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Cited by 758

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EVOLUTIONARY RELATIONSHIPS AND STRUCTURAL MECHANISMS OF AAA+ PROTEINS

Erzberger, Jan P., Berger, James M.·2006·Annual Review of Biophysics and Biomolecular Structure

Abstract

Complex cellular events commonly depend on the activity of molecular “machines” that efficiently couple enzymatic and regulatory functions within a multiprotein assembly. An essential and expanding subset of these assemblies comprises proteins of the ATPases associated with diverse cellular activities (AAA+) family. The defining feature of AAA+ proteins is a structurally conserved ATP-binding module that oligomerizes into active arrays. ATP binding and hydrolysis events at the interface of neighboring subunits drive conformational changes within the AAA+ assembly that direct translocation or remodeling of target substrates. In this review, we describe the critical features of the AAA+ domain, summarize our current knowledge of how this versatile element is incorporated into larger assemblies, and discuss specific adaptations of the AAA+ fold that allow complex molecular manipulations to be carried out for a highly diverse set of macromolecular targets.

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Metadata

Authors
Erzberger, J. P., & Berger, J. M.
Venue
Annual Review of Biophysics and Biomolecular Structure
Published
2006-06-01
Volume
35
Issue
1
Pages
93-114
ISSN
  • 1056-8700 (ISSN-L)
  • 1545-4266
OpenAlex
W2121431496
Cited by
758
References
1
FWCI
13.75
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: EVOLUTIONARY RELATIONSHIPS AND STRUCTURAL MECHANISMS OF AAA+ PROTEINS. https://app.cochat.ai/papers/10.1146/annurev.biophys.35.040405.101933
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Erzberger, J. P., & Berger, J. M. (2006). EVOLUTIONARY RELATIONSHIPS AND STRUCTURAL MECHANISMS OF AAA+ PROTEINS. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.35.040405.101933

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