Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (40206) 40206
Publication (7345) 7345
Book Chapter (708) 708
Book Review (429) 429
Dissertation (200) 200
Conference Proceeding (181) 181
Newsletter (165) 165
Reference (39) 39
Government Document (24) 24
Book / eBook (15) 15
Data Set (6) 6
Trade Publication Article (6) 6
Web Resource (6) 6
Magazine Article (5) 5
Streaming Video (5) 5
Newspaper Article (1) 1
Paper (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
humans (21086) 21086
index medicus (18106) 18106
animals (16145) 16145
biochemistry & molecular biology (11182) 11182
proteasome endopeptidase complex - metabolism (10724) 10724
proteasome (10113) 10113
cell biology (8372) 8372
ubiquitin (7318) 7318
mice (7094) 7094
proteins (6989) 6989
proteasome endopeptidase complex (5663) 5663
degradation (5619) 5619
apoptosis (5240) 5240
proteolysis (4848) 4848
ubiquitin-proteasome system (4675) 4675
ubiquitin - metabolism (4643) 4643
male (4421) 4421
oncology (4393) 4393
proteasome inhibitors (4298) 4298
research (4124) 4124
cell line, tumor (4025) 4025
expression (3912) 3912
female (3860) 3860
cancer (3831) 3831
ubiquitination (3739) 3739
cell line (3703) 3703
article (3632) 3632
phosphorylation (3607) 3607
bortezomib (3392) 3392
signal transduction (3260) 3260
cysteine endopeptidases - metabolism (3249) 3249
multienzyme complexes - metabolism (3158) 3158
physiological aspects (3088) 3088
protein (2979) 2979
activation (2972) 2972
rats (2900) 2900
molecular sequence data (2897) 2897
protein binding (2885) 2885
proteasomes (2884) 2884
amino acid sequence (2879) 2879
mutation (2845) 2845
analysis (2684) 2684
gene expression (2684) 2684
oxidative stress (2633) 2633
cells (2560) 2560
multidisciplinary sciences (2503) 2503
cells, cultured (2370) 2370
ubiquitin-proteasome pathway (2337) 2337
neurosciences (2299) 2299
autophagy (2290) 2290
genetic aspects (2155) 2155
nf-kappa-b (2139) 2139
pathway (2126) 2126
ubiquitin-protein ligases - metabolism (2094) 2094
proteasome endopeptidase complex - genetics (2029) 2029
gene-expression (2000) 2000
research article (1996) 1996
biophysics (1992) 1992
apoptosis - drug effects (1968) 1968
26s proteasome (1942) 1942
biology (1927) 1927
in-vivo (1843) 1843
immunology (1828) 1828
cell cycle (1826) 1826
hela cells (1794) 1794
blotting, western (1767) 1767
genetics & heredity (1726) 1726
20s proteasome (1722) 1722
transfection (1721) 1721
antineoplastic agents - pharmacology (1719) 1719
inhibition (1674) 1674
enzymes (1661) 1661
health aspects (1642) 1642
leupeptins - pharmacology (1628) 1628
pharmacology & pharmacy (1622) 1622
models, biological (1606) 1606
complex (1599) 1599
hematology (1537) 1537
gene (1509) 1509
saccharomyces-cerevisiae (1495) 1495
down-regulation (1479) 1479
medicine (1478) 1478
protein folding (1465) 1465
proteasome inhibitor (1460) 1460
identification (1458) 1458
ubiquitins - metabolism (1441) 1441
proteins - metabolism (1429) 1429
middle aged (1401) 1401
protein structure, tertiary (1401) 1401
in-vitro (1389) 1389
multiple myeloma (1384) 1384
gene expression regulation (1345) 1345
transcription (1339) 1339
kinases (1336) 1336
time factors (1328) 1328
molecular biology (1322) 1322
dna-binding proteins - metabolism (1304) 1304
endoplasmic-reticulum (1304) 1304
life sciences (1285) 1285
biochemistry (1282) 1282
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (40128) 40128
Japanese (294) 294
Chinese (175) 175
French (128) 128
Russian (125) 125
German (104) 104
Korean (40) 40
Polish (39) 39
Spanish (17) 17
Czech (16) 16
Ukrainian (12) 12
Hungarian (5) 5
Portuguese (3) 3
Italian (2) 2
Persian (2) 2
Catalan (1) 1
Dutch (1) 1
Hebrew (1) 1
Malay (1) 1
Swedish (1) 1
Turkish (1) 1
Welsh (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text Corrigendum: Pramel7 mediates ground-state pluripotency through proteasomal-epigenetic combined pathways
by Graf, Urs and Casanova, Elisa A and Wyck, Sarah and Dalcher, Damian and Gatti, Marco and Vollenweider, Eva and Okoniewski, Michal J and Weber, Fabienne A and Patel, Sameera S and Schmid, Marc W and Li, Jiwen and Sharif, Jafar and Wanner, Guido A and Koseki, Haruhiko and Wong, Jiemin and Pelczar, Pawel and Penengo, Lorenza and Santoro, Raffaella and Cinelli, Paolo
Nature cell biology, ISSN 1465-7392, 07/2017, Volume 19, Issue 8, p. 1003
This corrects the article DOI: 10.1038/ncb3554. 
