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1
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0030745347
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Actin: From cell biology to atomic detail
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of special interest. A good recent review on actin, with emphasis on the assembly and structure of the actin filament.
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Steinmetz MO, Stoffler D, Hoenger A, Bremer A, Aebi U. Actin: from cell biology to atomic detail. of special interest J Struct Biol. 119:1997;295-320 A good recent review on actin, with emphasis on the assembly and structure of the actin filament.
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(1997)
J Struct Biol
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Steinmetz, M.O.1
Stoffler, D.2
Hoenger, A.3
Bremer, A.4
Aebi, U.5
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2
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0022555884
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Actin and actin-binding proteins. A critical evaluation of mechanisms and functions
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Pollard TD, Cooper JA. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu Rev Biochem. 55:1986;987-1035.
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Annu Rev Biochem
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Pollard, T.D.1
Cooper, J.A.2
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3
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0030804033
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A correlative analysis of actin filament assembly, structure, and dynamics
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of special interest. A detailed study of actin filament assembly in the presence of metal ions and phalloidin. The proposal is made that polymerization can proceed through an alternative pathway involving so-called 'lower dimers' which contain actin - actin contacts that differ from normal F-actin structure.
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Steinmetz MO, Goldie KN, Aebi U. A correlative analysis of actin filament assembly, structure, and dynamics. of special interest J Cell Biol. 138:1997;559-574 A detailed study of actin filament assembly in the presence of metal ions and phalloidin. The proposal is made that polymerization can proceed through an alternative pathway involving so-called 'lower dimers' which contain actin - actin contacts that differ from normal F-actin structure.
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(1997)
J Cell Biol
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Steinmetz, M.O.1
Goldie, K.N.2
Aebi, U.3
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4
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0031104928
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Cell motility: Complex dynamics at the leading edge
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Machesky LM. Cell motility: complex dynamics at the leading edge. Curr Biol. 7:1997;R164-R167.
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Curr Biol
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MacHesky, L.M.1
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6
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0030982679
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Using explicitly represented biological relationships for database navigation and searching via the World-Wide Web
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of outstanding interest. This paper describes the development of the CySPID database (http://ycmi.med.yale.edu/cyspid) of cytoskeleton protein relationships and interactions. With the number of known actin-binding proteins continuing to grow at such a fantastic pace, the application of medical informatics and other computational approaches aimed at elucidating molecular relationships may soon become a necessity.
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Panzer S, Cooley L, Miller PL. Using explicitly represented biological relationships for database navigation and searching via the World-Wide Web. of outstanding interest Comput Appl Biosci. 13:1997;281-290 This paper describes the development of the CySPID database (http://ycmi.med.yale.edu/cyspid) of cytoskeleton protein relationships and interactions. With the number of known actin-binding proteins continuing to grow at such a fantastic pace, the application of medical informatics and other computational approaches aimed at elucidating molecular relationships may soon become a necessity.
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(1997)
Comput Appl Biosci
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Panzer, S.1
Cooley, L.2
Miller, P.L.3
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7
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0029084972
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Genetic disorders of the red cell membranes
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Delauney J. Genetic disorders of the red cell membranes. FEBS Lett. 369:1995;34-37.
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FEBS Lett
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Delauney, J.1
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8
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85030331928
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note
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http://www.neuro.wustl.edu/neuromuscular This web site, maintained by the Neuromuscular Disease Center, Washington University School of Medicine, St Louis, provides easy to access information about the molecular basis of various diseases. A good starting point for grant proposals.
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10
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0024988340
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Atomic structure of the actin:DNase I complex
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Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC. Atomic structure of the actin:DNase I complex. Nature. 347:1990;37-44.
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Nature
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Kabsch, W.1
Mannherz, H.G.2
Suck, D.3
Pai, E.F.4
Holmes, K.C.5
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11
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0027251071
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Structure of gelsolin segment 1 - Actin complex and the mechanism of severing
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McLaughlin P, Gooch JT, Mannherz M-G, Weeds AG. Structure of gelsolin segment 1 - actin complex and the mechanism of severing. Nature. 364:1993;685-692.
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McLaughlin, P.1
Gooch, J.T.2
Mannherz M-G3
Weeds, A.G.4
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12
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0027426150
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The structure of crystalline profilin - Actin
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Schutt CE, Myslik JC, Rozycki MD, Gooneskere NCW, Lindberg U. The structure of crystalline profilin - actin. Nature. 365:1993;810-816.
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Nature
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Schutt, C.E.1
Myslik, J.C.2
Rozycki, M.D.3
Gooneskere, N.C.W.4
Lindberg, U.5
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13
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0030575783
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The structure of an open state of beta-actin at 2.65 Å resolution
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of special interest. The actin monomer is shown to adopt an 'open state' when cocrystallized with profilin in 1.8 M potassium phosphate. When compared with the other three actin structures determined so far, this form of actin shows large domain movements. In addition to providing dramatic evidence of actin's conformational flexibility, this structure provides insights into profilin's regulatory effects on actin.
