(Q71712108)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8884602%20AND%20SRC:MED&resulttype=core&format=json

20 October 2019

title

Differential scanning calorimetric study of the complexes of modified myosin subfragment 1 with ADP and vanadate or beryllium fluoride (English)

1 reference

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20 October 2019

6

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20 October 2019

author name string

N L Golitsina

1

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20 October 2019

A A Bobkov

2

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20 October 2019

I V Dedova

3

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20 October 2019

D A Pavlov

4

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20 October 2019

O P Nikolaeva

5

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20 October 2019

D I Levitsky

7

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20 October 2019

publication date

1 August 1996

1 reference

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Journal of Muscle Research & Cell Motility

20 October 2019

published in

1 reference

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20 October 2019

volume

17

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20 October 2019

issue

4

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20 October 2019

page(s)

475-485

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Scanning microcalorimetry in studying temperature-induced changes in proteins.

20 October 2019

cites work

1 reference

12 December 2020

Velocity of movement of actin filaments in in vitro motility assay. Measured by fluorescence correlation spectroscopy

1 reference

12 December 2020

Myosin subfragment-1 is sufficient to move actin filaments in vitro

1 reference

12 December 2020

Mechanism of adenosine triphosphatase activity of trinitrophenylated myosin subfragment 1

1 reference

12 December 2020

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

1 reference

12 December 2020

Localization of the reactive trinitrophenylated lysyl residue of myosin ATPase site in the NH2-terminal (27 k domain) of S1 heavy chain

1 reference

12 December 2020

Kinetic characterization of reductively methylated myosin subfragment 1.

1 reference

12 December 2020

Inhibition of myosin ATPase by vanadate ion

1 reference

12 December 2020

Kinetic and equilibrium analysis of the interactions of actomyosin subfragment-1.ADP with beryllium fluoride

1 reference

12 December 2020

Effect of lysine methylation and other ATPase modulators on the active site of myosin subfragment 1.

1 reference

12 December 2020

The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction

1 reference

12 December 2020

Intermediate states of subfragment 1 and actosubfragment 1 ATPase: reevaluation of the mechanism

1 reference

12 December 2020

Formation of the stable myosin-ADP-aluminum fluoride and myosin-ADP-beryllium fluoride complexes and their analysis using 19F NMR

1 reference

12 December 2020

On the origin and transmission of force in actomyosin subfragment 1.

1 reference

12 December 2020

Analysis of orthophosphate-pyrophosphate mixtures resulting from weak pyrophosphatase activities

1 reference

12 December 2020

Inhibition of myosin ATPase by beryllium fluoride

1 reference

12 December 2020

Ionization of reactive lysyl residue of myosin subfragment 1

1 reference

12 December 2020

The difference between ADP-beryllium fluoride and ADP-aluminium fluoride complexes of the spin-labeled myosin subfragment 1

1 reference

12 December 2020

The characterization of vanadate-trapped nucleotide complexes with spin-labelled myosins

1 reference

12 December 2020

Myosin active-site trapping with vanadate ion

1 reference

12 December 2020

Resolution of conformational states of spin-labeled myosin during steady-state ATP hydrolysis

1 reference

12 December 2020

Effect of nucleotide binding on the proximity of the essential sulfhydryl groups of myosin. Chemical probing of movement of residues during conformational transitions

1 reference

12 December 2020

Inhibition of actomyosin ATPase by vanadate

1 reference

12 December 2020

Formation of Stable Inhibitory Complexes of Myosin Subfragment 1 Using Fluoroscandium Anions

1 reference

12 December 2020

Defining the “fast-reacting” thiols of myosin by reaction with 1,5 IAEDANS

1 reference

12 December 2020

The reactive SH1 and SH2 cysteines in myosin subfragment 1 are cross-linked at similar rates with reagents of different length

1 reference

12 December 2020

Differential scanning calorimetric study of the complexes of myosin subfragment 1 with nucleoside diphosphates and vanadate or beryllium fluoride

1 reference

12 December 2020

Calorimetric characterization of the stable complex of myosin subfragment 1 with ADP and beryllium fluoride

1 reference

12 December 2020

Observation of multiple myosin subfragment 1-ADP-fluoroberyllate complexes by 19F NMR spectroscopy

1 reference

12 December 2020

Interaction of spin-labeled and N-(iodoacetylaminoethyl)-5-naphthylamine-1-sulfonic acid SH1-blocked heavy meromyosin and myosin with actin and adenosine triphosphate

1 reference

12 December 2020

Characterization of stable beryllium fluoride, aluminum fluoride, and vanadate containing myosin subfragment 1-nucleotide complexes

1 reference

12 December 2020

Effects of nucleotide binding on thermal transitions and domain structure of myosin subfragment 1

1 reference

12 December 2020

Reactivity of essential thiols of myosin. Chemical probes of the activated state

1 reference

12 December 2020

10 Sulfhydryl modification and labeling of myosin

1 reference

12 December 2020

Extensively methylated myosin subfragment-1: examination of local structure, interactions with nucleotides and actin, and ligand-induced conformational changes

1 reference

12 December 2020

Chemical modification of myosin by active-site trapping of metal-nucleotides with thiol crosslinking reagents

1 reference

12 December 2020

Flexibility of the myosin heavy chain: direct evidence that the region containing SH1 and SH2 can move 10 A under the influence of nucleotide binding

1 reference

12 December 2020

Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin

1 reference

12 December 2020

Structural studies of myosin:nucleotide complexes: a revised model for the molecular basis of muscle contraction

1 reference

12 December 2020

Identifiers

DOI

10.1007/BF00123363

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8884602%20AND%20SRC:MED&resulttype=core&format=json

20 October 2019

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