Nature Search

Retrovirus envelope domain at 1.7 Å resolution

Deborah Fass
Stephen C. Harrison
Peter S. Kim
Research01 May 1996
Nature Structural Biology

Volume: 3, P: 465-469
Young secretory proteins go through a phase

Phase separation is a mechanism for non-organellar macromolecule segregation typical in the cell cytosol and nucleus. Two recent studies revealed functional phase separation within the endoplasmic reticulum, where calcium-mediated condensates co-ordinate chaperones and disulfide catalysts to enhance secretory protein production.

Deborah Fass
Carolyn S. Sevier
News & Views11 Nov 2025
Nature Cell Biology

Volume: 27, P: 1887-1888
Previously unknown type of protein crosslink discovered

Molecular crosslinks known as disulfides stabilize the 3D structures of many proteins, and sometimes regulate protein function. But disulfides are not alone — another type of regulatory protein crosslink has been discovered.

Deborah Fass
Sergey N. Semenov
News & Views05 May 2021
Nature

Volume: 593, P: 343-344
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p

Einav Gross
Carolyn S. Sevier
Deborah Fass
Research10 Dec 2001
Nature Structural Biology

Volume: 9, P: 61-67
Computational optimization of antibody humanness and stability by systematic energy-based ranking

A computational method for the systematic grafting of animal complementarity-determining regions onto thousands of human frameworks allows for the design of humanized versions of antibodies with improved stability.

Ariel Tennenhouse
Lev Khmelnitsky
Sarel J. Fleishman
Research07 Aug 2023
Nature Biomedical Engineering

Volume: 8, P: 30-44
Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module

Deborah Fass
Stephen Blacklow
James M. Berger
Research14 Aug 1997
Nature

Volume: 388, P: 691-693
Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands

Deborah Fass
Cynthia E. Bogden
James M. Berger
Research01 Apr 1999
Nature Structural Biology

Volume: 6, P: 322-326
Single-molecule spectroscopy exposes hidden states in an enzymatic electron relay

A major challenge in following electron transfer through dithiol/disulfide exchange is the dearth of accompanying spectroscopic effects. Here, the authors use single-molecule Förster resonance energy transfer experiments to illuminate disulfide bond rearrangements within the enzyme quiescin sulfhydryl oxidase.

Iris Grossman
Haim Yuval Aviram
Deborah Fass
ResearchOpen Access15 Oct 2015
Nature Communications

Volume: 6, P: 1-10
The dynamic disulphide relay of quiescin sulphydryl oxidase

The X-ray crystal structures of trypanosome and mammalian quiescin sulphydryl oxidase are determined; these structures and follow-up biochemical studies show that large conformational changes occur as the enzyme relays disulphide bonds through its redox-active sites.

Assaf Alon
Iris Grossman
Deborah Fass
Research15 Jul 2012
Nature

Volume: 488, P: 414-418
How intramembrane proteases bury hydrolytic reactions in the membrane

Elinor Erez
Deborah Fass
Eitan Bibi
Reviews20 May 2009
Nature

Volume: 459, P: 371-378
Improved molecular replacement by density- and energy-guided protein structure optimization

Frank DiMaio
Thomas C. Terwilliger
David Baker
Research01 May 2011
Nature

Volume: 473, P: 540-543

Search

Filter By:

Search

Quick links