DsbA-mediated disulfide bond formation and catalyzed prolyl isomerization in oxidative protein folding (Q72631408)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7890650%20AND%20SRC:MED&resulttype=core&format=json

28 October 2019

title

DsbA-mediated disulfide bond formation and catalyzed prolyl isomerization in oxidative protein folding (English)

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28 October 2019

author name string

C Frech

series ordinal

1

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28 October 2019

F X Schmid

series ordinal

2

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28 October 2019

language of work or name

English

0 references

publication date

1 March 1995

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Journal of Biological Chemistry

28 October 2019

number of pages

8

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based on heuristic

inferred from page(s)

published in

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28 October 2019

volume

270

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28 October 2019

issue

10

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28 October 2019

page(s)

5367-5374

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The bonds that tie: catalyzed disulfide bond formation

28 October 2019

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Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme

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Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells

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Intact disulfide bonds decelerate the folding of ribonuclease T1

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21 January 2018

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Identifiers

DOI

10.1074/JBC.270.10.5367

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7890650%20AND%20SRC:MED&resulttype=core&format=json

28 October 2019

1 reference