B43",
      "doi-asserted-by": "crossref",
      "first-page": "139",
      "DOI": "10.1016/0005-2795(81)90074-X",
      "article-title": "Effects of trace amounts of Ca2+ and Mg2+on the polymerization of actin",
      "volume": "667",
      "author": "Maruyama",
      "year": "1981",
      "journal-title": "Biochim Biophys Acta"
    },
    {
      "key": "2023072823055175900_B44",
      "doi-asserted-by": "crossref",
      "first-page": "433",
      "DOI": "10.1083/jcb.126.2.433",
      "article-title": "Determination of the \u03b1-actinin binding site on actin filaments by cryoelectron microscopy and image analysis",
      "volume": "126",
      "author": "McGough",
      "year": "1994",
      "journal-title": "J Cell Biol"
    },
    {
      "key": "2023072823055175900_B45",
      "doi-asserted-by": "crossref",
      "first-page": "365",
      "DOI": "10.1016/S0006-291X(88)80723-X",
      "article-title": "Cation binding sites on actin: a structural relationship between antigenic epitopes and cation exchange",
      "volume": "152",
      "author": "Mejean",
      "year": "1988",
      "journal-title": "Biochem Biophys Res Commun"
    },
    {
      "key": "2023072823055175900_B46",
      "doi-asserted-by": "crossref",
      "first-page": "217",
      "DOI": "10.1038/348217a0",
      "article-title": "Molecular structure of F-actin and location of surface binding sites",
      "volume": "348",
      "author": "Milligan",
      "year": "1990",
      "journal-title": "Nature (Lond)"
    },
    {
      "key": "2023072823055175900_B47",
      "doi-asserted-by": "crossref",
      "first-page": "785",
      "DOI": "10.1083/jcb.106.3.785",
      "article-title": "Probing actin polymerization by intermolecular crosslinking",
      "volume": "106",
      "author": "Millonig",
      "year": "1988",
      "journal-title": "J Cell Biol"
    },
    {
      "key": "2023072823055175900_B48",
      "doi-asserted-by": "crossref",
      "first-page": "8228",
      "DOI": "10.1016/S0021-9258(18)43413-8",
      "article-title": "Isolation and characterization of covalently crosslinked actin dimer",
      "volume": "256",
      "author": "Mockrin",
      "year": "1981",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "2023072823055175900_B49",
      "doi-asserted-by": "crossref",
      "first-page": "3215",
      "DOI": "10.1016/S0021-9258(18)32851-5",
      "article-title": "Kinetics of polymerization and ATP hydrolysis of covalently crosslinked actin dimer",
      "volume": "258",
      "author": "Mockrin",
      "year": "1983",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "2023072823055175900_B50",
      "doi-asserted-by": "crossref",
      "first-page": "1544",
      "DOI": "10.1021/bi00327a038",
      "article-title": "Actin oligomers below the critical concentration detected by fluorescence photobleaching recovery",
      "volume": "24",
      "author": "Mozo-Villarias",
      "year": "1985",
      "journal-title": "Biochemistry"
    },
    {
      "key": "2023072823055175900_B51",
      "doi-asserted-by": "crossref",
      "first-page": "317",
      "DOI": "10.1016/0304-3991(92)90022-C",
      "article-title": "Factors influencing the precision of quantitative scanning transmission electron microscopy",
      "volume": "46",
      "author": "M\u00fcller",
      "year": "1992",
      "journal-title": "Ultramicroscopy"
    },
    {
      "key": "2023072823055175900_B52",
      "doi-asserted-by": "crossref",
      "first-page": "1538",
      "DOI": "10.1021/bi00327a037",
      "article-title": "Presence of oligomers at subcritical actin concentrations",
      "volume": "24",
      "author": "Newman",
      "year": "1985",
      "journal-title": "Biochemistry"
    },
    {
      "key": "2023072823055175900_B53",
      "doi-asserted-by": "crossref",
      "first-page": "1043",
      "DOI": "10.1016/0022-2836(92)90520-T",
      "article-title": "Structural basis for the destabilization of F-actin by phosphate release following ATP-hydrolysis",
      "volume": "227",
      "author": "Orlova",
