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Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 4016 - 14
Journal Article
Nature, ISSN 0028-0836, 12/2015, Volume 528, Issue 7582, pp. 422 - 426
Journal Article
Nature Communications, ISSN 2041-1723, 11/2016, Volume 7, Issue 1, p. 12810
  Directed cell movement involves spatial and temporal regulation of the cortical microtubule (Mt) and actin networks to allow focal adhesions (FAs) to... 
Life Sciences
Journal Article
Nature Communications, ISSN 2041-1723, 12/2016, Volume 7, Issue 1
Journal Article
Nature Medicine, ISSN 1078-8956, 09/2017, Volume 23, Issue 9, pp. 1046 - 1054
It is generally assumed that recurrent mutations within a given cancer driver gene elicit similar drug responses. Cancer genome studies have identified... 
MEDICINE, RESEARCH & EXPERIMENTAL | BROMODOMAIN INHIBITORS | ENDOMETRIAL CARCINOMAS | UBIQUITIN LIGASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | TUMORS | CELL BIOLOGY | BREAST-CANCER | GENOMIC LANDSCAPE | PROSTATE-CANCER | RESISTANCE | MUTATIONS | Immunohistochemistry | Neoplasms, Cystic, Mucinous, and Serous - metabolism | Neoplasm Transplantation | Prostatic Neoplasms - metabolism | Immunoprecipitation | Apoptosis - drug effects | Heterocyclic Compounds, 3-Ring - pharmacology | Epigenesis, Genetic | Humans | Endometrial Neoplasms - metabolism | Drug Resistance, Neoplasm | Immunoblotting | Male | Molecular Targeted Therapy | Carcinoma, Endometrioid - metabolism | Neoplasms, Cystic, Mucinous, and Serous - genetics | Ubiquitination | Prostatic Neoplasms - genetics | Endometrial Neoplasms - genetics | Mass Spectrometry | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Chromatography, Liquid | Cullin Proteins - metabolism | Female | Nuclear Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | RNA-Binding Proteins - antagonists & inhibitors | Acetanilides - pharmacology | Carcinoma, Endometrioid - genetics | Carcinosarcoma - metabolism | Adenocarcinoma, Clear Cell - metabolism | Repressor Proteins - genetics | Nuclear Proteins - metabolism | Transcription Factors - antagonists & inhibitors | Reverse Transcriptase Polymerase Chain Reaction | Azepines - pharmacology | Transcription Factors - metabolism | Triazoles - pharmacology | Animals | Mice, Nude | Nuclear Proteins - antagonists & inhibitors | Cell Line, Tumor | Carcinosarcoma - genetics | Cell Proliferation - drug effects | Mutation | Adenocarcinoma, Clear Cell - genetics | RNA-Binding Proteins - metabolism | Care and treatment | Gene mutations | Proteolysis | Physiological aspects | Genetic aspects | Research | Cancer | Ubiquitin | Biodegradation | Inhibitor drugs | Endometrial cancer | Genomes | Pharmacology | Substrates | Mutants | Degradation | Proteins | Sensitivity | Missense mutation | Inhibitors | Bet protein | Gene mapping | Prostate cancer | Prostate | Endometrium | Ubiquitin-protein ligase
Journal Article
Nature, ISSN 0028-0836, 02/2011, Volume 470, Issue 7333, pp. 227 - 235
The anaphase-promoting complex or cyclosome (APC/C) is an unusually large E3 ubiquitin ligase responsible for regulating defined cell cycle transitions.... 
OVERLAP EXTENSION | APC/C | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | EVOLUTIONARY CONSERVATION | PROTEIN COMPLEXES | MACROMOLECULAR ASSEMBLIES | SACCHAROMYCES-CEREVISIAE | MASS-SPECTROMETRY | SUBSTRATE RECOGNITION | COMPLEX/CYCLOSOME | Anaphase-Promoting Complex-Cyclosome | Molecular Weight | Saccharomyces cerevisiae - genetics | Schizosaccharomyces - chemistry | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome | Substrate Specificity | Holoenzymes - chemistry | Structure-Activity Relationship | Protein Subunits - metabolism | Ubiquitination | Holoenzymes - metabolism | Apc2 Subunit, Anaphase-Promoting Complex-Cyclosome | Protein Subunits - isolation & purification | Mass Spectrometry | Saccharomyces cerevisiae Proteins - isolation & purification | Scattering, Radiation | Recombinant Proteins - metabolism | Saccharomyces cerevisiae Proteins - ultrastructure | Cell Line | Biocatalysis | Recombinant Proteins - ultrastructure | Models, Molecular | Recombinant Proteins - chemistry | Microscopy, Electron | Ubiquitin-Protein Ligase Complexes - chemistry | Saccharomyces cerevisiae - chemistry | Amino Acid Motifs | Animals | Ubiquitin-Protein Ligase Complexes - metabolism | Holoenzymes - ultrastructure | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Apc5 Subunit, Anaphase-Promoting Complex-Cyclosome | Protein Conformation | Protein Subunits - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Ubiquitin-Protein Ligase Complexes - ultrastructure | Ubiquitin | Proteins | Ligases | Models | Chemical properties | Structure | Anaphase | Enzymes | Phosphorylation | Microscopy
Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, p. 4016
Journal Article
eLife, ISSN 2050-084X, 03/2016, Volume 5, Issue 2016
The COP9-Signalosome (CSN) regulates cullin-RING ubiquitin ligase (CRL) activity and assembly by cleaving Nedd8 from cullins. Free CSN is autoinhibited, and it... 
JAB1/CSN5 | COP9 SIGNALOSOME | SCF | BIOLOGY | ARCHITECTURE | DYNAMICS | NEDD8 | CLEAVAGE | INHIBITOR | INSIGHTS | CSN | Physiological aspects | Observations | Ligases | Protein-protein interactions | Ubiquitin | Bioengineering | Enzymes | Microscopy | Affinity | Biology | Ubiquitin-protein ligase | Cullin
Journal Article
Nature Communications, ISSN 2041-1723, 08/2016, Volume 7, Issue 1, p. 12628
Human CtIP is a decisive factor in DNA double-strand break repair pathway choice by enabling DNA-end resection, the first step that differentiates homologous... 
E3 LIGASE | DAMAGE RESPONSE | STRAND BREAK REPAIR | NRF2 | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | UBIQUITYLATION | KEAP1 | CELL-CYCLE | HOMOLOGOUS RECOMBINATION | INSIGHTS
Journal Article
EMBO Molecular Medicine, ISSN 1757-4676, 10/2015, Volume 7, Issue 10, pp. 1285 - 1306
Journal Article