X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (93425) 93425
Newsletter (838) 838
Book Chapter (170) 170
Newspaper Article (150) 150
Book / eBook (69) 69
Publication (25) 25
Conference Proceeding (20) 20
Dissertation (20) 20
Magazine Article (10) 10
Government Document (9) 9
Reference (7) 7
Transcript (5) 5
Book Review (3) 3
Web Resource (3) 3
Trade Publication Article (2) 2
Journal / eJournal (1) 1
Paper (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
humans (69310) 69310
biochemistry & molecular biology (39330) 39330
animals (36126) 36126
cancer (28951) 28951
cell biology (28822) 28822
oncology (25827) 25827
cell line, tumor (23708) 23708
apoptosis (22779) 22779
mice (21759) 21759
female (21245) 21245
expression (19297) 19297
tumors (17679) 17679
proteins (17094) 17094
male (15864) 15864
gene expression (15594) 15594
research (13989) 13989
tumor suppressor protein p53 - metabolism (12841) 12841
signal transduction (12577) 12577
p53 (11703) 11703
genetic aspects (11485) 11485
mutation (11237) 11237
genetics & heredity (10937) 10937
gene expression regulation, neoplastic (10515) 10515
phosphorylation (10195) 10195
cell proliferation (10063) 10063
cell cycle (9336) 9336
metastasis (9144) 9144
middle aged (9096) 9096
activation (8863) 8863
analysis (8799) 8799
research article (8692) 8692
tumor suppressor protein p53 - genetics (8689) 8689
protein (8269) 8269
kinases (7893) 7893
genes (7527) 7527
gene (7525) 7525
breast cancer (7500) 7500
health aspects (7492) 7492
cells (7307) 7307
medicine (7250) 7250
multidisciplinary sciences (7241) 7241
cell line (7190) 7190
growth (7181) 7181
aged (7161) 7161
biology (7104) 7104
biochemistry (7100) 7100
molecular sequence data (7019) 7019
adult (7018) 7018
immunohistochemistry (6979) 6979
tumor proteins (6979) 6979
tumor-suppressor (6947) 6947
physiological aspects (6761) 6761
protein binding (6648) 6648
apoptosis - drug effects (6647) 6647
tumor cells, cultured (6632) 6632
prognosis (6443) 6443
development and progression (6320) 6320
down-regulation (5908) 5908
base sequence (5614) 5614
gene-expression (5512) 5512
tumor suppressor proteins - metabolism (5488) 5488
dna damage (5483) 5483
proliferation (5431) 5431
breast-cancer (5341) 5341
science (5336) 5336
care and treatment (5323) 5323
amino acid sequence (5289) 5289
dna (5231) 5231
transfection (5164) 5164
inhibition (5085) 5085
tumor suppressor genes (5057) 5057
tumor suppressor proteins - genetics (4987) 4987
blotting, western (4951) 4951
transcription (4817) 4817
cell growth (4771) 4771
antineoplastic agents - pharmacology (4759) 4759
dna methylation (4749) 4749
biophysics (4715) 4715
carcinoma (4698) 4698
identification (4669) 4669
deoxyribonucleic acid--dna (4622) 4622
genetics (4622) 4622
micrornas - genetics (4617) 4617
chemotherapy (4508) 4508
cells, cultured (4433) 4433
life sciences (4424) 4424
tumorigenesis (4385) 4385
molecular biology (4374) 4374
review (4365) 4365
cancer research (4348) 4348
cell proliferation - drug effects (4293) 4293
tumor suppressor proteins (4064) 4064
cancer therapies (4048) 4048
binding sites (4028) 4028
dna-binding proteins - metabolism (4004) 4004
in-vivo (4004) 4004
transcription factors (3940) 3940
pathology (3801) 3801
up-regulation (3706) 3706
microrna (3692) 3692
more...