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Chik JK, Lindberg U, Schutt CE. The structure of an open state of beta-actin at 2.65 Å resolution. of special interest J Mol Biol. 263:1996;607-623 The actin monomer is shown to adopt an 'open state' when cocrystallized with profilin in 1.8 M potassium phosphate. When compared with the other three actin structures determined so far, this form of actin shows large domain movements. In addition to providing dramatic evidence of actin's conformational flexibility, this structure provides insights into profilin's regulatory effects on actin.
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(1996)
J Mol Biol
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Chik, J.K.1
Lindberg, U.2
Schutt, C.E.3
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15
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0027131941
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Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
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Lorenz M, Popp D, Holmes KC. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J Mol Biol. 234:1993;826-836.
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J Mol Biol
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Lorenz, M.1
Popp, D.2
Holmes, K.C.3
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16
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0027511431
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A normal mode analysis of G-actin
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Tirion MM, Ben-Avraham D. A normal mode analysis of G-actin. J Mol Biol. 230:1993;186-195.
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J Mol Biol
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Tirion, M.M.1
Ben-Avraham, D.2
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17
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0028933051
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Structural studies on the ribbon-to-helix transition in profilin:actin crystals
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Schutt C, Rozycki M, Chik J, Lindberg U. Structural studies on the ribbon-to-helix transition in profilin:actin crystals. Biophys J. 68:1995;12s-18s.
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Schutt, C.1
Rozycki, M.2
Chik, J.3
Lindberg, U.4
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18
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0031057484
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Plugging into actin's architectonic socket
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of special interest. In this News and Views article the ribbon-to-helix model is used as the basis for modeling F-actin's interactions with the CH domain of α-actinin and domains G1-G4 of gelsolin. The model of Schutt and colleagues predicts very different contacts from those determined by interpretting electron microscopy structures in light of the Heidelberg model.
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Schutt CE, Kreatsoulas C, Page R, Lindberg U. Plugging into actin's architectonic socket. of special interest Nature Struct Biol. 4:1997;169-172 In this News and Views article the ribbon-to-helix model is used as the basis for modeling F-actin's interactions with the CH domain of α-actinin and domains G1-G4 of gelsolin. The model of Schutt and colleagues predicts very different contacts from those determined by interpretting electron microscopy structures in light of the Heidelberg model.
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(1997)
Nature Struct Biol
, vol.4
, pp. 169-172
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Schutt, C.E.1
Kreatsoulas, C.2
Page, R.3
Lindberg, U.4
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19
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0028176006
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Determination of the α-actinin binding site on actin filaments by cryoelectron microscopy and image analysis
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McGough A, Way M, DeRosier D. Determination of the α-actinin binding site on actin filaments by cryoelectron microscopy and image analysis. J Cell Biol. 126:1994;433-443.
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(1994)
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McGough, A.1
Way, M.2
Derosier, D.3
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20
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0028863184
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Molecular model of an actin filament capped by a severing protein
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McGough A, Way M. Molecular model of an actin filament capped by a severing protein. J Struct Biol. 115:1995;144-150.
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(1995)
J Struct Biol
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McGough, A.1
Way, M.2
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21
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0031879577
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Determination of the gelsolin binding site on F-actin: Implications for severing and capping
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of outstanding interest. The first direct demonstration of the binding site for gelsolin on the actin filament determined by electron cryomicroscopy and helical reconstruction. By studying a gelsolin derivative (G2 - 6) that has a reduced severing efficiency compared to gelsolin, McGough et al. were able to 'freeze' the severing mechanism in action, providing insights into how gelsolin severs after it binds F-actin.
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McGough A, Chiu W, Way M. Determination of the gelsolin binding site on F-actin: implications for severing and capping. of outstanding interest Biophys J. 74:1998;764-772 The first direct demonstration of the binding site for gelsolin on the actin filament determined by electron cryomicroscopy and helical reconstruction. By studying a gelsolin derivative (G2 - 6) that has a reduced severing efficiency compared to gelsolin, McGough et al. were able to 'freeze' the severing mechanism in action, providing insights into how gelsolin severs after it binds F-actin.
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(1998)
Biophys J
, vol.74
, pp. 764-772
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McGough, A.1
Chiu, W.2
Way, M.3
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22
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0031230805
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Only one F-actin model
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of special interest. A brief response to the 1997 article of Schutt and colleagues highlighting some of the major pieces of experimental evidence in conflict with the ribbon-to-helix model.
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Egelman EH, Orlova A, McGough A. Only one F-actin model. of special interest Nature Struct Biol. 4:1997;683-684 A brief response to the 1997 article of Schutt and colleagues highlighting some of the major pieces of experimental evidence in conflict with the ribbon-to-helix model.
