Mutation of any site of N-linked glycosylation accelerates the in vivo clearance of recombinant rabbit antithrombin. (Q54038989)

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9 November 2019

title

Mutation of any site of N-linked glycosylation accelerates the in vivo clearance of recombinant rabbit antithrombin (English)

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9 November 2019

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9 November 2019

H Ni

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9 November 2019

M A Blajchman

series ordinal

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9 November 2019

V S Ananthanarayanan

series ordinal

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9 November 2019

I J Smith

series ordinal

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9 November 2019

publication date

1 August 2000

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9 November 2019

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9 November 2019

volume

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9 November 2019

issue

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9 November 2019

page(s)

407-415

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Cloning and expression of the cDNA for human antithrom, bin III

9 November 2019

cites work

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7 January 2021

Isolation and partial characterization of two distinct types of antithrombin III from rabbit

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7 January 2021

Comparison of the behaviour in vivo of two molecular forms of antithrombin III.

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7 January 2021

Physiological variant of antithrombin-III lacks carbohydrate sidechain at Asn 135.

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7 January 2021

Antithrombin III-beta associates more readily than antithrombin III-alpha with uninjured and de-endothelialized aortic wall in vitro and in vivo

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7 January 2021

Amino acid substitutions of the P2 residue of human antithrombin that either enhance or impair function

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7 January 2021

Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycoluril

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7 January 2021

Use of kinetic analysis and mathematical modeling in the study of metabolic pathways in vivo. Applications to hepatic organic anion metabolism. (First of two parts).

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7 January 2021

Concepts and principles of glycobiology

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7 January 2021

Analysis of synthesis, processing, and secretion of proteins expressed in mammalian cells

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7 January 2021

Overexpression of recombinant human antithrombin III in Chinese hamster ovary cells results in malformation and decreased secretion of recombinant protein

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7 January 2021

Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity

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7 January 2021

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

1 reference

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7 January 2021

Amino acid sequence of porcine antithrombin III

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7 January 2021

Uses of antithrombin III concentrate in congenital and acquired deficiency states

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7 January 2021

Antiangiogenic activity of the cleaved conformation of the serpin antithrombin

1 reference

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7 January 2021

10.1016/S0049-3848(00)00263-2

Identifiers

DOI

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9 November 2019

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