Application of the Dale-Eisinger analysis to proximity mapping in the contractile system. - Wikidata - awgldk - TriplyDB

Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.

Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.

http://www.wikidata.org/entity/Q30413485

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On the origin and transmission of force in actomyosin subfragment 1.Resonance energy transfer from a cylindrical distribution of donors to a plane of acceptors. Location of apo-B100 protein on the human low-density lipoprotein particle.

P2860

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P2860

Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.

http://www.wikidata.org/entity/Q30413485

description

1984 nî lūn-bûn

@nan

1984 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

1984 թվականի հունիսին հրատարակված գիտական հոդված

@hy

1984年の論文

@ja

1984年論文

@yue

1984年論文

@zh-hant

1984年論文

@zh-hk

1984年論文

@zh-mo

1984年論文

@zh-tw

1984年论文

@wuu

name

Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.

@ast

Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.

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type

label

Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.

@ast

Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.

@en

prefLabel

Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.

@ast

Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.

@en

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P356

PNAS.81.12.3723

P1433

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

P1476

Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.

@en

P2093

M F Morales

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

P M Torgerson

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P2860

The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin

Fluorescence energy transfer as a spectroscopic ruler.

On the mechanism of energy transduction in myosin subfragment 1.

The use of singlet-singlet energy transfer to study macromolecular assemblies.

Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin.

Time-dependent fluorescence depolarization and lifetime studies of myosin subfragment-one in the presence of nucleotide and actin.

Studies on the role of myosin alkali light chains. Recombination and hybridization of light chains and heavy chains in subfragment-1 preparations.

Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1.

The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer.

Anisotropy decay of labelled actin. Evidence of the flexibility of the peptide chain in F-actin molecules.

P304

3723-3727

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scholarly article

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10.1073/PNAS.81.12.3723

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12

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81

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1984-06-01T00:00:00Z

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16609702

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6587387

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345291

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