NMR structure of the calreticulin P-domain (Q27630622)

7

0 references

Lars Ellgaard

object named as

L Ellgaard

1

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Torsten Herrmann

object named as

T Herrmann

3

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Peter Güntert

object named as

P Güntert

4

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author name string

R Riek

2

0 references

D Braun

5

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A Helenius

Proceedings of the National Academy of Sciences of the United States of America

6

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language of work or name

English

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publication date

13 March 2001

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published in

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volume

98

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issue

6

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page(s)

3133-8

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cites work

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Protein glucosylation and its role in protein folding

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Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro

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ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin

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Floating stereospecific assignment revisited: application to an 18 kDa protein and comparison with J-coupling data

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Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins

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Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi

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The X-Pro peptide bond as an nmr probe for conformational studies of flexible linear peptides

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Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

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Quaternary structure and assembly process of the T cell receptor

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