Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.

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Lineage structure of Streptococcus pneumoniae may be driven by immune selection on the groEL heat-shock protein.An information theoretic framework reveals a tunable allosteric network in group II chaperonins.

P2860

Q41490635-C158105D-CDB2-4C52-AC11-9FFB0F70CAB9 Q43756637-BA3B2039-F9B0-4947-B2ED-121B3A4A6444

P2860

Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.

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http://www.wikidata.org/entity/Q39586605

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Replacement of GroEL in Escher ...... eon Methanococcus maripaludis.

@en

Replacement of GroEL in Escher ...... eon Methanococcus maripaludis.

@nl

type

Item

label

Replacement of GroEL in Escher ...... eon Methanococcus maripaludis.

@en

Replacement of GroEL in Escher ...... eon Methanococcus maripaludis.

@nl

prefLabel

Replacement of GroEL in Escher ...... eon Methanococcus maripaludis.

@en

Replacement of GroEL in Escher ...... eon Methanococcus maripaludis.

@nl

P1476

Replacement of GroEL in Escher ...... eon Methanococcus maripaludis.

@en

P2093

Andrew T Large

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

Astrid Ursinus

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

Bevan Lin

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

Jörg Martin

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

Preethy Gowrinathan

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

Riddhi Shah

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

P2860

Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin

Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis

Chaperone machines for protein folding, unfolding and disaggregation

4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement

Crystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding Cycle

Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.

Mechanism of nucleotide sensing in group II chaperonins

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT

Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies

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2692-2700

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P31

scholarly article

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10.1128/JB.00317-16

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P407

English

P433

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P478

198

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P50

Peter A Lund

P577

2016-07-18T00:00:00Z

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P698

27432832

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P932

5019054

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Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.

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P2860

P2860

Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932