scispace - formally typeset
J

J. Wade Harper

Researcher at Harvard University

Publications -  292
Citations -  75309

J. Wade Harper is an academic researcher from Harvard University. The author has contributed to research in topics: Ubiquitin ligase & Ubiquitin. The author has an hindex of 109, co-authored 279 publications receiving 66267 citations. Previous affiliations of J. Wade Harper include University of Wisconsin-Madison & Institute of Cancer Research.

Papers
More filters
Journal ArticleDOI

Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways

Elizabeth T. Cirulli, +70 more
- 27 Mar 2015 - 
TL;DR: A moderate-scale sequencing study aimed at increasing the number of genes known to contribute to predisposition for ALS found several known ALS genes were found to be associated, and TBK1 (the gene encoding TANK-binding kinase 1) was identified as an ALS gene.
Journal ArticleDOI

Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways

TL;DR: A broad understanding of how E1 enzymes activate UBLs and how they selectively coordinate U BLs with downstream function has come from enzymatic, structural and genetic studies.
Journal ArticleDOI

Phosphorylation-Dependent Ubiquitination of Cyclin E by the SCFFbw7 Ubiquitin Ligase

TL;DR: The ubiquitin ligase responsible for cyclin E ubiquitination as SCFFbw7 is identified and it is demonstrated that it is functionally conserved in yeast, flies, and mammals.
Journal ArticleDOI

Altered cell differentiation and proliferation in mice lacking p57 KIP2 indicates a role in Beckwith–Wiedemann syndrome

TL;DR: Mice lacking the imprinted Cdk inhibitor p57KIP2 have altered cell proliferation and differentiation, leading to abdominal muscle defects; cleft palate; endochondral bone ossification defects with incomplete differentiation of hypertrophic chondrocytes; renal medullary dysplasia; adrenal cortical hyperplasia and cytomegaly; and lens cell hyperproliferation and apoptosis.
Journal ArticleDOI

Structure of the DDB1–CRBN E3 ubiquitin ligase in complex with thalidomide

TL;DR: The studies suggest that IMiDs block endogenous substrates (MEIS2) from binding to CRL4CRBN while the ligase complex is recruiting IKZF1 or IKzF3 for degradation, which implies that small molecules can modulate an E3 ubiquitin ligase and thereby upregulate or downregulate the ubiquitination of proteins.