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(1997)
Nature Struct Biol
, vol.4
, pp. 683-684
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Egelman, E.H.1
Orlova, A.2
McGough, A.3
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23
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0027226230
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Structure of the actinñmyosin complex and its implications for muscle contraction
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Rayment I, Holden HM, Whittaker M, Yohn M, Lorenz M, Holmes KC, Milligan RA. Structure of the actinñmyosin complex and its implications for muscle contraction. Science. 261:1993;58-65.
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(1993)
Science
, vol.261
, pp. 58-65
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Rayment, I.1
Holden, H.M.2
Whittaker, M.3
Yohn, M.4
Lorenz, M.5
Holmes, K.C.6
Milligan, R.A.7
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24
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0027220271
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Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1
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Schroder RR, Manstein DJ, Jahn W, Holden H, Rayment I, Holmes KC, Spudich JA. Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1. Nature. 364:1993;171-174.
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(1993)
Nature
, vol.364
, pp. 171-174
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Schroder, R.R.1
Manstein, D.J.2
Jahn, W.3
Holden, H.4
Rayment, I.5
Holmes, K.C.6
Spudich, J.A.7
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25
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0027340549
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A 13 Å map of the actin - Scruin filament from the Limulus acrosomal process
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Owen C, DeRosier DJ. A 13 Å map of the actin - scruin filament from the Limulus acrosomal process. J Cell Biol. 123:1993;337-344.
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(1993)
J Cell Biol
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Owen, C.1
Derosier, D.J.2
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26
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0030820734
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Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
-
of outstanding interest. The binding site for cofilin on the actin filament was determined by electron cryomicroscopy and helical reconstruction. In addition to providing the first direct structural information on how this class of proteins binds actin, this study presents the starting finding that cofilin binding alters actin filament twist. This dramatic alteration in F-actin structure represents a novel mechanism for regulating actin filament dynamics as well as its interactions with other cytoskeletal proteins.
-
McGough A, Pope B, Chiu W, Weeds A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. of outstanding interest J Cell Biol. 138:1997;771-781 The binding site for cofilin on the actin filament was determined by electron cryomicroscopy and helical reconstruction. In addition to providing the first direct structural information on how this class of proteins binds actin, this study presents the starting finding that cofilin binding alters actin filament twist. This dramatic alteration in F-actin structure represents a novel mechanism for regulating actin filament dynamics as well as its interactions with other cytoskeletal proteins.
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(1997)
J Cell Biol
, vol.138
, pp. 771-781
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McGough, A.1
Pope, B.2
Chiu, W.3
Weeds, A.4
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27
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0031572277
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New angles on actin dynamics
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Egelman EH. New angles on actin dynamics. Structure. 5:1997;1135-1137.
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(1997)
Structure
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Egelman, E.H.1
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28
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0030787462
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Stability and dynamics of G-actin: Back door water diffusion and behavior of a subdomain 3/4 loop
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of outstanding interest. An elegant study in which molecular dynamics simulations were used to probe the behavior of the actin monomer structure in solution. The results provide insights into possible domain movements within the actin monomer which may be linked to polymerization.
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Wriggers W, Schulten K. Stability and dynamics of G-actin: back door water diffusion and behavior of a subdomain 3 4 loop. of outstanding interest Biophys J. 73:1997;624-639 An elegant study in which molecular dynamics simulations were used to probe the behavior of the actin monomer structure in solution. The results provide insights into possible domain movements within the actin monomer which may be linked to polymerization.
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(1997)
Biophys J
, vol.73
, pp. 624-639
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Wriggers, W.1
Schulten, K.2
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29
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0031571664
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Modulation of yeast F-actin structure by a mutation in the nucleotide-binding cleft
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of special interest. A nice combination of the powerful yeast system with electron microscopy and helical reconstruction.
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Orlova A, Chen X, Rubenstein PA, Egelman EH. Modulation of yeast F-actin structure by a mutation in the nucleotide-binding cleft. of special interest J Mol Biol. 271:1997;235-243 A nice combination of the powerful yeast system with electron microscopy and helical reconstruction.
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(1997)
J Mol Biol
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, pp. 235-243
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Orlova, A.1
Chen, X.2
Rubenstein, P.A.3
Egelman, E.H.4
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30
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0028839660
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The ADF/cofilin proteins: Stimulus-responsive modulators of actin dynamics
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Moon A, Drubin D. The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics. Mol Biol Cell. 6:1995;1423-1431.
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Mol Biol Cell
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Moon, A.1
Drubin, D.2
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31
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0030727339
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Evidence for a conformational change in actin induced by fimbrin (N375) binding
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Hanein D, Matsudaira P, DeRosier DJ. Evidence for a conformational change in actin induced by fimbrin (N375) binding. J Cell Biol. 139:1997;387-396.
