By the same authors

AAA(+) superfamily ATPases: common structure-diverse function

Research output: Contribution to journalLiterature reviewpeer-review

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AAA(+) superfamily ATPases: common structure-diverse function. / Ogura, T ; Wilkinson, A J .

In: GENES TO CELLS, Vol. 6, No. 7, 07.2001, p. 575-597.

Research output: Contribution to journalLiterature reviewpeer-review

Harvard

Ogura, T & Wilkinson, AJ 2001, 'AAA(+) superfamily ATPases: common structure-diverse function', GENES TO CELLS, vol. 6, no. 7, pp. 575-597.

APA

Ogura, T., & Wilkinson, A. J. (2001). AAA(+) superfamily ATPases: common structure-diverse function. GENES TO CELLS, 6(7), 575-597.

Vancouver

Ogura T, Wilkinson AJ. AAA(+) superfamily ATPases: common structure-diverse function. GENES TO CELLS. 2001 Jul;6(7):575-597.

Author

Ogura, T ; Wilkinson, A J . / AAA(+) superfamily ATPases: common structure-diverse function. In: GENES TO CELLS. 2001 ; Vol. 6, No. 7. pp. 575-597.

Bibtex - Download

@article{3be63e7ddb5d4c40ad6705b91cc6d0b7,
title = "AAA(+) superfamily ATPases: common structure-diverse function",
abstract = "The AAA(+) superfamily of ATPases, which contain a homologous ATPase module, are found in an kingdoms of living organisms where they participate in diverse cellular processes including membrane fusion, proteolysis and DNA replication. Recent structural studies have revealed that they usually form ring-shaped oligomers, which are crucial for their ATPase activities and mechanisms of action. These ring-shaped oligomeric complexes are versatile in their mode of action, which collectively seem to involve some form of disruption of molecular or macromolecular structure; unfolding of proteins, disassembly of protein complexes, unwinding of DNA, or alteration of the state of DNA-protein complexes. Thus, the AAA(+) proteins represent a novel type of molecular chaperone. Comparative analyses have also revealed significant similarities and differences in structure and molecular mechanism between AAA(+) ATPases and other ring-shaped ATPases.",
keywords = "ATP-DEPENDENT PROTEASES, DNA-POLYMERASE-III, MEMBRANE-PROTEIN DEGRADATION, FTSH-MEDIATED PROTEOLYSIS, SENSITIVE FUSION PROTEIN, CHAPERONE-LIKE ACTIVITY, CELL-CYCLE PROGRESSION, REPLICATION-FACTOR-C, ESCHERICHIA-COLI, CRYSTAL-STRUCTURE",
author = "T Ogura and Wilkinson, {A J}",
year = "2001",
month = jul,
language = "English",
volume = "6",
pages = "575--597",
journal = "GENES TO CELLS",
issn = "1356-9597",
number = "7",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - AAA(+) superfamily ATPases: common structure-diverse function

AU - Ogura, T

AU - Wilkinson, A J

PY - 2001/7

Y1 - 2001/7

N2 - The AAA(+) superfamily of ATPases, which contain a homologous ATPase module, are found in an kingdoms of living organisms where they participate in diverse cellular processes including membrane fusion, proteolysis and DNA replication. Recent structural studies have revealed that they usually form ring-shaped oligomers, which are crucial for their ATPase activities and mechanisms of action. These ring-shaped oligomeric complexes are versatile in their mode of action, which collectively seem to involve some form of disruption of molecular or macromolecular structure; unfolding of proteins, disassembly of protein complexes, unwinding of DNA, or alteration of the state of DNA-protein complexes. Thus, the AAA(+) proteins represent a novel type of molecular chaperone. Comparative analyses have also revealed significant similarities and differences in structure and molecular mechanism between AAA(+) ATPases and other ring-shaped ATPases.

AB - The AAA(+) superfamily of ATPases, which contain a homologous ATPase module, are found in an kingdoms of living organisms where they participate in diverse cellular processes including membrane fusion, proteolysis and DNA replication. Recent structural studies have revealed that they usually form ring-shaped oligomers, which are crucial for their ATPase activities and mechanisms of action. These ring-shaped oligomeric complexes are versatile in their mode of action, which collectively seem to involve some form of disruption of molecular or macromolecular structure; unfolding of proteins, disassembly of protein complexes, unwinding of DNA, or alteration of the state of DNA-protein complexes. Thus, the AAA(+) proteins represent a novel type of molecular chaperone. Comparative analyses have also revealed significant similarities and differences in structure and molecular mechanism between AAA(+) ATPases and other ring-shaped ATPases.

KW - ATP-DEPENDENT PROTEASES

KW - DNA-POLYMERASE-III

KW - MEMBRANE-PROTEIN DEGRADATION

KW - FTSH-MEDIATED PROTEOLYSIS

KW - SENSITIVE FUSION PROTEIN

KW - CHAPERONE-LIKE ACTIVITY

KW - CELL-CYCLE PROGRESSION

KW - REPLICATION-FACTOR-C

KW - ESCHERICHIA-COLI

KW - CRYSTAL-STRUCTURE

M3 - Literature review

VL - 6

SP - 575

EP - 597

JO - GENES TO CELLS

JF - GENES TO CELLS

SN - 1356-9597

IS - 7

ER -