Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin. - Wikidata - wikimedia - TriplyDB

Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin.

Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin.

http://www.wikidata.org/entity/Q33265312

about

Load and Pi control flux through the branched kinetic cycle of myosin V.The molecular effects of skeletal muscle myosin regulatory light chain phosphorylation.Harmonic force spectroscopy measures load-dependent kinetics of individual human β-cardiac myosin molecules Single molecule techniques in DNA repair: a primer Hypertrophic and dilated cardiomyopathy mutations differentially affect the molecular force generation of mouse alpha-cardiac myosin in the laser trap assay.The direct molecular effects of fatigue and myosin regulatory light chain phosphorylation on the actomyosin contractile apparatus.A Drosophila model of dominant inclusion body myopathy type 3 shows diminished myosin kinetics that reduce muscle power and yield myofibrillar defects.The influence of myosin converter and relay domains on cross-bridge kinetics of Drosophila indirect flight muscle.Cardiomyopathy-linked myosin regulatory light chain mutations disrupt myosin strain-dependent biochemistry.Deletion of Drosophila muscle LIM protein decreases flight muscle stiffness and power generation.Kinetics of cardiac myosin isoforms in mouse myocardium are affected differently by presence of myosin binding protein-C Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.Roles for cardiac MyBP-C in maintaining myofilament lattice rigidity and prolonging myosin cross-bridge lifetime.Direct Measurements of Local Coupling between Myosin Molecules Are Consistent with a Model of Muscle Activation.Two-state model of acto-myosin attachment-detachment predicts C-process of sinusoidal analysis Expression of the inclusion body myopathy 3 mutation in Drosophila depresses myosin function and stability and recapitulates muscle inclusions and weakness.Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.A branched kinetic scheme describes the mechanochemical coupling of Myosin Va processivity in response to substrate.Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics.The kinetics of mechanically coupled myosins exhibit group size-dependent regimes.Myosin MgADP Release Rate Decreases as Sarcomere Length Increases in Skinned Rat Soleus Muscle Fibers.Distribution of myosin attachment times predicted from viscoelastic mechanics of striated muscle.Elevated rates of force development and MgATP binding in F764L and S532P myosin mutations causing dilated cardiomyopathy.A strain-dependency of Myosin off-rate must be sensitive to frequency to predict the B-process of sinusoidal analysis.Phosphate and ADP differently inhibit coordinated smooth muscle myosin groups.The molecular basis of thin filament activation: from single molecule to muscle Muscle activation described with a differential equation model for large ensembles of locally coupled molecular motors.The load dependence of rate constants.Measuring the Kinetic and Mechanical Properties of Non-processive Myosins Using Optical Tweezers.A mixed-kinetic model describes unloaded velocities of smooth, skeletal, and cardiac muscle myosin filaments in vitro.Kramers-like turnover in load-dependent activated dynamics.Five Alternative Myosin Converter Domains Influence Muscle Power, Stretch Activation, and Kinetics.

P2860

Q30488878-EA2C2273-C2EF-43A2-A0E5-D08F1E7D2395 Q30489420-6719B506-3D24-4E92-A100-87CDA6B29DDD Q30660760-2EAE8A45-BB3A-43AB-B852-7BEB2048233F Q30829969-B4139EE6-DE5A-4E41-BE77-4A010E4E8A83 Q33277814-FB835A42-B778-4832-A262-7D47F428C038 Q33784312-D1FD4D47-7F0A-424C-8DE8-297CA952859F Q33830492-C5D4DE08-9485-4811-913B-96B36578827A Q34099091-5A5987C0-3B33-4B1E-A36C-8D428E6D700B Q34182820-63A203A6-6E5C-4FFE-96FF-6D11563F27F9 Q34184362-40F7F417-1AC0-4D07-9018-6900DD7C3369 Q34642017-53B1F554-EFD0-4EF3-8B2F-980034150764 Q35051582-98A77222-28B8-4086-9FA5-BEFB9AD1F859 Q35246252-9FE07F5A-F541-4051-A1CB-A75C1870617F Q35831950-422A7B2B-AF71-4C02-AD19-C5F98982789A Q35878638-F09518FE-D031-4E6A-8DB7-D4C1B75DDABF Q35998580-D2911009-C48F-4DF9-B6C6-6CD527BC82B2 Q36150807-C2D7F6E0-84DB-4692-BF14-13DB29E0CDBA Q36238156-34FFB9D4-98FE-4D36-8EDE-3A584379E039 Q36981755-34351A7F-EC14-4E0B-8D95-F0A12634358C Q37204383-AE976533-0E48-4774-B5DE-0D72CF1D2265 Q39223604-E99BCBA2-67F3-490A-B035-6FA5BD721C2D Q39532707-D482A0E1-0464-493A-B7FC-8374D13110C0 Q41287417-53B1720B-C4C6-4B17-AEEB-E8996B19042C Q41458977-4DE8DBBA-AE2B-4910-9265-AE433CF71C68 Q42183030-AA38E0E9-8C0F-4B99-A537-B1430C29BEFA Q42266722-22A0DB6D-7D7D-453D-953A-73E643D6B091 Q44748338-C04DACA5-7100-489B-B3DE-607CADBCB5CA Q45952768-39CDC0E8-1B86-4A60-AE04-05F6C4F4EA87 Q47141269-91FACAA9-90FF-4129-890B-A781687DCEC4 Q47169132-29FF8C78-948D-433F-AE06-745059DAAC26 Q51811840-B729811C-1E22-44B0-8849-D8DE7FB6D0D6 Q52655823-322DFC92-68C5-402A-8F3D-7881DD6C0307

P2860

Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin.

http://www.wikidata.org/entity/Q33265312

description

2006 nî lūn-bûn

@nan

2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Mutation of a conserved glycin ...... -dependent kinetics of myosin.

