A point mutation in the regulatory light chain reduces the step size of skeletal muscle myosin. - Wikidata - awgldk - TriplyDB

A point mutation in the regulatory light chain reduces the step size of skeletal muscle myosin.

A point mutation in the regulatory light chain reduces the step size of skeletal muscle myosin.

http://www.wikidata.org/entity/Q37285004

about

Functional consequences of a mutation in an expressed human alpha-cardiac actin at a site implicated in familial hypertrophic cardiomyopathy In vivo myosin step-size from zebrafish skeletal muscle Visualizing key hinges and a potential major source of compliance in the lever arm of myosin The Qdot-labeled actin super-resolution motility assay measures low-duty cycle muscle myosin step size.Effect of low pH on single skeletal muscle myosin mechanics and kinetics Cardiomyopathy-linked myosin regulatory light chain mutations disrupt myosin strain-dependent biochemistry.In vivo orientation of single myosin lever arms in zebrafish skeletal muscle An alternative domain near the ATP binding pocket of Drosophila myosin affects muscle fiber kinetics.Impact of familial hypertrophic cardiomyopathy-linked mutations in the NH2 terminus of the RLC on β-myosin cross-bridge mechanics Single myosin cross-bridge orientation in cardiac papillary muscle detects lever-arm shear strain in transduction.Functional, structural, and chemical changes in myosin associated with hydrogen peroxide treatment of skeletal muscle fibers.Modification of interface between regulatory and essential light chains hampers phosphorylation-dependent activation of smooth muscle myosin Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.In vitro and in vivo single myosin step-sizes in striated muscle Functional effects of the hypertrophic cardiomyopathy R403Q mutation are different in an alpha- or beta-myosin heavy chain backbone Myosin II isoforms in smooth muscle: heterogeneity and function.Regulatory light chain mutations associated with cardiomyopathy affect myosin mechanics and kinetics Smooth muscle heavy meromyosin phosphorylated on one of its two heads supports force and motion A re-interpretation of the rate of tension redevelopment (k(TR)) in active muscle.Ventricular myosin modifies in vitro step-size when phosphorylated.Phosphorylation of a single head of smooth muscle myosin activates the whole molecule.Kinetic analysis of the slow skeletal myosin MHC-1 isoform from bovine masseter muscle Modulation of Skeletal Muscle Contraction by Myosin Phosphorylation.Single cardiac ventricular myosins are autonomous motors.

P2860

Q24317180-52F1C212-E66D-410A-BAC6-74471F4A2BCD Q27336210-040749C4-D71F-46B0-8FE7-FC4CF25587C7 Q27666354-6DFDB3C7-00D1-491F-A6B0-1BA44C427033 Q30538393-22A7BB4C-4350-4602-A474-90157DB38670 Q33334784-64EAF65B-FE82-4439-939B-23B26A55DA56 Q34182820-CB60775D-F546-4E5F-906C-4AE576137773 Q34203787-6732BE4F-9974-4151-92FE-18E20E5DB415 Q34452473-B94FB193-09BD-4700-BF2C-7A6AD95C2C7A Q34726797-5348E0BB-F9DC-4DC2-9F76-F55358A76D27 Q35224545-FE5996B6-F703-443D-8AB8-37B6B93C917C Q35427426-D21DE79C-2772-48ED-8274-83A307CFB23A Q36052486-CA0F52D2-656A-4D06-AD38-641397C6B24B Q36150807-92000897-F191-44E5-A1C7-F7089AC32A35 Q36609420-C7B33E0F-AEBD-4BE7-A4D5-4B467A628993 Q36761852-A62789DE-8CEF-4E82-9C39-31D938A829E7 Q36809519-BC207EF9-BFEA-4864-832D-EEF1EE6A7175 Q37175862-9D3213FE-BD66-4788-82E5-BBE8B209A641 Q37258501-D76B320B-B05E-4557-BE06-1790E624816F Q37539919-B3A4679F-0C25-449B-9670-B7D7E9E6500B Q40024218-EE910555-65D8-4227-B931-DC7F62E4DF23 Q40291917-E078CE57-420A-4FCC-8AD2-7F4CEBE9D8B4 Q40792968-54B9F862-6CE1-443F-8B05-33D973DD57FB Q46425964-91482614-925D-4A14-B036-8BF689995870 Q52579753-6EE84C1E-E033-4E87-96B5-DA427C262A5D

P2860

A point mutation in the regulatory light chain reduces the step size of skeletal muscle myosin.

http://www.wikidata.org/entity/Q37285004

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 15 July 2004

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

A point mutation in the regula ...... ize of skeletal muscle myosin.

