Mechanisms of deubiquitinase specificity and regulation
TET Mevissen, D Komander - Annual review of biochemistry, 2017 - annualreviews.org
Protein ubiquitination is one of the most powerful posttranslational modifications of proteins,
as it regulates a plethora of cellular processes in distinct manners. Simple …
as it regulates a plethora of cellular processes in distinct manners. Simple …
[HTML][HTML] Regulation of proteolysis by human deubiquitinating enzymes
ZM Eletr, KD Wilkinson - Biochimica et Biophysica Acta (BBA)-Molecular …, 2014 - Elsevier
The post-translational attachment of one or several ubiquitin molecules to a protein
generates a variety of targeting signals that are used in many different ways in the cell …
generates a variety of targeting signals that are used in many different ways in the cell …
Structural basis for the activation and inhibition of the UCH37 deubiquitylase
RT VanderLinden, CW Hemmis, B Schmitt, A Ndoja… - Molecular cell, 2015 - cell.com
The UCH37 deubiquitylase functions in two large and very different complexes, the 26S
proteasome and the INO80 chromatin remodeler. We have performed biochemical …
proteasome and the INO80 chromatin remodeler. We have performed biochemical …
Ubiquitin carboxyl-terminal hydrolases: involvement in cancer progression and clinical implications
Y Fang, X Shen - Cancer and Metastasis Reviews, 2017 - Springer
Protein ubiquitination and deubiquitination participate in a number of biological processes,
including cell growth, differentiation, transcriptional regulation, and oncogenesis. Ubiquitin C …
including cell growth, differentiation, transcriptional regulation, and oncogenesis. Ubiquitin C …
The potential role of ubiquitin c-terminal hydrolases in oncogenesis
Y Fang, D Fu, XZ Shen - Biochimica et Biophysica Acta (BBA)-Reviews on …, 2010 - Elsevier
Deubiquitinating enzymes (DUBs), capable of removing ubiquitin (Ub) from protein
substrates, are involved in numerous biological processes. The ubiquitin C-terminal …
substrates, are involved in numerous biological processes. The ubiquitin C-terminal …
Knotting and unknotting of a protein in single molecule experiments
Spontaneous folding of a polypeptide chain into a knotted structure remains one of the most
puzzling and fascinating features of protein folding. The folding of knotted proteins is on the …
puzzling and fascinating features of protein folding. The folding of knotted proteins is on the …
Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2
Rpn13 is a subunit of the proteasome that serves as a receptor for both ubiquitin and Uch37,
one of the proteasome's three deubiquitinating enzymes. We have determined the structure …
one of the proteasome's three deubiquitinating enzymes. We have determined the structure …
Immunotherapy against several tumors including gastrointestinal and gastric cancer
J Fritsche, T Weinschenk, S Walter… - US Patent …, 2015 - Google Patents
The present invention relates to peptides, nucleic acids and cells for use in
immunotherapeutic methods. In particular, the present invention relates to the …
immunotherapeutic methods. In particular, the present invention relates to the …
Structures and folding pathways of topologically knotted proteins
In the last decade, a new class of proteins has emerged that contain a topological knot in
their backbone. Although these structures are rare, they nevertheless challenge our …
their backbone. Although these structures are rare, they nevertheless challenge our …
Structure characterization of the 26S proteasome
In all eukaryotic cells, 26S proteasome plays an essential role in the process of ATP-
dependent protein degradation. In this review, we focus on structure characterization of the …
dependent protein degradation. In this review, we focus on structure characterization of the …