Library Location Library Location
Library Location Library Location
X
Sort by Item Count (A-Z)
Filter by Count
Gerstein Science - Stacks (21) 21
Collection Dvlpm't (Acquisitions) - Vendor file (7) 7
Online Resources - Online (5) 5
Sunnybrook Health Sciences Centre - Sunnybrook Stacks (4) 4
UofT at Mississauga - Stacks (4) 4
Collection Dvlpm't (Acquisitions) - Closed Orders (2) 2
Earth Sciences (Noranda) - Circulation Desk (2) 2
Earth Sciences (Noranda) - Oversize (2) 2
Earth Sciences (Noranda) - Stacks (2) 2
Gerstein Science - Circulation Desk (2) 2
Gerstein Science - Reserve desk (2) 2
St. Michael's College (John M. Kelly) - 2nd Floor (2) 2
Trinity College (John W Graham) - Stacks (2) 2
UofT at Mississauga - Circulation Desk (2) 2
Victoria University E.J. Pratt - Circulation Desk (2) 2
Victoria University E.J. Pratt - Oversize (2) 2
Gerstein Science - Bindery (1) 1
Gerstein Science - Periodical Stacks (1) 1
St. Michael's Hospital - Circulation Desk (1) 1
St. Michael's Hospital - Stacks (1) 1
UofT at Scarborough - Stacks (1) 1
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (94503) 94503
Japanese (245) 245
Chinese (184) 184
French (49) 49
German (45) 45
Russian (44) 44
Portuguese (39) 39
Spanish (36) 36
Italian (19) 19
Polish (18) 18
Dutch (13) 13
Korean (13) 13
Norwegian (13) 13
Hungarian (9) 9
Romanian (9) 9
Czech (8) 8
Turkish (3) 3
Arabic (2) 2
Croatian (2) 2
Corsican (1) 1
Danish (1) 1
Ukrainian (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Nature (London), ISSN 0028-0836, 08/2009, Volume 460, Issue 7257, pp. 904 - 908
.... aUPD is associated not only with loss-of-function mutations of tumour suppressor genes... 
TRANSFORMATION | PROTEIN | RETROVIRAL VECTOR GCDNSAP | NEGATIVE REGULATION | MULTIDISCIPLINARY SCIENCES | HEMATOPOIETIC STEM-CELLS | V-CBL | MUTATIONS | UBIQUITIN LIGASES | MYELODYSPLASTIC SYNDROMES | P53 | NIH 3T3 Cells | Neoplasm Transplantation | ras Proteins - genetics | Phosphorylation | Proto-Oncogene Proteins c-cbl - metabolism | Humans | Leukemia, Myeloid - genetics | Molecular Sequence Data | ras Proteins - metabolism | Male | Leukemia, Myeloid - pathology | Allelic Imbalance | Ubiquitination | Base Sequence | Female | Proto-Oncogene Proteins c-cbl - deficiency | Genes, Tumor Suppressor | Proto-Oncogene Proteins c-cbl - genetics | Amino Acid Sequence | Oncogenes - genetics | Mutant Proteins - genetics | Models, Molecular | Mutant Proteins - metabolism | Chromosomes, Human, Pair 11 - genetics | Proto-Oncogene Proteins c-cbl - chemistry | Mice, Knockout | Animals | Uniparental Disomy - genetics | Leukemia, Myeloid - metabolism | Mice, Nude | Mutant Proteins - chemistry | Proto-Oncogene Proteins c-cbl - antagonists & inhibitors | Protein Conformation | Mice | Mutation | Gene mutations | Myelocytic leukemia | Physiological aspects | Tumor suppressor genes | Development and progression | Genetic aspects | Nonlymphoid leukemia | Research | Protein kinases | Proteins | Genes | Amino acids | Kinases | Cells | Clinical outcomes | Crystal structure | cytokine sensitivity | tumor suppressor | myelodysplasia | 490 | LOH | ubiquitination
Journal Article
Nature structural & molecular biology, ISSN 1545-9985, 2010, Volume 17, Issue 10, pp. 1247 - 1254
... of genome stability after mutations in proteins that carry out repair through homologous recombination, such as BRCA2 (refs. 2,3). In mammalian cells, homologous... 
POLY(ADP-RIBOSE) POLYMERASE | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | DOUBLE-STRAND BREAKS | HISTONE H2AX | FANCONI-ANEMIA | CELL BIOLOGY | RAD51 | BIOPHYSICS | IN-VIVO | SUSCEPTIBILITY GENE | D-LOOP FORMATION | DNA-REPAIR | Recombination, Genetic - physiology | DNA, Neoplasm - metabolism | Humans | Neoplasm Proteins - physiology | DNA Repair - physiology | Molecular Sequence Data | Structure-Activity Relationship | DNA Breaks, Double-Stranded | BRCA2 Protein - physiology | Breast Neoplasms - metabolism | Base Sequence | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Female | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Nucleic Acid Conformation | Fanconi Anemia Complementation Group N Protein | Peptide Fragments - metabolism | Neoplasm Proteins - chemistry | Nuclear Proteins - chemistry | Poly(ADP-ribose) Polymerase Inhibitors | Protein Interaction Mapping | Tumor Suppressor Proteins - physiology | Peptide Fragments - chemistry | Apoptosis Regulatory Proteins | Models, Biological | Rad51 Recombinase - chemistry | Rad51 Recombinase - physiology | BRCA2 Protein - chemistry | Nuclear Proteins - physiology | Poly (ADP-Ribose) Polymerase-1 | Breast cancer | Genetic aspects | Research | BRCA mutations | Ovarian cancer | Proteins | Mutation | Molecular biology | Prostate cancer | homologous recombination | BRCA2 | PALB2
Journal Article
The FEBS Journal, ISSN 1742-464X, 10/2017, Volume 284, Issue 19, pp. 3218 - 3229
.... 1H, 15N spectra showed that the C‐terminal SH3 domain of BIN1 isoform 1 (BIN1Iso1) is not mobile in solution but locked with the core of the protein... 