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(1997)
J Cell Biol
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Hanein, D.1
Matsudaira, P.2
Derosier, D.J.3
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32
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0031576324
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3-D image reconstruction of reconstituted smooth muscle thin filaments containing calponin: Visualization of interactions between F-actin and calponin
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Hodgkinson JL, El-Mezgueldi M, Craig R, Vibert P, Marston SB, Lehman W. 3-D image reconstruction of reconstituted smooth muscle thin filaments containing calponin: visualization of interactions between F-actin and calponin. J Mol Biol. 273:1997;150-159.
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(1997)
J Mol Biol
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Hodgkinson, J.L.1
El-Mezgueldi, M.2
Craig, R.3
Vibert, P.4
Marston, S.B.5
Lehman, W.6
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33
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0029822651
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Torsional rigidity of single actin filaments and actin - Actin bond breaking force under torsion measured directly by in vitro micromanipulation
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of outstanding interest. of special interest. An interesting use of molecular tweezers and micromanipulators to probe the physical properties of F-actin. The study demonstrated that actin has increased fragility when twisted. This may help explain the increased fragmentation rate of cofilin-decorated filaments (see McGough et al. [26]).
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of outstanding interest Tsuda Y, Yasutake H, Ishijima A, Yanagida T. Torsional rigidity of single actin filaments and actin - actin bond breaking force under torsion measured directly by in vitro micromanipulation. of special interest Proc Natl Acad Sci USA. 93:1997;12937-12942 An interesting use of molecular tweezers and micromanipulators to probe the physical properties of F-actin. The study demonstrated that actin has increased fragility when twisted. This may help explain the increased fragmentation rate of cofilin-decorated filaments (see McGough et al. [26]).
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(1997)
Proc Natl Acad Sci USA
, vol.93
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Tsuda, Y.1
Yasutake, H.2
Ishijima, A.3
Yanagida, T.4
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34
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0030878880
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Detection of single-molecule interactions using correlated thermal diffusion
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of special interest. An elegant study of binding events involving single myosin molecules using a modification of traditional optical tweezer technology.
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Mehta AD, Finer JT, Spudich JA. Detection of single-molecule interactions using correlated thermal diffusion. of special interest Proc Natl Acad Sci USA. 94:1997;7927-7931 An elegant study of binding events involving single myosin molecules using a modification of traditional optical tweezer technology.
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(1997)
Proc Natl Acad Sci USA
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Mehta, A.D.1
Finer, J.T.2
Spudich, J.A.3
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35
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0030564835
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Cooperativity in F-actin: Binding of gelsolin at the barbed end affects structure and dynamics of the whole filament
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Prochniewicz E, Zhang Q, Janmey PA, Thomas DD. Cooperativity in F-actin: binding of gelsolin at the barbed end affects structure and dynamics of the whole filament. J Mol Biol. 260:1996;756-766.
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Prochniewicz, E.1
Zhang, Q.2
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36
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0014945329
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Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry
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DeRosier DJ, Moore PB. Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry. J Mol Biol. 52:1970;355-369.
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Computer image processing of electron micrographs of biological structures with helical symmetry
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Stewart M. Computer image processing of electron micrographs of biological structures with helical symmetry. J Electron Microsc Tech. 9:1988;325-358.
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0024273235
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The erythroid membrane skeleton: Expression and assembly during erythropoiesis
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Woods CM, Lazarides E. The erythroid membrane skeleton: expression and assembly during erythropoiesis. Annu Rev Med. 39:1988;107-122.
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Woods, C.M.1
Lazarides, E.2
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39
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0031566964
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Steric-model for activation of muscle thin filaments
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of special interest. A careful study of the effects of calcium and myosin head binding on tropomyosin's position in thin filaments from frog skeletal muscle.
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Vibert P, Craig R, Lehman W. Steric-model for activation of muscle thin filaments. of special interest J Mol Biol. 266:1997;8-14 A careful study of the effects of calcium and myosin head binding on tropomyosin's position in thin filaments from frog skeletal muscle.
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J Mol Biol
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Vibert, P.1
Craig, R.2
Lehman, W.3
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Signalling through the lipid products of phosphoinositide-3-OH kinase
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Toker A, Cantley LC. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature. 387:1997;673-676.
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Nature
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Toker, A.1
Cantley, L.C.2
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0030855302
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The structure of divalent cation-induced aggregates of PIP2 and their alteration by gelsolin and tau
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Flanagan LA, Cunningham CA, Chen J, Prestwich GD, Kosik KS, Janmey PA. The structure of divalent cation-induced aggregates of PIP2 and their alteration by gelsolin and tau. Biophys J. 73:1997;1440-1447.
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Biophys J
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Flanagan, L.A.1
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Chen, J.3
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Kosik, K.S.5
Janmey, P.A.6
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Phosphatidylserine liposomes can be tethered by caldesmon to actin filaments
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Makuch R, Zasada A, Mabuchi K, Krauze K, Wang C-LA, Dabrowska R. Phosphatidylserine liposomes can be tethered by caldesmon to actin filaments. Biophys J. 73:1997;1607-1616.
