(Q34304306)

1 August 2017

title

Structure of the Ca(2+)-free Gla domain sheds light on membrane binding of blood coagulation proteins (English)

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1 August 2017

Sunnerhagen M

1

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1 August 2017

Forsén S

2

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1 August 2017

Hoffrén AM

3

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1 August 2017

Drakenberg T

4

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1 August 2017

Teleman O

5

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1 August 2017

Stenflo J

6

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1 August 2017

publication date

1 June 1995

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Nature structural biology

1 August 2017

published in

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1 August 2017

volume

2

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1 August 2017

issue

6

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1 August 2017

page(s)

504-509

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Vitamin K-Dependent Formation of γ-Carboxyglutamic Acid

1 August 2017

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The molecular basis of blood coagulation

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Structure of prothrombin fragment 1 refined at 2.8 A resolution

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Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding

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Ca2+ binding to calbindin D9k strongly affects backbone dynamics: measurements of exchange rates of individual amide protons using 1H NMR.

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Rat annexin V crystal structure: Ca(2+)-induced conformational changes

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Relationship between annexin V tryptophan exposure, calcium, and phospholipid binding

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Calcium-myristoyl protein switch

31 March 2020

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Role of the acylated amino terminus of recoverin in Ca(2+)-dependent membrane interaction

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Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin

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31 March 2020

Identifiers

DOI

10.1038/NSB0695-504

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1 August 2017

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