The myosin catalytic domain does not rotate during the working power stroke.

about

Polarized fluorescence depletion reports orientation distribution and rotational dynamics of muscle cross-bridges.Mechanochemical coupling in spin-labeled, active, isometric muscle Actin Sliding Velocities are Influenced by the Driving Forces of Actin-Myosin Binding.

P2860

Q30539061-1475C8F7-E61C-4B1A-A5DE-164087C3EA33 Q34171746-3DE7E08A-E5FA-4092-AAAE-5DD319F0B041 Q39874098-10BADEDC-4854-4BCA-978B-07EA516E2B42

P2860

The myosin catalytic domain does not rotate during the working power stroke.

Item

http://www.wikidata.org/entity/Q42541035

description

1995 nî lūn-bûn

@nan

1995年の論文

@ja

1995年論文

@yue

1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

@wuu

1995年论文

@zh

1995年论文

@zh-cn

name

The myosin catalytic domain does not rotate during the working power stroke.

@en

The myosin catalytic domain does not rotate during the working power stroke.

@nl

type

Item

label

The myosin catalytic domain does not rotate during the working power stroke.

@en

The myosin catalytic domain does not rotate during the working power stroke.

@nl

prefLabel

The myosin catalytic domain does not rotate during the working power stroke.

@en

The myosin catalytic domain does not rotate during the working power stroke.

@nl

P1476

The myosin catalytic domain does not rotate during the working power stroke.

@en

P2093

A J Baker

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

E Pate

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

L Zhao

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

R Cooke

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

P2860

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

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

The inhibition of rabbit skeletal muscle contraction by hydrogen ions and phosphate.

Relationships between chemical and mechanical events during muscular contraction.

Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibres.

Time-resolved rotational dynamics of phosphorescent-labeled myosin heads in contracting muscle fibers.

Myosin heads have a broad orientational distribution during isometric muscle contraction: time-resolved EPR studies using caged ATP.

Flash and smash: rapid freezing of muscle fibers activated by photolysis of caged ATP.

Orientational disorder and motion of weakly attached cross-bridges.

Paramagnetic probes attached to a light chain on the myosin head are highly disordered in active muscle fibers.

P304

994-999

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

P31

scholarly article

P356

10.1016/S0006-3495(95)79974-X

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

P407

English

P433

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

P478

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

P577

1995-09-01T00:00:00Z

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

P698

8519999

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

P932

1236328

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

The myosin catalytic domain does not rotate during the working power stroke.

about

P2860

P2860

The myosin catalytic domain does not rotate during the working power stroke.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932