SH3 domain | nuclear magnetic resonance spectroscopy | protein–protein interaction | Tau | BIN1 | Alzheimer's disease | ALZHEIMERS-DISEASE | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | PATHOLOGY | MODEL | IDENTIFIES VARIANTS | AMPHIPHYSIN | MEMBRANE CURVATURE | protein-protein interaction | BINDING | EXPRESSION | GENOME-WIDE ASSOCIATION | Adaptor Proteins, Signal Transducing - chemistry | Humans | Peptides - genetics | tau Proteins - metabolism | tau Proteins - chemistry | Peptides - metabolism | Protein Isoforms - metabolism | tau Proteins - genetics | Protein Isoforms - chemistry | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Nuclear Magnetic Resonance, Biomolecular | Neurons - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Binding Sites | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Tumor Suppressor Proteins - metabolism | Neurons - chemistry | Peptides - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Nuclear Proteins - chemistry | Amino Acid Motifs | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Adaptor Proteins, Signal Transducing - genetics | Protein Binding | Kinetics | Adaptor Proteins, Signal Transducing - metabolism | Protein Isoforms - genetics | Nuclear magnetic resonance spectroscopy | Neurons | Protein-protein interactions | Spectroscopy | Clathrin | Nuclear magnetic resonance--NMR | Peptides | Neurodegenerative diseases | Pathogenesis | Complexity | Proteins | Magnetic resonance spectroscopy | Tau protein | Spectrum analysis | Isoforms | Alzheimers disease | Binding sites | tau Proteins/metabolism | Nuclear Proteins/chemistry | Protein Isoforms/chemistry | Protein Isoforms/genetics | Adaptor Proteins, Signal Transducing/genetics | Recombinant Proteins/metabolism | Peptides/metabolism | Life Sciences | Recombinant Proteins/chemistry | Adaptor Proteins, Signal Transducing/chemistry | Nuclear Proteins/metabolism | Tumor Suppressor Proteins/chemistry | Nuclear Proteins/genetics | Tumor Suppressor Proteins/metabolism | Protein Isoforms/metabolism | Peptides/chemistry | Recombinant Proteins/genetics | Biochemistry, Molecular Biology | Escherichia coli/genetics | Escherichia coli/metabolism | Adaptor Proteins, Signal Transducing/metabolism | Neurons/chemistry | Tumor Suppressor Proteins/genetics | tau Proteins/genetics | Neurons/metabolism | Peptides/genetics | tau Proteins/chemistry
Journal Article
Nature structural & molecular biology, ISSN 1545-9985, 2010, Volume 17, Issue 10, pp. 1255 - 1259
Journal Article
by Chu, Y and Yang, X
Oncogene, ISSN 1476-5594, 2010, Volume 30, Issue 9, pp. 1108 - 1116
.... Despite increasing recognition of the importance of this process, an extremely limited number of small ubiquitin-like modifier (SUMO) protein ligases (E3s... 
Mdm2 | TRIM proteins | sumoylation | SUMOE3 ligase | PML | p53 | BIOCHEMISTRY & MOLECULAR BIOLOGY | PML NUCLEAR-BODIES | DNA-DAMAGE | REGULATES P53 | FAMILY PROTEINS | SUMO E3 ligase | UBIQUITIN LIGASES | CELL BIOLOGY | RET FINGER PROTEIN | ONCOLOGY | GENETICS & HEREDITY | TUMOR-SUPPRESSOR | C-JUN | Immunoprecipitation | Transcription Factors - chemistry | Humans | Tumor Suppressor Protein p53 - genetics | DNA-Binding Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - genetics | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Proto-Oncogene Proteins c-mdm2 - metabolism | Cell Line | Tumor Suppressor Proteins - metabolism | Small Ubiquitin-Related Modifier Proteins - metabolism | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | Nuclear Proteins - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Transcription Factors - metabolism | Animals | Small Ubiquitin-Related Modifier Proteins - chemistry | Ubiquitin-Conjugating Enzymes - metabolism | Protein Binding | Sumoylation | RNA, Small Interfering | Ubiquitin-Protein Ligases - genetics | Microscopy, Fluorescence | Promyelocytic Leukemia Protein | Physiological aspects | Tumor suppressor genes | Research | Tumor proteins | Ligases | Proteins | Enzymes | Biochemistry | Cellular biology | Gene expression
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2017, Volume 292, Issue 37, pp. 15205 - 15215
... reactivation in cancer are not well-understood. Surprisingly, here we found occupancy of the metastasis suppressor non-metastatic 2 (NME2... 
