Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

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HSP90C interacts with PsbO1 and facilitates its thylakoid distribution from chloroplast stroma in Arabidopsis.Sorting of SEC translocase SCY components to different membranes in chloroplasts.

P2860

Q47251677-72B952D8-A409-4DAB-B8DF-E7000F77ED70 Q47676861-C0DB9AA6-DB47-4AFA-A4CC-DFA51E43E2E8

P2860

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

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http://www.wikidata.org/entity/Q36323439

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2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

@wuu

2015年学术文章

@zh-cn

2015年学术文章

@zh-hans

2015年学术文章

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@zh-sg

2015年學術文章

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2015年學術文章

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@zh-hant

name

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

@ast

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

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type

Item

label

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

@ast

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

@en

prefLabel

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

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Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

@en

P1476

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

@en

P2093

Donna E Fernandez

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

Kentaro Inoue

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

P2860

Blue-native PAGE in plants: a tool in analysis of protein-protein interactions

Structure and mechanism of Escherichia coli type I signal peptidase

Targeting of lumenal proteins across the thylakoid membrane

Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications

Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor

UCSF Chimera--a visualization system for exploratory research and analysis

Predicting subcellular localization of proteins based on their N-terminal amino acid sequence

Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport

Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone

Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP

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28778-28791

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scholarly article

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10.1074/JBC.M115.684829

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P407

English

P433

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

P478

290

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

P50

Joshua K Endow

Rajneesh Singhal

P577

2015-10-07T00:00:00Z

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P698

26446787

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

P921

molecular chaperones

P932

4661394

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Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

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P2860

P2860

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932