      "year": "1992",
      "journal-title": "J Mol Biol"
    },
    {
      "key": "2023072823055175900_B54",
      "doi-asserted-by": "crossref",
      "first-page": "334",
      "DOI": "10.1006/jmbi.1993.1393",
      "article-title": "A conformational change in the actin subunit can change the flexibility of the actin filament",
      "volume": "232",
      "author": "Orlova",
      "year": "1993",
      "journal-title": "J Mol Biol"
    },
    {
      "key": "2023072823055175900_B55",
      "doi-asserted-by": "crossref",
      "first-page": "469",
      "DOI": "10.1006/jmbi.1996.0761",
      "article-title": "Cooperativity rigor binding of myosin to actin is a function of F-actin structure",
      "volume": "265",
      "author": "Orlova",
      "year": "1997",
      "journal-title": "J Mol Biol"
    },
    {
      "key": "2023072823055175900_B56",
      "doi-asserted-by": "crossref",
      "first-page": "598",
      "DOI": "10.1006/jmbi.1994.0049",
      "article-title": "Structural dynamics of F-actin: II. Cooperativity in structural transitions",
      "volume": "245",
      "author": "Orlova",
      "year": "1995",
      "journal-title": "J Mol Biol"
    },
    {
      "key": "2023072823055175900_B57",
      "doi-asserted-by": "crossref",
      "first-page": "337",
      "DOI": "10.1083/jcb.123.2.337",
      "article-title": "A 13-\u00c5 map of the actin-scruin filament from the limulus acrosomal process",
      "volume": "123",
      "author": "Owen",
      "year": "1993",
      "journal-title": "J Cell Biol"
    },
    {
      "key": "2023072823055175900_B58",
      "doi-asserted-by": "crossref",
      "first-page": "2747",
      "DOI": "10.1083/jcb.103.6.2747",
      "article-title": "Rate constant for the reactions of ATP- and ADP-actin with the ends of actin filaments",
      "volume": "103",
      "author": "Pollard",
      "year": "1986",
      "journal-title": "J Cell Biol"
    },
    {
      "key": "2023072823055175900_B59",
      "doi-asserted-by": "crossref",
      "first-page": "33",
      "DOI": "10.1016/S0955-0674(05)80028-6",
      "article-title": "Actin",
      "volume": "2",
      "author": "Pollard",
      "year": "1990",
      "journal-title": "Curr Opin Cell Biol"
    },
    {
      "key": "2023072823055175900_B60",
      "doi-asserted-by": "crossref",
      "first-page": "756",
      "DOI": "10.1006/jmbi.1996.0435",
      "article-title": "Cooperativity in F-actin: binding of gelsolin at the barbed end affects structure and dynamics of the whole filament",
      "volume": "260",
      "author": "Prochniewicz",
      "year": "1996",
      "journal-title": "J Mol Biol"
    },
    {
      "key": "2023072823055175900_B61",
      "doi-asserted-by": "crossref",
      "first-page": "230",
      "DOI": "10.1006/jsbi.1996.0035",
      "article-title": "Semper: distortion compensation, selective averaging, 3-D reconstruction, and transfer function correction in a highly programmable system",
      "volume": "116",
      "author": "Saxton",
      "year": "1996",
      "journal-title": "J Struct Biol"
    },
    {
      "key": "2023072823055175900_B62",
      "doi-asserted-by": "crossref",
      "first-page": "129",
      "DOI": "10.1016/0167-4838(95)00186-5",
      "article-title": "Mg- and Ca-actin filaments appear virtually identical in steady state as determined by dynamic light scattering",
      "volume": "1253",
      "author": "Scharf",
      "year": "1995",
      "journal-title": "Biochim Biophys Acta"
    },
    {
      "key": "2023072823055175900_B63",
      "doi-asserted-by": "crossref",
      "first-page": "478",
      "DOI": "10.1016/0006-291X(83)90548-X",
      "article-title": "The tightly-bound divalent cation regulates actin polymerization",
      "volume": "116",
      "author": "Selden",
      "year": "1983",
      "journal-title": "Biochem Biophys Res Commun"
    },
    {
      "key": "2023072823055175900_B64",
      "doi-asserted-by": "crossref",
      "first-page": "215",
      "DOI": "10.1007/BF01753554",
      "article-title": "Kinetic comparison between Mg-actin and Ca-actin",
      "volume": "7",
      "author": "Selden",
      "year": "1986",
      "journal-title": "J Musc Res Cell Motil"
    },
    {
      "key": "2023072823055175900_B65",
      "first-page": "1627",
      "article-title": "Computer generated Fourier transforms of helical particles",
      "volume": "7",
      "author": "Smith",
      "year": "1974",
      "journal-title": "J Phys A Gen Phys"
    },
    {
      "key": "2023072823055175900_B66",
      "doi-asserted-by": "crossref",
      "first-page": "35",
      "DOI": "10.1006/jsbi.1996.0007",
      "article-title": "The micrograph data processing program",
      "volume": "116",
      "author": "Smith",
      "year": "1996",
      "journal-title": "J Struct Biol"
    },
    {
      "key": "2023072823055175900_B67",
      "doi-asserted-by": "crossref",
      "first-page": "243",
      "DOI": "10.1016/0022-2836(76)90083-8",
      "article-title": "Studies on the structure of the bacteriophage T4 tail sheath. I. The recovery of 3-D structural information from the extended sheath",
      "volume": "106",
      "author": "Smith",
      "year": "1976",
      "journal-title": "J Mol Biol"
    },
    {
      "key": "2023072823055175900_B68",
      "doi-asserted-by": "crossref",
      "first-page": "113",
      "DOI": "10.1016/0304-3991(84)90062-7",
      "article-title": "Toward an alignment of the actin molecule in the actin filament",
      "volume": "13",
      "author": "Smith",
      "year": "1984",
      "journal-title": "Ultramicroscopy"
    },
    {
      "key": "2023072823055175900_B69",
      "doi-asserted-by": "crossref",
      "first-page": "4866",
      "DOI": "10.1016/S0021-9258(18)62016-2",
      "article-title": "The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of tropomyosin-troponin complex with actin and the proteolytic fragments of myosin",
      "volume": "246",
      "author": "Spudich",
      "year": "1971",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "2023072823055175900_B70",
      "doi-asserted-by": "crossref",
      "first-page": "351",
      "DOI": "10.1016/0022-2836(88)90246-X",
      "article-title": "Molecular substructure of a viral receptor-recognition protein. The gp 17 tail-fibre of bacteriophage T7",
      "volume": "200",
      "author": "Steven",
      "year": "1988",
      "journal-title": "J Mol Biol"
    },
    {
      "key": "2023072823055175900_B71",
      "doi-asserted-by": "crossref",
      "first-page": "1005",
      "DOI": "10.1083/jcb.104.4.1005",
      "article-title": "The variable twist of actin and its modulation by actin-binding proteins",
      "volume": "104",
      "author": "Stokes",
      "year": "1987",
      "journal-title": "J Cell Biol"
    },
    {
      "key": "2023072823055175900_B72",
      "doi-asserted-by": "crossref",
      "first-page": "731",
      "DOI": "10.1111/j.1432-1033.1993.tb17603.x",
      "article-title": "Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion",
      "volume": "211",
      "author": "Strzelecka-Golaszewska",
      "year": "1993",
      "journal-title": "Eur J Biochem"
    },
    {
      "key": "2023072823055175900_B73",
      "doi-asserted-by": "crossref",
      "first-page": "713",
      "DOI": "10.1042/bj3160713",
      "article-title": "Effects of the type of divalent cation, Ca2+ or Mg2+, bound at the high-affinity site and on the ionic composition of the solution on the structure of F-actin",
      "volume": "316",
      "author": "Strzelecka-Golaszewska",
      "year": "1996",
      "journal-title": "Biochem J"
    },
    {
      "key": "2023072823055175900_B74",
      "doi-asserted-by": "crossref",
      "first-page": "3207",
      "DOI": "10.1021/bi00256a027",
      "article-title": "Cytochalasin D and platelet gelsolin accelerate actin polymer formation. A model for regulation of the extent of actin polymer formation in vivo.",
      "volume": "21",
      "author": "Tellam",
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      "author": "Valentin-Ranc",
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