Structure and mechanism of helicases and nucleic acid translocases

MR Singleton, MS Dillingham, DB Wigley - Annu. Rev. Biochem., 2007 - annualreviews.org
Helicases and translocases are a ubiquitous, highly diverse group of proteins that perform
an extraordinary variety of functions in cells. Consequently, this review sets out to define a …

X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in …

CD Putnam, M Hammel, GL Hura… - Quarterly reviews of …, 2007 - cambridge.org
Crystallography supplies unparalleled detail on structural information critical for mechanistic
analyses; however, it is restricted to describing low energy conformations of …

Evolutionary relationships and structural mechanisms of AAA+ proteins

JP Erzberger, JM Berger - Annu. Rev. Biophys. Biomol. Struct., 2006 - annualreviews.org
Complex cellular events commonly depend on the activity of molecular “machines” that
efficiently couple enzymatic and regulatory functions within a multiprotein assembly. An …

Evolutionary history and higher order classification of AAA+ ATPases

LM Iyer, DD Leipe, EV Koonin, L Aravind - Journal of structural biology, 2004 - Elsevier
The AAA+ ATPases are enzymes containing a P-loop NTPase domain, and function as
molecular chaperones, ATPase subunits of proteases, helicases or nucleic-acid-stimulated …

Mechanisms and regulation of DNA replication initiation in eukaryotes

MW Parker, MR Botchan, JM Berger - Critical reviews in …, 2017 - Taylor & Francis
Cellular DNA replication is initiated through the action of multiprotein complexes that
recognize replication start sites in the chromosome (termed origins) and facilitate duplex …

Helicase structure and mechanism

JM Caruthers, DB McKay - Current opinion in structural biology, 2002 - Elsevier
Structural information on helicase proteins has expanded recently beyond the DNA
helicases Rep and PcrA, and the hepatitis C virus RNA helicase to include UvrB, members …

[HTML][HTML] Structure and function of the AAA+ nucleotide binding pocket

P Wendler, S Ciniawsky, M Kock, S Kube - Biochimica et Biophysica Acta …, 2012 - Elsevier
Members of the diverse superfamily of AAA+ proteins are molecular machines responsible
for a wide range of essential cellular processes. In this review we summarise structural and …

STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: multiple, complex domain architectures, unusual phyletic patterns …

DD Leipe, EV Koonin, L Aravind - Journal of molecular biology, 2004 - Elsevier
Using sequence profile analysis and sequence-based structure predictions, we define a
previously unrecognized, widespread class of P-loop NTPases. The signal transduction …

The clinical continuum of cryopyrinopathies: novel CIAS1 mutations in North American patients and a new cryopyrin model

I Aksentijevich, C D. Putnam, EF Remmers… - Arthritis & …, 2007 - Wiley Online Library
Objective The cryopyrinopathies are a group of rare autoinflammatory disorders that are
caused by mutations in CIAS1, encoding the cryopyrin protein. However, cryopyrin …

[HTML][HTML] Mechanism of AAA+ ATPase-mediated RuvAB–Holliday junction branch migration

J Wald, D Fahrenkamp, N Goessweiner-Mohr… - Nature, 2022 - nature.com
The Holliday junction is a key intermediate formed during DNA recombination across all
kingdoms of life. In bacteria, the Holliday junction is processed by two homo-hexameric …