(Q34413306)

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Two naturally occurring alpha2,6-sialyltransferase forms with a single amino acid change in the catalytic domain differ in their catalytic activity and proteolytic processing

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scholarly article

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Europe PubMed Central

PubMed publication ID

2 August 2017

Two naturally occurring alpha2,6-sialyltransferase forms with a single amino acid change in the catalytic domain differ in their catalytic activity and proteolytic processing (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

1 reference

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J Ma

1

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

R Qian

2

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Europe PubMed Central

PubMed publication ID

2 August 2017

F M Rausa

3

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Europe PubMed Central

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2 August 2017

K J Colley

4

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Europe PubMed Central

PubMed publication ID

2 August 2017

language of work or name

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publication date

1 January 1997

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Europe PubMed Central

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2 August 2017

Journal of Biological Chemistry

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2 August 2017

272

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Europe PubMed Central

PubMed publication ID

2 August 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

672-679

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Biological roles of oligosaccharides: all of the theories are correct

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A disulfide-bonded dimer of the Golgi beta-galactoside alpha2,6-sialyltransferase is catalytically inactive yet still retains the ability to bind galactose

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Identifiers

10.1074/JBC.272.1.672

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

ResearchGate publication ID

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