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Journal Article
Nature Communications, ISSN 2041-1723, 10/2016, Volume 7, Issue 1, p. 13166
The COP9 signalosome (CSN) is a central component of the activation and remodelling cycle of cullin-RING E3 ubiquitin ligases (CRLs), the largest enzyme family... 
UBIQUITIN LIGASE COMPLEX | JAB1/CSN5 | CELL LYMPHOMA | SUBSTRATE | MULTIDISCIPLINARY SCIENCES | PROTEASOME | SCF | F-BOX PROTEINS | DEGRADATION | BORTEZOMIB | DEUBIQUITINATION | NEDD8 Protein - metabolism | Peptide Hydrolases - genetics | Pyrazoles - chemical synthesis | Antineoplastic Agents - chemical synthesis | Humans | Gene Expression Regulation, Neoplastic | Intracellular Signaling Peptides and Proteins - metabolism | Molecular Targeted Therapy | COP9 Signalosome Complex - antagonists & inhibitors | Proteolysis - drug effects | Isoenzymes - metabolism | Female | Antineoplastic Agents - pharmacology | Intracellular Signaling Peptides and Proteins - genetics | Lymphoma, Large-Cell, Anaplastic - metabolism | Lymphoma, Large-Cell, Anaplastic - genetics | Peptide Hydrolases - metabolism | Pyrazoles - pharmacology | Isoenzymes - genetics | HCT116 Cells | Intracellular Signaling Peptides and Proteins - antagonists & inhibitors | THP-1 Cells | Ubiquitin-Protein Ligases - metabolism | Azepines - chemical synthesis | NEDD8 Protein - genetics | Mice, SCID | Azepines - pharmacology | Xenograft Model Antitumor Assays | Animals | Tumor Burden - drug effects | Lymphoma, Large-Cell, Anaplastic - drug therapy | COP9 Signalosome Complex - genetics | Lymphoma, Large-Cell, Anaplastic - pathology | Mice | Protein Processing, Post-Translational | Ubiquitin-Protein Ligases - genetics | COP9 Signalosome Complex - metabolism
Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 01/2017, Volume 56, Issue 5, pp. 1294 - 1297
CSN5 is the zinc metalloprotease subunit of the COP9 signalosome (CSN), which is an important regulator of cullin‐RING E3 ubiquitin ligases (CRLs). CSN5 is... 
CSN5 | inhibitors | azaindoles | ubiquitin ligases | metalloproteases | MECHANISM | SCF | HUMAN COP9 SIGNALOSOME | NEDD8 | CANCER | CHEMISTRY, MULTIDISCIPLINARY | Ubiquitin | Ligases | Proteases | Zinc | Binding | Substrate inhibition | Proteinase inhibitors | Cullin | Degradation | Ubiquitination | Inhibitors | Protease inhibitors | Skp2 protein | Metalloproteinase | Viability | Recognition
Journal Article
Biochemical Society Transactions, ISSN 0300-5127, 2003, Volume 31, Issue 6, pp. 1243 - 1247
Journal Article
Current Pharmaceutical Design, ISSN 1381-6128, 01/2007, Volume 13, Issue 3, pp. 271 - 285
Journal Article
Nature Cell Biology, ISSN 1465-7392, 08/2006, Volume 8, Issue 8, pp. 894 - 896
γ-secretase and signal peptide peptidase (SPP) are unusual GxGD aspartyl proteases, which mediate intramembrane proteolysis. In addition to SPP, a family of... 
ENZYME | SIGNAL PEPTIDE PEPTIDASE | SUBSTRATE | NICASTRIN | NOTCH-1 | PROTEOLYSIS | IDENTIFICATION | CELL BIOLOGY
Journal Article
Science, ISSN 0036-8075, 6/2002, Volume 296, Issue 5576, pp. 2215 - 2218
Signal peptide peptidase (SPP) catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. In humans, SPP... 
Comets | Yeasts | Databases | RNA | Presenilins | Neurons | Humans | Amino acids | Reports | Membrane proteins | P branes | TRANSPORT | INTRAMEMBRANE PROTEOLYSIS | PROTEINS | GAMMA-SECRETASE | MULTIDISCIPLINARY SCIENCES | Presenilin-2 | Presenilin-1 | Saccharomyces cerevisiae - genetics | Molecular Sequence Data | Aspartic Acid Endopeptidases - genetics | Azirines - pharmacology | Protease Inhibitors - pharmacology | Aspartic Acid Endopeptidases - isolation & purification | Amyloid Precursor Protein Secretases | Cloning, Molecular | Conserved Sequence | Membrane Proteins - metabolism | Binding Sites | Endoplasmic Reticulum - enzymology | Recombinant Proteins - metabolism | Amino Acid Sequence | Aspartic Acid Endopeptidases - chemistry | Endopeptidases - metabolism | Membrane Proteins - isolation & purification | Azirines - chemical synthesis | Membrane Proteins - genetics | Recombinant Proteins - chemistry | Glycosylation | Amino Acid Motifs | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Membrane Proteins - chemistry | Aspartic Acid Endopeptidases - metabolism | Biotin - pharmacology | Biotin - chemical synthesis | Protease Inhibitors - chemical synthesis | Mutation | Biotin - analogs & derivatives | Cell research | Peptides | Proteolysis | Proteases | Analysis | Research | Alzheimer's disease | Signal peptides | Proteins | Membranes | Biochemistry
Journal Article
Journal of Immunology, ISSN 0022-1767, 03/2012, Volume 188, Issue 6, pp. 2794 - 2804
Journal Article