Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain (Q57752679)

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1 January 2020

title

Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain (English)

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2

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Kentaro Tomii

3

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Hidekazu Hiroaki

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author name string

Kumiko Shiozawa

1

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Azusa Seto

4

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Natsuko Goda

5

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Yutaka Akiyama

6

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Toshiyuki Shimizu

7

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Masahiro Shirakawa

8

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language of work or name

English

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publication date

24 August 2004

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Journal of Biological Chemistry

1 January 2020

published in

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volume

279

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issue

48

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page(s)

50060-50068

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Peroxisomes, lipid metabolism, and human disease

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Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: evidence that PTS1 protein import is mediated by a cycling receptor

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Two AAA family peroxins, PpPex1p and PpPex6p, interact with each other in an ATP-dependent manner and are associated with different subcellular membranous structures distinct from peroxisomes

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The peroxisome biogenesis factors pex4p, pex22p, pex1p, and pex6p act in the terminal steps of peroxisomal matrix protein import

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Crystallographic characterization of the N-terminal domain of PEX1

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21 January 2018

Identifiers

DOI

10.1074/JBC.M407837200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15328346%20AND%20SRC:MED&resulttype=core&format=json

1 January 2020

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