@ast

Mutation of a conserved glycin ...... -dependent kinetics of myosin.

@en

Mutation of a conserved glycin ...... -dependent kinetics of myosin.

@nl

type

label

Mutation of a conserved glycin ...... -dependent kinetics of myosin.

@ast

Mutation of a conserved glycin ...... -dependent kinetics of myosin.

@en

Mutation of a conserved glycin ...... -dependent kinetics of myosin.

@nl

prefLabel

Mutation of a conserved glycin ...... -dependent kinetics of myosin.

@ast

Mutation of a conserved glycin ...... -dependent kinetics of myosin.

@en

Mutation of a conserved glycin ...... -dependent kinetics of myosin.

@nl

P1433

Q33265312-91E68590-B1C9-4617-9396-5331200372A8

P1476

Q33265312-BB7EC685-1034-48B2-8CE3-FBD28E317130

P2093

Q33265312-0E332B3D-F35D-4EBF-A84E-8181E55A77F6

Q33265312-23680637-8464-43EE-973C-0277DB1EF393

Q33265312-5483B9AB-F4C0-449D-931C-C036A73672F0

Q33265312-F8AE1B0E-D091-49D4-9F14-DC2B3281D835

P2860

Q33265312-018FE20B-F98A-483B-A118-C0140386B528

Q33265312-06EA52DD-1FFA-4E39-AE0D-E74806799800

Q33265312-092D3586-9103-473C-8B8A-A2D7938DECF5

Q33265312-0B8321C2-F077-4F34-A638-8243133224A3

Q33265312-0BF6419D-2C3D-47F5-B17B-78CB0C6C9DB6

Q33265312-15B18A50-BACA-46FD-9947-B75D1290CBF3

Q33265312-1CBC3D27-9BF9-4EF8-8E59-B4A44F4805E8

Q33265312-1CC160E3-E8A3-432A-8AF3-566C712233CF

Q33265312-1DC05049-E3CC-457D-BD20-9564E02EB06F

Q33265312-2E8B7506-EFDA-49C7-9687-C92B5A698795

P304

Q33265312-C9DF49AC-6B7D-40DE-94FF-A549C4A4108B

P31

Q33265312-15043A34-29FA-4508-A2AA-B46343D56F2D

P356

Q33265312-511043D4-50C0-44E6-B0A0-C9CD2140E123

P407

Q33265312-C13CBE63-140F-406E-B6B0-C86CE9FD84BA

P433

Q33265312-4851CCAE-71A7-4380-AE2C-00BADFFD8978

P478

Q33265312-1DD06FD9-BA7E-4D66-86BE-B970799D9F87

P50

Q33265312-FE5ADD8E-0D0B-4102-A338-CF813F86633F

P577

Q33265312-576DA62E-1190-4AFD-8F2C-A1D03058EE3F

P5875

Q33265312-9B144D81-0A15-44D3-8607-5651477DD70C

P698

Q33265312-51275AE5-1128-41C4-8EDD-80B65BF89572

P932

Q33265312-7F2089E6-52C5-456A-BDB0-4E11500250A2

P356

BIOPHYSJ.106.097618

P1433

Biophysical Journal

P1476

Mutation of a conserved glycin ...... -dependent kinetics of myosin.

@en

P2093

David M Warshaw

http://www.w3.org/2001/XMLSchema#string

Joseph B Patlak

http://www.w3.org/2001/XMLSchema#string

Kathleen M Trybus

http://www.w3.org/2001/XMLSchema#string

Patricia M Fagnant

http://www.w3.org/2001/XMLSchema#string

P2860

Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head

Three conformational states of scallop myosin S1

Three-dimensional structure of myosin subfragment-1: a molecular motor

Models for the specific adhesion of cells to cells

Myosin regulatory light chain phosphorylation and strain modulate adenosine diphosphate release from smooth muscle Myosin.

Structural mechanism of the recovery stroke in the myosin molecular motor.

A mutant heterodimeric myosin with one inactive head generates maximal displacement.

The light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever.

Slip sliding away: load-dependence of velocity generated by skeletal muscle myosin molecules in the laser trap.

The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules

P304

1623-1631

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1529/BIOPHYSJ.106.097618

http://www.w3.org/2001/XMLSchema#string

P407

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

92

http://www.w3.org/2001/XMLSchema#string

P50

P577

2006-12-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

6657265

http://www.w3.org/2001/XMLSchema#string

P698

17142278

http://www.w3.org/2001/XMLSchema#string

P932

1796825

http://www.w3.org/2001/XMLSchema#string