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Makuch, R.1
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Yamada KM, Geiger B. Molecular interactions in cell adhesion complexes. Curr Opin Cell Biol. 9:1997;76-85.
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Actomyosin interactin in striated muscle
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Muscle proteins - Their actions and interactions
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Holmes KC. Muscle proteins - their actions and interactions. Curr Opin Struct Biol. 6:1996;781-789.
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The variable twist of actin and its modulation by actin-binding proteins
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48
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0030692707
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Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis
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of special interest. The state of the art for F-actin reconstructions.
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Jontes JD, Milligan RA. Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis. of special interest J Cell Biol. 139:1997;683-693 The state of the art for F-actin reconstructions.
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J Cell Biol
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Jontes, J.D.1
Milligan, R.A.2
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49
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Conformational changes due to calcium-induced calmodulin dissociation in brush border myosin-I-decorated F-actin revealed by cryoelectron microscopy and image analysis
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Whittaker M, Milligan RA. Conformational changes due to calcium-induced calmodulin dissociation in brush border myosin-I-decorated F-actin revealed by cryoelectron microscopy and image analysis. J Mol Biol. 269:1997;548-557.
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J Mol Biol
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Whittaker, M.1
Milligan, R.A.2
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50
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0029176506
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A 35-Å movement of smooth muscle myosin on ADP release
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Whittaker M, Wilson-Kubalek EM, Smith JE, Faust L, Milligan RA, Sweeney HL. A 35-Å movement of smooth muscle myosin on ADP release. Nature. 378:1995;748-751.
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Nature
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Whittaker, M.1
Wilson-Kubalek, E.M.2
Smith, J.E.3
Faust, L.4
Milligan, R.A.5
Sweeney, H.L.6
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51
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0029562245
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A 32 degree tail swing in brush border mysoin I on ADP release
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Jontes JD, Wilson-Kubalek EM, Milligan RA. A 32 degree tail swing in brush border mysoin I on ADP release. Nature. 378:1995;751-753.
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Jontes, J.D.1
Wilson-Kubalek, E.M.2
Milligan, R.A.3
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52
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0030678623
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Flexibility within myosin heads revealed by negative stain and single-particle analysis
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of outstanding interest. A beautiful, careful study of negatively stained myosin molecules by electron microscopy and single-particle image analysis. Comparison of averaged images with the atomic model of myosin subfragment-1 shows that there is substantial conformational flexibility between the motor domain and the rest of the molecule even in the absence of nucleotide.
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Burgess SA, Walker M, White HD, Trinick J. Flexibility within myosin heads revealed by negative stain and single-particle analysis. of outstanding interest J Cell Biol. 139:1997;675-681 A beautiful, careful study of negatively stained myosin molecules by electron microscopy and single-particle image analysis. Comparison of averaged images with the atomic model of myosin subfragment-1 shows that there is substantial conformational flexibility between the motor domain and the rest of the molecule even in the absence of nucleotide.
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(1997)
J Cell Biol
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Burgess, S.A.1
Walker, M.2
White, H.D.3
Trinick, J.4
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53
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0031056521
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Cryo-atomic force microscopy of smooth muscle myosin
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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.
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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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(1997)
Biophys J
, vol.72
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Zhang, Y.1
Shao, Z.2
Somlyo, A.P.3
Somlyo, A.V.4
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54
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0031581885
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Three-dimensional structure of brush border myosin-I at ~20 Å resolution by electron microscopy and image analysis
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of special interest. Two-dimensional crystals of the unconventional myosin brush border myosin-I, which associates with membranes in cells, were grown on lipid monolayers and analyzed by electron microscopy and image reconstruction. The probable carboxy-terminal lipid-binding domain is visualized in association with the lipid surface.
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Jontes JD, Milligan RA. Three-dimensional structure of brush border myosin-I at ~20 Å resolution by electron microscopy and image analysis. of special interest J Mol Biol. 266:1997;331-342 Two-dimensional crystals of the unconventional myosin brush border myosin-I, which associates with membranes in cells, were grown on lipid monolayers and analyzed by electron microscopy and image reconstruction. The probable carboxy-terminal lipid-binding domain is visualized in association with the lipid surface.
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(1997)
J Mol Biol
, vol.266
, pp. 331-342
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Jontes, J.D.1
Milligan, R.A.2
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55
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0030939055
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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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of special interest. A fascinating demonstration of the use of cysteine - gold interactions to produce a two-dimensional array of identically oriented myosin molecules. This technique should have many applications beyond the study of motor proteins.