CELLS | ACTIVATION | NM23-H2 | DNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | TRANSCRIPTION | GENE-EXPRESSION | HUMAN CANCERS | PROMOTER | GENOME | Epigenetic Repression | Humans | Protein Multimerization | Neoplasm Proteins - antagonists & inhibitors | Fibrosarcoma - metabolism | Neoplasm Proteins - metabolism | NM23 Nucleoside Diphosphate Kinases - genetics | NM23 Nucleoside Diphosphate Kinases - metabolism | Repressor Proteins - antagonists & inhibitors | Fibrosarcoma - pathology | Telomerase - genetics | Chromatin Immunoprecipitation | RNA Interference | Carcinoma - enzymology | G-Quadruplexes | Telomerase - metabolism | Carcinoma - pathology | Neoplasm Proteins - genetics | Genes, Reporter | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | NM23 Nucleoside Diphosphate Kinases - chemistry | Promoter Regions, Genetic | Repressor Proteins - chemistry | Mutagenesis, Site-Directed | Histone Demethylases - chemistry | NM23 Nucleoside Diphosphate Kinases - antagonists & inhibitors | Cells, Cultured | Recombinant Proteins - chemistry | Repressor Proteins - genetics | Neoplasm Proteins - chemistry | Histone Demethylases - metabolism | Point Mutation | Cell Line, Tumor | Carcinoma - metabolism | Telomerase - antagonists & inhibitors | Fibrosarcoma - enzymology | Amino Acid Substitution | Gene Regulation | transcription regulation | chromatin modification | G-quadruplex | telomerase reverse transcriptase (TERT) | NME2 | REST repressor complex | epigenetics
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 08/2013, Volume 135, Issue 31, pp. 11623 - 11633
Journal Article
PLoS biology, ISSN 1545-7885, 2019, Volume 17, Issue 7, pp. e3000367 - e3000367
.... E7 is one of the two HPV-encoded oncoproteins and directs recruitment and subsequent degradation of tumor-suppressive proteins such as retinoblastoma protein (pRb... 
COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | BIOLOGY | INDEPENDENT FUNCTIONS | DIMERIZATION | DEGRADATION | TYROSINE PHOSPHATASES | MECHANISMS | IDENTIFICATION | TYPE-16 E7 | Oncogene Proteins, Viral - chemistry | Humans | Uterine Cervical Neoplasms - pathology | DNA-Binding Proteins - metabolism | Protein Tyrosine Phosphatases, Non-Receptor - chemistry | Uterine Cervical Neoplasms - metabolism | Protein Tyrosine Phosphatases, Non-Receptor - genetics | HEK293 Cells | Protein Domains | Female | Oncogene Proteins, Viral - genetics | Retinoblastoma Protein - chemistry | Oncogene Proteins, Viral - metabolism | Amino Acid Sequence | Cell Line | Retinoblastoma Protein - metabolism | Models, Molecular | DNA-Binding Proteins - genetics | Uterine Cervical Neoplasms - genetics | DNA-Binding Proteins - chemistry | Sequence Homology, Amino Acid | Cell Transformation, Neoplastic | Retinoblastoma Protein - genetics | Protein Tyrosine Phosphatases, Non-Receptor - metabolism | Cell Line, Tumor | Protein Binding | HeLa Cells | Proteins | Tyrosine | Phosphatases | Crystals | Structure | Papillomavirus infections | Cervical cancer | Protein binding | Tumors | Cell proliferation | Biotechnology | Transformation | Phosphorylation | Leukocyte migration | Funding | Kinases | Phosphatase | Degradation | Human papillomavirus | Human papilloma viruses | Tumorigenesis | Catalysis | Genotypes | Supervision | Crystal structure | Binding | Retinoblastoma protein | Cervix | Metabolism | Mutagenesis | Tumor suppressor genes | Software | Disruption | Retinoblastoma | Cell migration | Cancer | Structural analysis | Protein-tyrosine-phosphatase | Index Medicus
Journal Article