Impact of the 237th residue on the folding of human carbonic anhydrase II.

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Effects of silica nanoparticle supported ionic liquid as additive on thermal reversibility of human carbonic anhydrase II.Modified β-casein restores thermal reversibility of human carbonic anhydrase II: the salt bridge mechanism.

P2860

Q36914922-FB805930-9382-437F-B289-2E5D4A0D9CE9 Q45927485-9A0ABD20-138B-45D8-9933-81F3A435635A

P2860

Impact of the 237th residue on the folding of human carbonic anhydrase II.

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http://www.wikidata.org/entity/Q35048525

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2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Impact of the 237th residue on the folding of human carbonic anhydrase II.

@en

type

Item

label

Impact of the 237th residue on the folding of human carbonic anhydrase II.

@en

prefLabel

Impact of the 237th residue on the folding of human carbonic anhydrase II.

@en

P1476

Impact of the 237th residue on the folding of human carbonic anhydrase II.

@en

P2093

Ming-Jie Wu

http://www.w3.org/2001/XMLSchema#string

Yan Jiang

http://www.w3.org/2001/XMLSchema#string

Yong-Bin Yan

http://www.w3.org/2001/XMLSchema#string

P2860

The FoldX web server: an online force field

Molecular basis of human carbonic anhydrase II deficiency

Carbonic anhydrase II deficiency identified as the primary defect in the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification

A single mutation at the sheet switch region results in conformational changes favoring lambda6 light-chain fibrillogenesis

Structure and mechanism of carbonic anhydrase

Protein folding and misfolding

Human carbonic anhydrases and carbonic anhydrase deficiencies

Structure-based redesign of the dimerization interface reduces the toxicity of zinc-finger nucleases

ADAN: a database for prediction of protein-protein interaction of modular domains mediated by linear motifs.

A three-state prediction of single point mutations on protein stability changes.

P304

2797-2807

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P31

scholarly article

P356

10.3390/IJMS12052797

http://www.w3.org/2001/XMLSchema#string

P407

English

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http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2011-04-28T00:00:00Z

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P5875

51231595

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P698

21686151

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P932

3116157

http://www.w3.org/2001/XMLSchema#string

Impact of the 237th residue on the folding of human carbonic anhydrase II.

about

P2860

P2860

Impact of the 237th residue on the folding of human carbonic anhydrase II.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932