-
Sasaki YC, Yasuda K, Suzuki Y, Ishibashi T, Satoh I, Fujiki Y, Ishiwata S. Two-dimensional arrangement of a functional protein by cysteine - gold interaction: enzyme activity and characterization of a protein monolayer on a gold substrate. of special interest Biophys J. 72:1997;1842-1848 A fascinating demonstration of the use of cysteine - gold interactions to produce a two-dimensional array of identically oriented myosin molecules. This technique should have many applications beyond the study of motor proteins.
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(1997)
Biophys J
, vol.72
, pp. 1842-1848
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Sasaki, Y.C.1
Yasuda, K.2
Suzuki, Y.3
Ishibashi, T.4
Satoh, I.5
Fujiki, Y.6
Ishiwata, S.7
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56
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0031041817
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Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap
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Guiford WH, Dupuis DE, Kennedy G, Wu J, Patlak JB, Warshaw DM. Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap. Biophys J. 72:1997;1006-1021.
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(1997)
Biophys J
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Guiford, W.H.1
Dupuis, D.E.2
Kennedy, G.3
Wu, J.4
Patlak, J.B.5
Warshaw, D.M.6
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57
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Smooth and skeletal muscle single-molecule mechanical experiments
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Molloy JE, White DCS. Smooth and skeletal muscle single-molecule mechanical experiments. Biophys J. 72:1997;984-986.
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Biophys J
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Molloy, J.E.1
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58
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Zou G, Phillips GN Jr. A cellular automaton for the regulatory behavior of muscle thin filaments. Biophys J. 67:1994;11-28.
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Zou, G.1
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59
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Visualization of dynamic simulations of muscle thin filaments
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Zou G, Gorry GA, Phillips GN Jr. Visualization of dynamic simulations of muscle thin filaments. J Mol Graph. 13:1995;116-121.
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J Mol Graph
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Zou, G.1
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60
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Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: Effects of caldesmon
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Hodgkinson JL, Marston SB, Craig R, Vibert P, Lehman W. Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: effects of caldesmon. Biophys J. 72:1997;2398-2404.
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Biophys J
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Hodgkinson, J.L.1
Marston, S.B.2
Craig, R.3
Vibert, P.4
Lehman, W.5
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61
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85081163982
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Visualization of caldesmon on smooth muscle thin filaments
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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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Lehman W, Vibert P, Craig R. Visualization of caldesmon on smooth muscle thin filaments. of outstanding interest J Mol Biol. 273:1997;150-159 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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(1997)
J Mol Biol
, vol.273
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Lehman, W.1
Vibert, P.2
Craig, R.3
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62
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Actin-bundling proteins
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Otto JJ. Actin-bundling proteins. Curr Opin Cell Biol. 6:1994;105-109.
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Curr Opin Cell Biol
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Otto, J.J.1
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63
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0031413406
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A strategy for electron tomographic data collection and crystallographic reconstruction of biological bundles
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Sherman MB, Jakana J, Sun S, Matsudara P, Chiu W, Schmid MF. A strategy for electron tomographic data collection and crystallographic reconstruction of biological bundles. J Struct Biol. 20:1997;245-256.
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(1997)
J Struct Biol
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Sherman, M.B.1
Jakana, J.2
Sun, S.3
Matsudara, P.4
Chiu, W.5
Schmid, M.F.6
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64
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0030724661
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Tomographic three-dimensional reconstruction of insect flight muscle partially relaxed by AMPPNP and ethylene glycol
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of outstanding interest. This important work uses electron tomography to reconstruct the actomyosin interactions in insect flight muscle. The results support the proposal that rotation of the motor domain on actin and movements of regulatory domain both contribute to the power stroke.
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Schmitz H, Reedy MC, Reedy MK, Tregear RT, Taylor KA. Tomographic three-dimensional reconstruction of insect flight muscle partially relaxed by AMPPNP and ethylene glycol. of outstanding interest J Cell Biol. 139:1997;695-707 This important work uses electron tomography to reconstruct the actomyosin interactions in insect flight muscle. The results support the proposal that rotation of the motor domain on actin and movements of regulatory domain both contribute to the power stroke.
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(1997)
J Cell Biol
, vol.139
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Schmitz, H.1
Reedy, M.C.2
Reedy, M.K.3
Tregear, R.T.4
Taylor, K.A.5
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65
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0026506363
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Formation of 2-D paracrystals of F-actin on phospholipid layers mixed with quaternary ammonium surfactants
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Taylor KA, Taylor DW. Formation of 2-D paracrystals of F-actin on phospholipid layers mixed with quaternary ammonium surfactants. J Struct Biol. 108:1992;140-147.
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J Struct Biol
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Taylor, K.A.1
Taylor, D.W.2
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66
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0027992919
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Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: Demonstration of unipolar α-actinin - F-actin crosslinking
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Taylor KA, Taylor DA. Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: demonstration of unipolar α-actinin - F-actin crosslinking. Biophys J. 67:1994;1976-1983.
