(Q44295640)

1 December 2017

title

Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation (English)

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1 December 2017

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Mohamad Aman Jairajpuri

1

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1 December 2017

Aiqin Lu

2

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1 December 2017

Umesh Desai

3

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1 December 2017

Steven T Olson

4

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1 December 2017

Ingemar Bjork

5

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1 December 2017

Susan C Bock

6

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1 December 2017

language of work or name

English

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publication date

29 January 2003

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Journal of Biological Chemistry

1 December 2017

published in

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1 December 2017

volume

278

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1 December 2017

issue

18

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1 December 2017

page(s)

15941-15950

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Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability

1 December 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M212319200

Requirement of lysine residues outside of the proposed pentasaccharide binding region for high affinity heparin binding and activation of human antithrombin III.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Lysine residue 114 in human antithrombin III is required for heparin pentasaccharide-mediated activation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

The role of Arg46 and Arg47 of antithrombin in heparin binding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Importance of lysine 125 for heparin binding and activation of antithrombin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

The anticoagulant activation of antithrombin by heparin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Helix D elongation and allosteric activation of antithrombin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Thermodynamic analysis of the heparin interaction with a basic cyclic peptide using isothermal titration calorimetry.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Insight into residues critical for antithrombin function from analysis of an expanded database of sequences that includes frog, turtle, and ostrich antithrombins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Antithrombin in vertebrate species: conservation of the heparin-dependent anticoagulant mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Elimination of P1 arginine 393 interaction with underlying glutamic acid 255 partially activates antithrombin III for thrombin inhibition but not factor Xa inhibition

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a beta-like variant in baculovirus-infected insect cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

The Size and Shape of Human and Bovine Antithrombin III

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Deconvolution of the fluorescence emission spectrum of human antithrombin and identification of the tryptophan residues that are responsive to heparin binding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

Identification of critical molecular interactions mediating heparin activation of antithrombin: implications for the design of improved heparin anticoagulants

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M212319200

21 January 2018

Identifiers

DOI

10.1074/JBC.M212319200

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1 December 2017

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