about
The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptideRapid microtubule self-assembly kineticsThe structured core of human β tubulin confers isotype-specific polymerization properties.Brownian motion of inert tracer macromolecules in polymerized and spontaneously bundled mixtures of actin and filamin.Tracer diffusion in F-actin and Ficoll mixtures. Toward a model for cytoplasm.Concentration dependence of variability in growth rates of microtubulesCooperative polymerization reactions. Analytical approximations, numerical examples, and experimental strategy.Detection and characterization of actin monomers, oligomers, and filaments in solution by measurement of fluorescence photobleaching recovery.A quantitative analysis of microtubule elongation.Three-dimensional structure of the central mitotic spindle of Diatoma vulgareThree-dimensional structure of actin filaments and of an actin gel made with actin-binding protein.Mutations in Human Tubulin Proximal to the Kinesin-Binding Site Alter Dynamic Instability at Microtubule Plus- and Minus-Ends.Suppression of microtubule assembly kinetics by the mitotic protein TPX2.Thin filament length regulation in striated muscle sarcomeres: pointed-end dynamics go beyond a nebulin ruler.Tactoidal state and phase transitions in systems of linear polymers of variable lengthDirected elongation model for microtubule GTP hydrolysis.Quantitative computational models of molecular self-assembly in systems biology.Invited review: Microtubule severing enzymes couple atpase activity with tubulin GTPase spring loading.Electrophoresis and orientation of F-actin in agarose gels.GTPase activity at ends of microtubules.Important factors determining the nanoscale tracking precision of dynamic microtubule ends.The length distribution of frangible biofilaments.Nucleated polymerization with secondary pathways. III. Equilibrium behavior and oligomer populations.Some perspectives on the viscosity of actin filaments.Does actin bind to the ends of thin filaments in skeletal muscle?Ligand induced galectin-3 protein self-association.Protein Polymerization into Fibrils from the Viewpoint of Nucleation Theory.The scope of moderate pressure changes for kinetic and equilibrium studies of biochemical systems.A kinetic analysis of the assembly of microtubules in vitro.Reduction in microtubule dynamics in vitro by brain microtubule-associated proteins and by a microtubule-associated protein-2 second repeated sequence analogue.Asymptotic solutions of the Oosawa model for the length distribution of biofilaments.End-growth/evaporation living polymerization kinetics revisited.Monte Carlo simulations of microtubule arrays: The critical roles of rescue transitions, the cell boundary, and tubulin concentration in shaping microtubule distributions.
P2860
Q28854601-9854B26A-032A-4EE7-AC78-AD562B8DAF85Q30504124-6F4A2F55-F581-4E6A-9F32-8B02EC1C2782Q30761012-2105BA34-9B48-4B52-8577-9C9E34B0B008Q33755270-6B9F02C1-91A3-4152-AD31-54EF942F681EQ34126128-749ABC96-7629-4598-84DC-680D5A673A15Q34178789-79AC40B7-ECF3-43B3-A0E1-5D8764F36F38Q34258739-E55DCC14-6174-4225-BEE1-CC3753C477FAQ34534827-6D3114B4-DFD6-4029-9922-70689F5C0F23Q36198289-38B85CA4-71A9-4F87-8F9B-68215709787AQ36203844-DF13517F-2144-4594-821F-BA900F4148F0Q36622297-81F1D8AB-3D1E-4ECE-8244-1BF8ABF46AEBQ36800259-1594AF45-F6DE-4335-AAAB-4DCFDDF9E010Q36856746-F1AAC6E1-D7B7-4642-87AC-31FA70056B65Q37269778-B592BD2B-E39D-4522-8C3C-9FA0377FE517Q37333081-8D2F12F9-CF38-428F-B192-6CCBE51493F0Q37688171-7A846C95-03B0-4E47-8BF3-B7582C250796Q38680217-E5F3111C-2384-4CE1-84D3-C119CBAAC6A9Q38796151-2C299C70-6AD3-4E8C-9A09-5AE8208F7B1DQ39619472-CAA81EBD-4834-42A6-8F89-E8B7489DFF4AQ40131043-AE0A6476-E871-4AFF-8E8B-8D3BB6637645Q40195868-F9504831-AD51-4E82-8DF0-232580A457EFQ40371204-611E782D-B128-4A2B-A44C-AC42C234D92FQ41055376-FB987924-B10A-4ED5-BEA6-E3B3C78A2A35Q41377767-9C9E2109-45B4-461A-8356-503E97A3C868Q41470021-C3759241-CAB7-4CA0-8B1D-9B810100D4E8Q41853356-32F40AE6-CB3D-4BAA-A3C1-12B93F7870A3Q42135525-CB086F08-0C87-4BDA-86CE-99445E64AC57Q47958566-52971206-1D65-46C6-ABA3-190E38AE5A61Q48274450-BF5C2D6D-E715-4FAD-BF33-C01221F93336Q48329944-97C17019-AF8D-45BF-A0C1-059AF0FDB511Q51083983-788D37D5-23EF-4BEB-9225-B3F569F1B6E2Q51587569-03ED08D2-53E6-4492-B87C-B4B4A9D1D57FQ54996796-FF4FDAA5-E32D-4088-BFFC-EA3DA7624603
P2860
description
1970 nî lūn-bûn
@nan
1970年の論文
@ja
1970年学术文章
@wuu
1970年学术文章
@zh
1970年学术文章
@zh-cn
1970年学术文章
@zh-hans
1970年学术文章
@zh-my
1970年学术文章
@zh-sg
1970年學術文章
@yue
1970年學術文章
@zh-hant
name
Size distribution of protein polymers.
@en
Size distribution of protein polymers.
@nl
type
label
Size distribution of protein polymers.
@en
Size distribution of protein polymers.
@nl
prefLabel
Size distribution of protein polymers.
@en
Size distribution of protein polymers.
@nl
P1476
Size distribution of protein polymers.
@en
P2093
P356
10.1016/0022-5193(70)90129-3
P407
P577
1970-04-01T00:00:00Z