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Biophys J
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Taylor, K.A.1
Taylor, D.A.2
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68
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0030042322
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Spectrin: On the path from structure to function
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Viel A, Branton D. Spectrin: on the path from structure to function. Curr Opin Cell Biol. 8:1996;49-55.
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(1996)
Curr Opin Cell Biol
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Viel, A.1
Branton, D.2
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69
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0031040068
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Crystal structure of a calponin homology domain
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of special interest. This paper presents the first atomic structure for a member of the large family of actin-binding proteins that share the calponin homology domain.
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Carugo KD, Banuelos S, Saraste M. Crystal structure of a calponin homology domain. of special interest Nature Struct Biol. 4:1997;175-179 This paper presents the first atomic structure for a member of the large family of actin-binding proteins that share the calponin homology domain.
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(1997)
Nature Struct Biol
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, pp. 175-179
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Carugo, K.D.1
Banuelos, S.2
Saraste, M.3
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70
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0031228501
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The structure of an actin-crosslinking domain from human fimbrin
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of special interest. 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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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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(1997)
Nature Struct Biol
, vol.4
, pp. 708-712
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Goldsmith, S.C.1
Pokala, N.2
Shen, W.3
Fedorov, A.A.4
Matsudaira, P.5
Almo, S.C.6
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71
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Crystal structure of the repetitive segments of spectrin
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Yan Y, Winograd E, Viel A, Cronin T, Harrison SC, Branton D. Crystal structure of the repetitive segments of spectrin. Science. 262:1993;2027-2030.
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(1993)
Science
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, pp. 2027-2030
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Yan, Y.1
Winograd, E.2
Viel, A.3
Cronin, T.4
Harrison, S.C.5
Branton, D.6
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72
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0028244489
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Structure of the pleckstrin homology domain from beta-spectrin
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Macias MJ, Musacchio A, Ponstingl H, Nilges M, Saraste M, Oschkinat H. Structure of the pleckstrin homology domain from beta-spectrin. Nature. 369:1994;675-677.
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Nature
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, pp. 675-677
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MacIas, M.J.1
Musacchio, A.2
Ponstingl, H.3
Nilges, M.4
Saraste, M.5
Oschkinat, H.6
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73
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0026437577
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Crystal structure of a Src-homology 3 (SH3) domain
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Musacchio A, Noble M, Pauptit R, Wierenga R, Saraste M. Crystal structure of a Src-homology 3 (SH3) domain. Nature. 359:1992;851-855.
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(1992)
Nature
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Musacchio, A.1
Noble, M.2
Pauptit, R.3
Wierenga, R.4
Saraste, M.5
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74
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0031566434
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Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from beta-spectrin
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Nilges M, Macias MJ, O'Donoghue SI, Oschkinat H. Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin. J Mol Biol. 269:1997;408-422.
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(1997)
J Mol Biol
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Nilges, M.1
MacIas, M.J.2
O'Donoghue, S.I.3
Oschkinat, H.4
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75
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0031592935
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Solution structure of the spectrin repeat: A left-handed antiparallel triple-helical coiled-coil
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Pascual J, Pfuhl M, Walther D, Saraste M, Nilges M. Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil. J Mol Biol. 273:1997;740-751.
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J Mol Biol
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Pascual, J.1
Pfuhl, M.2
Walther, D.3
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76
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On the structure of erythrocyte spectrin in partially expanded membrane skeletons
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McGough AM, Josephs R. On the structure of erythrocyte spectrin in partially expanded membrane skeletons. Proc Natl Acad Sci USA. 87:1990;5208-5212.
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Proc Natl Acad Sci USA
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McGough, A.M.1
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77
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0027474019
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Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers
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Taylor KA, Taylor DW. Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers. J Mol Biol. 230:1993;196-205.
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J Mol Biol
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Taylor, K.A.1
Taylor, D.W.2
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78
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0028244823
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Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin
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Bubb MR, Senderowicz AMJ, Sausville EA, Duncan KLK, Korn ED. Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J Biol Chem. 269:1994;14869-14871.
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J Biol Chem
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Bubb, M.R.1
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Sausville, E.A.3
Duncan, K.L.K.4
Korn, E.D.5
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79
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0028967310
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Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments
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Bubb MR, Spector I, Bershadsky AD, Korn ED. Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments. J Biol Chem. 270:1995;3463-3466.
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J Biol Chem
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Bubb, M.R.1
Spector, I.2
Bershadsky, A.D.3
Korn, E.D.4
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80
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Misakinolide A is a marine macrolide that caps but does not sever filamentous actin
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Terry DR, Spector I, Higa T, Bubb MR. Misakinolide A is a marine macrolide that caps but does not sever filamentous actin. J Biol Chem. 272:1997;7841-7845.