Proteasomes
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Dealing with proteasomal stress: p38δ to the rescue
Journal of Cell Science, ISSN 0021-9533, 07/2018, Volume 131, Issue 14, pp. e1404 - e1404
Proteasomes
Journal Article
Details down arrow
3. Full Text Structure-and function-based design of Plasmodium-selective proteasome inhibitors
by Li, Hao and O'Donoghue, Anthony J and Van Der Linden, Wouter A and Xie, Stanley C and Yoo, Euna and Foe, Ian T and Tilley, Leann and Craik, Charles S and Da Fonseca, Paula C. A and Bogyo, Matthew
Nature, ISSN 0028-0836, 02/2016, Volume 530, Issue 7589, pp. 233 - 236
The proteasome is a multi-component protease complex responsible for regulating key processes such as the cell cycle and antigen presentation(1). Compounds... 
VISUALIZATION | FALCIPARUM MALARIA | MECHANISM | SPECIFICITY | ARTEMISININ RESISTANCE | MULTIDISCIPLINARY SCIENCES | VALIDATION | ELECTRON-MICROSCOPY | IDENTIFICATION | PARASITE | HUMAN 20S PROTEASOME | Plasmodium falciparum - enzymology | Plasmodium - enzymology | Plasmodium chabaudi - enzymology | Species Specificity | Humans | Proteasome Inhibitors - chemistry | Plasmodium - drug effects | Plasmodium falciparum - drug effects | Protein Subunits - metabolism | Dose-Response Relationship, Drug | Artemisinins - pharmacology | Plasmodium chabaudi - physiology | Drug Design | Plasmodium - growth & development | Female | Drug Resistance | Antimalarials - adverse effects | Catalytic Domain | Proteasome Inhibitors - pharmacology | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Proteasome Inhibitors - toxicity | Proteasome Inhibitors - adverse effects | Antimalarials - pharmacology | Cryoelectron Microscopy | Drug Synergism | Animals | Substrate Specificity - drug effects | Proteasome Endopeptidase Complex - ultrastructure | Antimalarials - chemistry | Plasmodium chabaudi - drug effects | Mice | Mice, Inbred BALB C | Protein Subunits - antagonists & inhibitors | Protein Subunits - chemistry | Antimalarials - toxicity | Enzyme Activation | Plasmodium falciparum - growth & development | Proteasome Endopeptidase Complex - metabolism | Ubiquitin-proteasome system | Plasmodium | Health aspects | Proteins | Malaria | Protease inhibitors | Proteases | Erythrocytes | Ligands | Parasites | Drug dosages
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. Full Text Recognition and processing of ubiquitin-protein conjugates by the proteasome
by Finley, Daniel
Annual Review of Biochemistry, ISSN 0066-4154, 2009, Volume 78, Issue 1, pp. 477 - 513
The proteasome is an intricate molecular machine, which serves to degrade proteins following their conjugation to ubiquitin. Substrates dock onto the... 
Ubiquitin | Protein degradation | Protease | Deubiquitination | Proteasome | proteasome | MULTIUBIQUITIN-CHAIN-BINDING | REG-GAMMA PROTEASOME | BIOCHEMISTRY & MOLECULAR BIOLOGY | SACCHAROMYCES-CEREVISIAE | ubiquitin | protease | 20S PROTEASOME | UCH37 DEUBIQUITINATING ENZYME | deubiquitination | CELL-CYCLE | 19S REGULATORY PARTICLE | DNA-REPAIR | 26 S-PROTEASOME | protein degradation | ATP-DEPENDENT PROTEASES | Animals | Arabidopsis - enzymology | Proteins - metabolism | Humans | Ubiquitin - chemistry | Ubiquitin - metabolism | Proteasome Endopeptidase Complex - chemistry | Proteasome Endopeptidase Complex - metabolism | Chemical properties | Genetic regulation | Ubiquitin-proteasome system | Proteolysis | Analysis | Adenosine triphosphatase
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text Molecular architecture and assembly of the eukaryotic proteasome
by Tomko Jr, Robert J and Hochstrasser, Mark
Annual Review of Biochemistry, ISSN 0066-4154, 06/2013, Volume 82, Issue 1, pp. 415 - 445
The eukaryotic ubiquitin-proteasome system is responsible for most aspects of regulatory and quality-control protein degradation in cells. Its substrates,... 
