Ligand-promoted protein folding by biased kinetic partitioning.

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Cognate Ligand Chaperoning: a Novel Mechanism for the Post-translational Regulation of Neurotransmitter Receptor Biogenesis.Stilbene Boronic Acids Form a Covalent Bond with Human Transthyretin and Inhibit Its Aggregation.Blocking protein quality control to counter hereditary cancers.

P2860

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P2860

Ligand-promoted protein folding by biased kinetic partitioning.

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http://www.wikidata.org/entity/Q41842078

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2017 nî lūn-bûn

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2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

2017年论文

@zh

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name

Ligand-promoted protein folding by biased kinetic partitioning.

@en

type

Item

label

Ligand-promoted protein folding by biased kinetic partitioning.

@en

prefLabel

Ligand-promoted protein folding by biased kinetic partitioning.

@en

P1476

Ligand-promoted protein folding by biased kinetic partitioning.

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P2093

Derrick T Deming

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

Karan S Hingorani

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

Lila M Gierasch

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

Matthew C Metcalf

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

Scott C Garman

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

P2860

Rescue of ΔF508-CFTR trafficking via a GRASP-dependent unconventional secretion pathway

Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease

Sorting out the trash: the spatial nature of eukaryotic protein quality control

Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge

Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.

Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state

The Molecular Basis of Pharmacological Chaperoning in Human α-Galactosidase

Chaperonin overexpression promotes genetic variation and enzyme evolution

Immunoglobulin aggregation leading to Russell body formation is prevented by the antibody light chain

Quinary structure modulates protein stability in cells.

P2888

nchembio.2303

P304

369-371

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P31

scholarly article

P356

10.1038/NCHEMBIO.2303

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

P433

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

P478

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

P50

Evan T Powers

P577

2017-02-20T00:00:00Z

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

P698

28218913

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

P921

protein folding

P932

5362304

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

Ligand-promoted protein folding by biased kinetic partitioning.

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P2860

P2860

Ligand-promoted protein folding by biased kinetic partitioning.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932