Results 101 to 110 of about 129,362 (255)

E3 Ubiquitin Ligases: Key Regulators of Hormone Signaling in Plants*

Molecular & Cellular Proteomics, 2018
Ubiquitin-mediated control of protein stability is central to most aspects of plant hormone signaling. Attachment of ubiquitin to target proteins occurs via an enzymatic cascade with the final step being catalyzed by a family of enzymes known as E3 ...
Dior R. Kelley
semanticscholar   +1 more source

Regulation of biological processes by ubiquitin ligases: a focus on the Pagano Lab’s contribution

Frontiers in Cell and Developmental Biology
Protein homeostasis depends on many fundamental processes including mRNA synthesis, translation, post-translational modifications, and proteolysis.
Philipp Kaldis, Philipp Kaldis, Lisa A. Porter, Lisa A. Porter   +3 more
doaj   +1 more source

Decoys provide a scalable platform for the identification of plant E3 ubiquitin ligases that regulate circadian function

eLife, 2019
The circadian clock relies on regulated degradation of clock proteins to maintain rhythmicity. Despite this, we know few components that mediate protein degradation.
Ann Feke, Wei Liu, Jing Hong, Man-Wah Li, Chin-Mei Lee, Elton K Zhou, Joshua M Gendron   +6 more
doaj   +1 more source

PUB-MS - a mass-spectrometry-based method to monitor protein-protein proximity in vivo [PDF]

arXiv, 2011
The common techniques to study protein-protein proximity in vivo are not well-adapted to the capabilities and the expertise of a standard proteomics laboratory, typically based on the use of mass spectrometry. With the aim of closing this gap, we have developed PUB-MS (for Proximity Utilizing Biotinylation and Mass Spectrometry), an approach to monitor
arxiv  

Ubiquitin Ligases in Control: Regulating NLRP3 Inflammasome Activation

Frontiers in Bioscience-Landmark
Ubiquitin ligases play pivotal roles in the regulation of NLR family pyrin domain containing 3 (NLRP3) inflammasome activation, a critical process in innate immunity and inflammatory responses.
Swarna Beesetti
doaj   +1 more source

Ubiquitin-dependent degradation of IκBα is mediated by a ubiquitin ligase Skp1/Cul 1/F-box protein FWD1 [PDF]

, 1999
Shigetsugu Hatakeyama, Masatoshi Kitagawa, Keiko Nakayama, Michiko Shirane, Masaki Matsumoto, Kimihiko Hattori, Hideaki Higashi, Hiroyasu Nakano, Ko Okumura, Kazunori Onoé, Robert A. Good, Kei-ichi Nakayama   +11 more
openalex   +1 more source

A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. [PDF]

, 1995
J M Huibregtse, Martin Scheffner, Sylvie Beaudenon, Peter M. Howley   +3 more
openalex   +1 more source

A Network of Ubiquitin Ligases Is Important for the Dynamics of Misfolded Protein Aggregates in Yeast*

Journal of Biological Chemistry, 2012
Background: Misfolded proteins are degraded via the ubiquitin/proteasome pathway or form aggregates that are cleared by autophagy. Results: Several yeast ubiquitin ligases protect against aggregate formation and promote aggregate clearance. Conclusion: A
M. Theodoraki, Nadinath B. Nillegoda, J. Saini, A. Caplan   +3 more
semanticscholar   +1 more source

The Role of Ubiquitin and the 26S Proteasome in Plant Abiotic Stress Signaling

Frontiers in Plant Science, 2014
Ubiquitin is a small, highly conserved, ubiquitously expressed eukaryotic protein with immensely important and diverse regulatory functions. A well-studied function of ubiquitin is its role in selective proteolysis by the ubiquitin-proteasome system (UPS)
Stone L Sophia
doaj   +1 more source

Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53 [PDF]

, 2000
Shengyun Fang, Jane Jensen, Robert L. Ludwig, Karen H. Vousden, Allan M. Weissman   +4 more
openalex   +1 more source