@en

A point mutation in the regula ...... ize of skeletal muscle myosin.

@nl

type

label

A point mutation in the regula ...... ize of skeletal muscle myosin.

@en

A point mutation in the regula ...... ize of skeletal muscle myosin.

@nl

prefLabel

A point mutation in the regula ...... ize of skeletal muscle myosin.

@en

A point mutation in the regula ...... ize of skeletal muscle myosin.

@nl

P1433

Q37285004-D1B48792-9C94-463F-BFE8-36CE7355F4F7

P1476

Q37285004-AA1B525F-5BAF-4FB1-B04F-CDEA4EEDD2A7

P2093

Q37285004-13B5468D-1424-4B24-BED5-0FC1CF3E9744

Q37285004-35AFC69A-5B2F-457B-BF85-DD71D2AFF554

Q37285004-425F2FCA-635A-4E2D-9A5E-8F92CC58F052

Q37285004-6A630E3A-DFE3-48B6-86A7-0266125DE6B8

P2860

Q37285004-015DEB68-9EFA-4368-AAE3-FC0D8D70ED77

Q37285004-057F6DD9-A26A-44DA-BFFE-82B38CB4AD4B

Q37285004-25AD605D-2029-481B-9151-D10A8416D014

Q37285004-2E15EC55-9269-49A4-966B-AAAAC0B7E587

Q37285004-302F0BAD-7452-483E-95E6-1FDCEDBC7F0C

Q37285004-30A88E47-477A-4358-BE12-C2C409321866

Q37285004-3BB3CC88-61F2-4D80-99A7-DAE651276860

Q37285004-3C381CCC-76D6-4F89-A6A5-E3D3FD731C70

Q37285004-42D5EDD9-0AA0-4365-A403-0BE85AC72D6A

Q37285004-4941A590-FFA6-4A1B-86DC-CFE269B1299F

P304

Q37285004-2E72D6F2-5FF2-4117-B59C-ECA139ACAC54

P31

Q37285004-2BC4C936-7DF9-4E28-AD8B-9A152C34F271

P356

Q37285004-991C2567-B349-415F-BD90-733B075FF034

P407

Q37285004-7009BE59-2E0D-4C1E-9EA2-26C96354D2C7

P433

Q37285004-3B8CDBC0-541C-4985-A4D9-1BB5CED98FA2

P478

Q37285004-C88348F1-282C-4670-BE0C-ED414E4F3DD9

P577

Q37285004-59600F6D-B296-4E60-A245-EEF174DA277F

P5875

Q37285004-415746EA-31E2-4502-988C-E9D9122FEA56

P698

Q37285004-472AD0B4-6476-4958-8E43-43A1502C5677

P932

Q37285004-86EDC5FA-4AC2-40CC-8CAD-B78C7A84CBC4

P356

PNAS.0401699101

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

A point mutation in the regula ...... ize of skeletal muscle myosin.

@en

P2093

David M Warshaw

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

Guillermina S Waller

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

Jennifer J Sherwood

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

Susan Lowey

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

P2860

Myosin light chain mutations in familial hypertrophic cardiomyopathy: phenotypic presentation and frequency in Danish and South African populations

Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2

X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-

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

Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state

The genetic basis for cardiomyopathy: from mutation identification to mechanistic paradigms

The myosin power stroke

Structure of the actin-myosin complex and its implications for muscle contraction

Altered kinetics of contraction in skeletal muscle fibers containing a mutant myosin regulatory light chain with reduced divalent cation binding

The Genetic Basis for Cardiomyopathy

P304

10973-10978

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

P31

scholarly article

P356

10.1073/PNAS.0401699101

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

P407

P433

30

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

P478

101

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

P577

2004-07-15T00:00:00Z

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

P5875

8452188

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

P698

15256600

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

P932

503728

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