Structural insights on the dynamics of proteasome formation.

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Structural insights on the dynamics of proteasome formation.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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2017年學術文章

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Structural insights on the dynamics of proteasome formation.

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Structural insights on the dynamics of proteasome formation.

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Structural insights on the dynamics of proteasome formation.

@en

Structural insights on the dynamics of proteasome formation.

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Structural insights on the dynamics of proteasome formation.

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Structural insights on the dynamics of proteasome formation.

@nl

P1476

Structural insights on the dynamics of proteasome formation.

@en

P2093

Koichi Kato

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

Tadashi Satoh

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

P2860

A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes

Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones

Chaperone-mediated pathway of proteasome regulatory particle assembly

Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry

Membrane protein structures without crystals, by single particle electron cryomicroscopy

The structure of the mammalian 20S proteasome at 2.75 A resolution

Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S proteasome

Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes

Crystal Structure of Yeast Rpn14, a Chaperone of the 19 S Regulatory Particle of the Proteasome

Structure of a Proteasome Pba1-Pba2 Complex: IMPLICATIONS FOR PROTEASOME ASSEMBLY, ACTIVATION, AND BIOLOGICAL FUNCTION

P2888

s12551-017-0381-4

P304

597-604

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P31

scholarly article

review article

P356

10.1007/S12551-017-0381-4

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P433

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

P478

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

P50

Koichi Kato

T Satoh

P577

2017-12-14T00:00:00Z

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P698

29243089

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P932

5899738

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