J
Joel H. Weiner
Researcher at University of Alberta
Publications - 28
Citations - 3854
Joel H. Weiner is an academic researcher from University of Alberta. The author has contributed to research in topics: Reductase & Amino acid. The author has an hindex of 25, co-authored 28 publications receiving 3728 citations. Previous affiliations of Joel H. Weiner include University of British Columbia & Canadian Institutes of Health Research.
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Journal ArticleDOI
A Novel and Ubiquitous System for Membrane Targeting and Secretion of Cofactor-Containing Proteins
Joel H. Weiner,P T Bilous,Gillian Shaw,Shannon P Lubitz,Laura S. Frost,Gavin H. Thomas,Jeffrey A. Cole,Raymond J. Turner +7 more
TL;DR: The identification of the proteins encoded by the mttABC operon, which mediate a novel Sec-independent membrane targeting and translocation system in Escherichia coli that interacts with cofactor-containing redox proteins having a S/TRRXFLK "twin arginine" leader motif, is reported.
Journal ArticleDOI
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
Michela G. Bertero,Richard A. Rothery,Monica Palak,Cynthia Hou,Daniel Lim,Francis Blasco,Joel H. Weiner,Natalie C. J. Strynadka +7 more
TL;DR: The NarGHI structure identifies the number, coordination scheme and environment of the redox-active prosthetic groups, a unique coordination of the molybdenum atom, the first structural evidence for the role of an open bicyclic form of themolybdo-bis in the catalytic mechanism and a novel fold of the membrane anchor subunit.
Journal ArticleDOI
The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs
Ian T. Paulsen,Ronald A. Skurray,Roland Tam,Milton H. Saier,Raymond J. Turner,Joel H. Weiner,Edward B. Goldberg,Leonas L. Grinius +7 more
TL;DR: Hydropathy and residue distribution analyses of this family suggest a structural model in which the polypeptide chain spans the membrane four times as mildly amphipathic α‐helices, and a possible mechanistic model of drug efflux.
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The deoxyribonucleic acid unwinding protein of Escherichia coli. Properties and functions in replication.
TL;DR: The DNA unwinding protein of Escherichia coli has been purified to homogeneity by a simple procedure which utilizes its stability to heating and depends on its essential role in the conversion of phage G4 single-stranded DNA to the replicative form.
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The prokaryotic complex iron-sulfur molybdoenzyme family.
TL;DR: There is a bias against the presence of soluble periplasmic molybdoenzymes in bacteria lacking an outer membrane and the CISM archetypes and related enzymes rely on the tat translocon to transport fully folded monomeric or dimeric subunits across the cytoplasmic membrane.