(Q27730158)

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Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy

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Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy (English)

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S J Freedman

1

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B C Furie

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2

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B Furie

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3

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J D Baleja

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4

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language of work or name

English

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publication date

7 April 1995

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published in

Journal of Biological Chemistry

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volume

270

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issue

14

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page(s)

7980-7

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cites work

The molecular basis of blood coagulation

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retrieved

21 January 2018

Comparison of lipid binding and kinetic properties of normal, variant, and gamma-carboxyglutamic acid modified human factor IX and factor IXa.

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21 January 2018

Isolation and characterization of a cDNA coding for human factor IX

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reference URL

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retrieved

21 January 2018

Molecular cloning of the gene for human anti-haemophilic factor IX.

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reference URL

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21 January 2018

The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1

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21 January 2018

The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X‐ray structures

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reference URL

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21 January 2018

An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance.

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reference URL

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21 January 2018

Activation of factor IX by the reaction product of tissue factor and factor VII: additional pathway for initiating blood coagulation

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reference URL

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21 January 2018

Three-dimensional structure of the kringle sequence: structure of prothrombin fragment 1.

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reference URL

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21 January 2018

A gamma-carboxyglutamic acid (gamma) variant (gamma 6D, gamma 7D) of human activated protein C displays greatly reduced activity as an anticoagulant

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reference URL

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21 January 2018

Recognition site directing vitamin K-dependent gamma-carboxylation resides on the propeptide of factor IX

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reference URL

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21 January 2018

Solution structure of iron(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional proton NMR

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.270.14.7980

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21 January 2018

Structure and order of the protein and carbohydrate domains of prothrombin fragment 1

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.270.14.7980

retrieved

21 January 2018

Structure of Ca2+ prothrombin fragment 1 including the conformation of the Gla domain

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.270.14.7980

retrieved

21 January 2018

Role of the hexapeptide disulfide loop present in the gamma-carboxyglutamic acid domain of human protein C in its activation properties and in the in vitro anticoagulant activity of activated protein C

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.270.14.7980

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21 January 2018

Identifiers

DOI

10.1074/JBC.270.14.7980

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PubMed publication ID

7713897

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ResearchGate publication ID

15485082

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(Q27730158)

Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy

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