User profiles for Z. A. Ripstein

Zev Ripstein

Department of Chemistry; University of Manitoba
Verified email at umanitoba.ca
Cited by 685

Processing of cryo-EM movie data

ZA Ripstein, JL Rubinstein - Methods in enzymology, 2016 - Elsevier
Direct detector device (DDD) cameras dramatically enhance the capabilities of electron
cryomicroscopy (cryo-EM) due to their improved detective quantum efficiency (DQE) relative to …

Structure of a AAA+ unfoldase in the process of unfolding substrate

ZA Ripstein, R Huang, R Augustyniak, LE Kay… - Elife, 2017 - elifesciences.org
Ripstein et al. used a technique called electron cryomicroscopy to study a AAA+ unfoldase
from a microbe called Thermoplasma acidophilum. The enzymes were supplied with a …

[HTML][HTML] Electron-event representation data enable efficient cryoEM file storage with full preservation of spatial and temporal resolution

…, G Singla Lezcano, B Janssen, L Yu, ZA Ripstein… - IUCrJ, 2020 - scripts.iucr.org
Direct detector device (DDD) cameras have revolutionized electron cryomicroscopy (cryoEM)
with their high detective quantum efficiency (DQE) and output of movie data. A high ratio of …

A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery

ZA Ripstein, S Vahidi, WA Houry, JL Rubinstein… - Elife, 2020 - elifesciences.org
The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair
of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently …

[HTML][HTML] Shake-it-off: a simple ultrasonic cryo-EM specimen-preparation device

JL Rubinstein, H Guo, ZA Ripstein… - … Section D: Structural …, 2019 - scripts.iucr.org
Although microscopes and image-analysis software for electron cryomicroscopy (cryo-EM)
have improved dramatically in recent years, specimen-preparation methods have lagged …

Reversible inhibition of the ClpP protease via an N-terminal conformational switch

S Vahidi, ZA Ripstein, M Bonomi… - Proceedings of the …, 2018 - National Acad Sciences
Protein homeostasis is critically important for cell viability. Key to this process is the refolding
of misfolded or aggregated proteins by molecular chaperones or, alternatively, their …

An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR

S Vahidi, ZA Ripstein, JB Juravsky… - Proceedings of the …, 2020 - National Acad Sciences
The 300-kDa ClpP1P2 protease from Mycobacterium tuberculosis collaborates with the AAA+
(ATPases associated with a variety of cellular activities) unfoldases, ClpC1 and ClpX, to …

Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study

R Huang, ZA Ripstein, R Augustyniak… - Proceedings of the …, 2016 - National Acad Sciences
The AAA+ (ATPases associated with a variety of cellular activities) enzymes play critical
roles in a variety of homeostatic processes in all kingdoms of life. Valosin-containing protein-like …

Cooperative subunit dynamics modulate p97 function

R Huang, ZA Ripstein… - Proceedings of the …, 2019 - National Acad Sciences
p97 is an essential hexameric AAA+ ATPase involved in a wide range of cellular processes.
Mutations in the enzyme are implicated in the etiology of an autosomal dominant …

Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP

RW Harkness, Y Toyama, ZA Ripstein… - Proceedings of the …, 2021 - National Acad Sciences
DegP is an oligomeric protein with dual protease and chaperone activity that regulates protein
homeostasis and virulence factor trafficking in the periplasm of gram-negative bacteria. A …