Ubiquitin | Deubiquitylation | Proteolysis | ATPase | Assembly | Proteasome | proteasome | BIOCHEMISTRY & MOLECULAR BIOLOGY | YEAST 26S PROTEASOME | METHANOCALDOCOCCUS-JANNASCHII | SACCHAROMYCES-CEREVISIAE | ubiquitin | deubiquitylation | 2.75 ANGSTROM RESOLUTION | STRUCTURAL BASIS | MAMMALIAN 20S PROTEASOMES | assembly | 19S REGULATORY PARTICLE | S-PROTEASOME | proteolysis | CORE PARTICLE | PRECURSOR COMPLEXES | Cryoelectron Microscopy | Animals | Molecular Chaperones - metabolism | Eukaryota | Humans | Ubiquitin - metabolism | Proteasome Endopeptidase Complex - chemistry | Proteasome Endopeptidase Complex - metabolism | Physiological aspects | Research | Molecular biology | Ubiquitin-proteasome system | Adenosine triphosphatase
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text Structural Biology of the Proteasome
by Kish-Trier, Erik and Hill, Christopher P
Annual Review of Biophysics, ISSN 1936-122X, 5/2013, Volume 42, Issue 1, pp. 29 - 49
The proteasome refers to a collection of complexes centered on the 20S proteasome core particle (20S CP), a complex of 28 subunits that houses proteolytic... 
regulated degradation | macromolecule assembly | intracellular proteolysis | conformational changes | proteasome structure | regulated degradation proteasome structure | DEUBIQUITINATING ENZYME | REGULATORY PARTICLE | COMPLEX | PROTEIN | CRYSTAL-STRUCTURE | 26S PROTEASOME | 20S PROTEASOME | BIOPHYSICS | DEGRADATION | S-PROTEASOME | SUBUNIT | Archaea - metabolism | Bacteria - metabolism | Animals | Molecular Chaperones - metabolism | Humans | Models, Molecular | Nuclear Magnetic Resonance, Biomolecular | Proteasome Endopeptidase Complex - chemistry | Protein Subunits - chemistry | Proteasome Endopeptidase Complex - metabolism | Eukaryota - metabolism | Proteins | Physiological aspects | Research | Ubiquitin-proteasome system | Molecular biology | Structure | X-ray crystallography | electron microscopy | nuclear magnetic resonance
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text Proteasome Structure and Assembly
by Budenholzer, Lauren and Cheng, Chin Leng and Li, Yanjie and Hochstrasser, Mark
Journal of Molecular Biology, ISSN 0022-2836, 11/2017, Volume 429, Issue 22, pp. 3500 - 3524
The eukaryotic 26S proteasome is a large multisubunit complex that degrades the majority of proteins in the cell under normal conditions. The 26S proteasome... 
ubiquitin proteasome system | proteasome | proteasome assembly | protein degradation | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | UBIQUITIN-LIKE PROTEIN | YEAST 26S PROTEASOME | TRANSCRIPTION FACTOR NRF1 | BETA-TYPE SUBUNITS | MAMMALIAN 20S PROTEASOMES | 19S REGULATORY PARTICLE | REVEALS FUNCTIONAL ASYMMETRIES | CORE PARTICLE | AAA PLUS UNFOLDASE | Cryoelectron Microscopy | Eukaryotic Cells - enzymology | Proteasome Endopeptidase Complex - metabolism | Proteasome Endopeptidase Complex - ultrastructure | Protein Multimerization | Ubiquitin | Proteolysis | Phosphatases
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text The Logic of the 26S Proteasome
by Collins, Galen Andrew and Goldberg, Alfred L
Cell, ISSN 0092-8674, 05/2017, Volume 169, Issue 5, pp. 792 - 806
The ubiquitin proteasome pathway is responsible for most of the protein degradation in mammalian cells. Rates of degradation by this pathway have generally... 
ubiquitin proteasome system | protein turnover | protein degradation | proteasome phosphorylation | DEUBIQUITINATING ENZYME | REGULATORY PARTICLE | EUKARYOTIC PROTEASOME | 20 S PROTEASOMES | PROTEIN-DEGRADATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOLECULAR-WEIGHT PROTEASES | MEDIATED DEGRADATION | MISFOLDED PROTEINS | FUNCTIONAL ASYMMETRIES | BRANCHED UBIQUITIN CHAINS | CELL BIOLOGY | Phosphorylation | Ubiquitination | Animals | Proteolysis | Allosteric Regulation | Humans | Eukaryota - chemistry | Adenosine Triphosphatases - metabolism | Proteasome Endopeptidase Complex - chemistry | Proteasome Endopeptidase Complex - metabolism | Eukaryota - metabolism | Ubiquitin | Cells
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights