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Volumn 8, Issue 2, 1998, Pages 166-176

F-actin-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; F ACTIN;

EID: 0032054640     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80034-1     Document Type: Article
Times cited : (109)

References (91)
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    • of outstanding interest. This paper presents an elegant study of two-headed, smooth muscle myosin molecules in the extended (6S) conformation by cryo-atomic force microscopy. The images are of sufficient resolution and quality to permit interpretation of structural features consistent with the regulatory domains as well as with α-helical coiled-coils. Conformational changes associated with thiophosphorylation of the myosin molecules were also observed.
    • Zhang Y, Shao Z, Somlyo AP, Somlyo AV. Cryo-atomic force microscopy of smooth muscle myosin. of outstanding interest Biophys J. 72:1997;1308-1318 This paper presents an elegant study of two-headed, smooth muscle myosin molecules in the extended (6S) conformation by cryo-atomic force microscopy. The images are of sufficient resolution and quality to permit interpretation of structural features consistent with the regulatory domains as well as with α-helical coiled-coils. Conformational changes associated with thiophosphorylation of the myosin molecules were also observed.
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    • Two-dimensional arrangement of a functional protein by cysteine - Gold interaction: Enzyme activity and characterization of a protein monolayer on a gold substrate
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    • Visualization of caldesmon on smooth muscle thin filaments
    • of outstanding interest. The first direct demonstration of the caldesmon-binding site on smooth muscle thin filaments determined from helical reconstructions of negatively stained specimens. The caldesmon-binding site involves subdomains 1 and 2 of longitudinally associated actin monomers overlapping the so-called 'weak' myosin-binding site. The locations of both caldesmon and tropomyosin in these filaments may explain caldesmon's inhibitory effects on both actomyosin ATPase activity as well as filament severing by gelsolin.
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    • Tomographic three-dimensional reconstruction of insect flight muscle partially relaxed by AMPPNP and ethylene glycol
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    • Crystal structure of a calponin homology domain
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    • The structure of an actin-crosslinking domain from human fimbrin
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    • Goldsmith SC, Pokala N, Shen W, Fedorov AA, Matsudaira P, Almo SC. The structure of an actin-crosslinking domain from human fimbrin. of special interest Nature Struct Biol. 4:1997;708-712 X-ray crystallography was used to determine the structure of the amino-terminal domain (ABD1) of human fimbrin, a member of the calponin homology domain family of actin-crosslinking proteins. Residues previously implicated in actin binding are mapped to the two subdomains comprising ABD1. Their failure to form a single molecular surface leads to the proposal that rearrangements of the subdomains comprising ABD1 may be required for actin binding.
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    • The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation
    • of outstanding interest. The elusive structure of the F-actin-severing protein gelsolin has been determined by X-ray crystallography. This fascinating structure reveals much about the regulation of gelsolin's activities in the absence of calcium and provides support for the view that large-scale conformational changes in gelsolin accompany severing.
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    • Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
    • of special interest. A 'clustered-charged-to-alanine' strategy of mutagenesis was used to probe the regions of yeast cofilin important in actin interactions. The effects of systematic mutations in cofilin were probed using yeast phenotypes and in vitro binding studies. The results contradict the proposal that cofilin and gelsolin domain 1 share a similar actin-binding surface.
    • Lappalainen P, Fedorov EV, Fedorov AA, Almo SC, Drubin DG. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. of special interest EMBO J. 16:1997;5520-5530 A 'clustered-charged-to-alanine' strategy of mutagenesis was used to probe the regions of yeast cofilin important in actin interactions. The effects of systematic mutations in cofilin were probed using yeast phenotypes and in vitro binding studies. The results contradict the proposal that cofilin and gelsolin domain 1 share a similar actin-binding surface.
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    • Evalutaing atomic models of F-actin with an undecagold-tagged phalloidin derivative
    • of outstanding interest. This elegant study uses an undecagold-tagged derivative to map phalloidin's binding site on the actin filament. The authors interpret their results in light of both the Holmes - Lorenz and Schutt - Lindberg F-actin models and find their data to be in strong agreement with the former.
    • Steinmetz MO, Stoffler D, Muller SA, Jahn W, Wolpensinger B, Goldie KN, Engel A, Faulstich H, Aebi U. Evalutaing atomic models of F-actin with an undecagold-tagged phalloidin derivative. of outstanding interest J Mol Biol. 1998; This elegant study uses an undecagold-tagged derivative to map phalloidin's binding site on the actin filament. The authors interpret their results in light of both the Holmes - Lorenz and Schutt - Lindberg F-actin models and find their data to be in strong agreement with the former.
    • (1998) J Mol Biol
    • Steinmetz, M.O.1    Stoffler, D.2    Muller, S.A.3    Jahn, W.4    Wolpensinger, B.5    Goldie, K.N.6    Engel, A.7    Faulstich, H.8    Aebi, U.9


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