Jennifer L Olszewski
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Explore the profile of Jennifer L Olszewski including associated specialties, affiliations and a list of published articles.
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9
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986
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Recent Articles
1.
Dove K, Olszewski J, Martino L, Duda D, Wu X, Miller D, et al.
Structure
. 2017 May;
25(6):890-900.e5.
PMID: 28552575
RING-between-RING (RBR) E3s contain RING1 domains that are structurally similar yet mechanistically distinct from canonical RING domains. Both types of E3 bind E2∼ubiquitin (E2∼Ub) via their RINGs but canonical RING...
2.
Scott D, Rhee D, Duda D, Kelsall I, Olszewski J, Paulo J, et al.
Cell
. 2016 Aug;
166(5):1198-1214.e24.
PMID: 27565346
Hundreds of human cullin-RING E3 ligases (CRLs) modify thousands of proteins with ubiquitin (UB) to achieve vast regulation. Current dogma posits that CRLs first catalyze UB transfer from an E2...
3.
Ordureau A, Heo J, Duda D, Paulo J, Olszewski J, Yanishevski D, et al.
Proc Natl Acad Sci U S A
. 2015 May;
112(21):6637-42.
PMID: 25969509
The PTEN-induced putative kinase protein 1 (PINK1) and ubiquitin (UB) ligase PARKIN direct damaged mitochondria for mitophagy. PINK1 promotes PARKIN recruitment to the mitochondrial outer membrane (MOM) for ubiquitylation of...
4.
Ordureau A, Sarraf S, Duda D, Heo J, Jedrychowski M, Sviderskiy V, et al.
Mol Cell
. 2014 Oct;
56(3):360-375.
PMID: 25284222
Phosphorylation is often used to promote protein ubiquitylation, yet we rarely understand quantitatively how ligase activation and ubiquitin (UB) chain assembly are integrated with phosphoregulation. Here we employ quantitative proteomics...
5.
Kelsall I, Duda D, Olszewski J, Hofmann K, Knebel A, Langevin F, et al.
EMBO J
. 2013 Oct;
32(21):2848-60.
PMID: 24076655
RING (Really Interesting New Gene)-in-between-RING (RBR) enzymes are a distinct class of E3 ubiquitin ligases possessing a cluster of three zinc-binding domains that cooperate to catalyse ubiquitin transfer. The regulation...
6.
Duda D, Olszewski J, Schuermann J, Kurinov I, Miller D, Nourse A, et al.
Structure
. 2013 May;
21(6):1030-41.
PMID: 23707686
A distinct mechanism for ubiquitin (Ub) ligation has recently been proposed for the RING1-IBR-RING2 (RBR) family of E3s: an N-terminal RING1 domain recruits a thioester-linked intermediate complex between Ub and...
7.
Kaiser S, Mao K, Taherbhoy A, Yu S, Olszewski J, Duda D, et al.
Nat Struct Mol Biol
. 2012 Nov;
19(12):1242-9.
PMID: 23142976
Core functions of autophagy are mediated by ubiquitin-like protein (UBL) cascades, in which a homodimeric E1 enzyme, Atg7, directs the UBLs Atg8 and Atg12 to their respective E2 enzymes, Atg3...
8.
Duda D, Olszewski J, Tron A, Hammel M, Lambert L, Waddell M, et al.
Mol Cell
. 2012 Jul;
47(3):371-82.
PMID: 22748924
The approximately 300 human cullin-RING ligases (CRLs) are multisubunit E3s in which a RING protein, either RBX1 or RBX2, recruits an E2 to catalyze ubiquitination. RBX1-containing CRLs also can bind...
9.
Tron A, Arai T, Duda D, Kuwabara H, Olszewski J, Fujiwara Y, et al.
Mol Cell
. 2012 Mar;
46(1):67-78.
PMID: 22405651
Fbw7, a substrate receptor for Cul1-RING-ligase (CRL1), facilitates the ubiquitination and degradation of several proteins, including Cyclin E and c-Myc. In spite of much effort, the mechanisms underlying Fbw7 regulation...