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J Biol Chem
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Terry, D.R.1
Spector, I.2
Higa, T.3
Bubb, M.R.4
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81
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0031058410
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NMR structure of the 35-residue villin headpiece subdomain
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of special interest. NMR was used to determine the three-dimensional structure of HP-36, an autonomously folding subdomain that is contained within the carboxy-terminal domain of villin (also called 'headpiece'). HP-36 forms a triple-helical structure that is unrelated to any previously identified actin-binding domain. The residues implicated to date in F-actin binding all reside in the carboxy-terminal helix of this domain.
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McKnight CJ, Matsudaira PI, Kim PS. NMR structure of the 35-residue villin headpiece subdomain. of special interest Nature Struct Biol. 4:1997;180-184 NMR was used to determine the three-dimensional structure of HP-36, an autonomously folding subdomain that is contained within the carboxy-terminal domain of villin (also called 'headpiece'). HP-36 forms a triple-helical structure that is unrelated to any previously identified actin-binding domain. The residues implicated to date in F-actin binding all reside in the carboxy-terminal helix of this domain.
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(1997)
Nature Struct Biol
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McKnight, C.J.1
Matsudaira, P.I.2
Kim, P.S.3
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82
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0030829385
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The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation
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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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Burtnick LD, Koepf EK, Grimes J, Jones EY, Stuart DI, McLaughlin PJ, Robinson RC. The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation. of outstanding interest Cell. 90:1997;661-670 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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(1997)
Cell
, vol.90
, pp. 661-670
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Burtnick, L.D.1
Koepf, E.K.2
Grimes, J.3
Jones, E.Y.4
Stuart, D.I.5
McLaughlin, P.J.6
Robinson, R.C.7
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83
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Probing the effects of calcium on gelsolin
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Pope BJ, Gooch JT, Weeds AG. Probing the effects of calcium on gelsolin. Biochemistry. 36:1997;15848-15855.
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(1997)
Biochemistry
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Pope, B.J.1
Gooch, J.T.2
Weeds, A.G.3
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84
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0030843484
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Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
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Carlier M-F, Laurent V, Santolini J, Melki R, Didry D, Xia G-X, Hong Y, Chua N-H, Pantaloni D. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J Cell Biol. 136:1997;1307-1322.
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(1997)
J Cell Biol
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Carlier M-F1
Laurent, V.2
Santolini, J.3
Melki, R.4
Didry, D.5
Xia G-X6
Hong, Y.7
Chua N-H8
Pantaloni, D.9
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85
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0030604703
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Tertiary structure of destrin and structural similarity between two actin-regulating protein families
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of special interest. NMR was used to determine the tertiary structure of human destrin, a member of the cofilin/ADF family. Representing the first structure for this class of proteins, the destrin structure reveals a surprisingly striking similarity to the highly conserved gelsolin domain.
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Hatanaka H, Ogura K, Moriyama M, Ichikawa S, Yahara I, Inagaki F. Tertiary structure of destrin and structural similarity between two actin-regulating protein families. of special interest Cell. 85:1996;1047-1055 NMR was used to determine the tertiary structure of human destrin, a member of the cofilin/ADF family. Representing the first structure for this class of proteins, the destrin structure reveals a surprisingly striking similarity to the highly conserved gelsolin domain.
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(1996)
Cell
, vol.85
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Hatanaka, H.1
Ogura, K.2
Moriyama, M.3
Ichikawa, S.4
Yahara, I.5
Inagaki, F.6
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86
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Structure determination of yeast cofilin
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Fedorov AA, Lappalainen P, Fedorov EV, Drubin DG, Almo SC. Structure determination of yeast cofilin. Nature Struct Biol. 4:1997;366-369.
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(1997)
Nature Struct Biol
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Fedorov, A.A.1
Lappalainen, P.2
Fedorov, E.V.3
Drubin, D.G.4
Almo, S.C.5
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87
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Crystal structure of the actin-binding protein actophorin from Acanthamoeba
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Leonard SA, Gittis AG, Petrella EC, Pollard TD, Lattman EE. Crystal structure of the actin-binding protein actophorin from Acanthamoeba. Nature Struct Biol. 4:1997;369-373.
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Nature Struct Biol
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Leonard, S.A.1
Gittis, A.G.2
Petrella, E.C.3
Pollard, T.D.4
Lattman, E.E.5
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88
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Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
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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.
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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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(1997)
EMBO J
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Lappalainen, P.1
Fedorov, E.V.2
Fedorov, A.A.3
Almo, S.C.4
Drubin, D.G.5
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89
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Low resolution meets high: Towards a resolution continuum
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Baker TS, Johnson JE. Low resolution meets high: towards a resolution continuum. Curr Opin Struct Biol. 6:1996;585-594.
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(1996)
Curr Opin Struct Biol
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Baker, T.S.1
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Evalutaing atomic models of F-actin with an undecagold-tagged phalloidin derivative
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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.
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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.
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J Mol Biol
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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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