Folding intermediates are involved in genetic diseases? (Q41664525)

6 October 2017

title

Folding intermediates are involved in genetic diseases? (English)

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6 October 2017

Bychkova VE

1

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6 October 2017

Ptitsyn OB

series ordinal

2

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6 October 2017

language of work or name

English

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publication date

1 February 1995

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6 October 2017

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6 October 2017

volume

359

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6 October 2017

issue

1

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6 October 2017

page(s)

6-8

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Temperature-sensitive mutants blocked in the folding or subunit of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30 degrees C.

6 October 2017

cites work

1 reference

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Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein. III. Intensive polypeptide chains synthesized at 39 degrees C.

21 January 2018

1 reference

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Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive

21 January 2018

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The mechanism of Z alpha 1-antitrypsin accumulation in the liver

21 January 2018

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The LDL receptor locus in familial hypercholesterolemia: mutational analysis of a membrane protein

21 January 2018

1 reference

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Deletion in cysteine-rich region of LDL receptor impedes transport to cell surface in WHHL rabbit

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2895%2900004-S

The 'molten globule' state is involved in the translocation of proteins across membranes?

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2895%2900004-S

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2895%2900004-S

Prevention of protein denaturation under heat stress by the chaperonin Hsp60

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2895%2900004-S

Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2895%2900004-S

The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2895%2900004-S

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

21 January 2018

1 reference

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Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2895%2900004-S

High-resolution structure of the oligomerization domain of p53 by multidimensional NMR

21 January 2018

1 reference

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Z and the insoluble answer

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2895%2900004-S

Intracellular protein trafficking defects in human disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2895%2900004-S

Single amino acid mutations block a late step in the folding of beta-lactamase from Staphylococcus aureus

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2895%2900004-S

p53: a glimpse at the puppet behind the shadow play

21 January 2018

1 reference

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10.1016/0014-5793(95)00004-S

21 January 2018

Identifiers

DOI

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6 October 2017

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