X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (1082) 1082
Publication (209) 209
Book / eBook (52) 52
Book Review (11) 11
Book Chapter (9) 9
Conference Proceeding (1) 1
Data Set (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (508) 508
humans (365) 365
animals (355) 355
biochemistry & molecular biology (339) 339
proteins (291) 291
dna (288) 288
cell biology (246) 246
research (217) 217
dna replication (210) 210
molecular sequence data (199) 199
dna helicases - metabolism (192) 192
multidisciplinary sciences (182) 182
research article (180) 180
mutation (164) 164
dna-binding proteins - metabolism (163) 163
genetic aspects (158) 158
deoxyribonucleic acid--dna (152) 152
protein binding (151) 151
microscopy, electron (144) 144
dna repair (135) 135
genomes (134) 134
genes (131) 131
base sequence (129) 129
dna helicases - genetics (126) 126
protein (126) 126
models, molecular (125) 125
amino acid sequence (119) 119
article (118) 118
gene expression (117) 117
genetics (117) 117
biology (116) 116
analysis (115) 115
genetics & heredity (114) 114
molecular biology (112) 112
physiological aspects (105) 105
dna helicases (104) 104
saccharomyces-cerevisiae (104) 104
mice (102) 102
virology (100) 100
genomics (97) 97
escherichia-coli (96) 96
rna (96) 96
dna - metabolism (94) 94
dna damage (94) 94
microbiology (93) 93
medicine (91) 91
science (91) 91
viruses (90) 90
dna helicases - chemistry (88) 88
electron microscopy (88) 88
replication (87) 87
cell cycle (86) 86
deoxyribonucleic acid (86) 86
dna-binding proteins - genetics (86) 86
male (86) 86
nucleic acid conformation (86) 86
chromatin (82) 82
female (82) 82
binding sites (80) 80
chromosomes (79) 79
transcription (79) 79
biochemistry (77) 77
dna - chemistry (77) 77
adenosine triphosphatases - metabolism (76) 76
dna helicases - ultrastructure (75) 75
saccharomyces cerevisiae - genetics (75) 75
crystal-structure (74) 74
transcription, genetic (74) 74
binding (72) 72
enzymes (72) 72
dna - ultrastructure (70) 70
phylogeny (70) 70
recombination, genetic (70) 70
cells (69) 69
nuclear proteins - metabolism (69) 69
gene (68) 68
cell line (67) 67
dna-binding proteins - chemistry (67) 67
helicase (67) 67
telomere - ultrastructure (67) 67
yeast (67) 67
expression (65) 65
sequence analysis, dna (65) 65
dna-binding proteins - ultrastructure (64) 64
protein structure, tertiary (63) 63
life sciences (62) 62
recombination (61) 61
chromatin - ultrastructure (60) 60
protein conformation (60) 60
saccharomyces cerevisiae proteins - metabolism (60) 60
genome, viral (59) 59
identification (59) 59
biophysics (57) 57
escherichia coli - genetics (57) 57
hela cells (56) 56
homologous recombination (56) 56
plasmids (56) 56
bacteria (54) 54
bacterial proteins - metabolism (54) 54
sequence alignment (54) 54
more...
Library Location Library Location
Library Location Library Location
X
Sort by Item Count (A-Z)
Filter by Count
Gerstein Science - Stacks (42) 42
UTL at Downsview - May be requested (10) 10
UofT at Mississauga - Stacks (9) 9
Collection Dvlpm't (Acquisitions) - Closed Orders (6) 6
Collection Dvlpm't (Acquisitions) - Vendor file (6) 6
UofT at Scarborough - Stacks (6) 6
Online Resources - Online (3) 3
Chemistry (A D Allen) - Stacks (2) 2
Earth Sciences (Noranda) - Stacks (2) 2
Gerstein Science - Reference (2) 2
UofT at Scarborough - Withdrawn (2) 2
Engineering & Comp. Sci. - Stacks (1) 1
Physics - Missing (1) 1
St. Michael's Hospital - Stacks (1) 1
Sunnybrook Health Sciences Centre - Sunnybrook Stacks (1) 1
Trinity College (John W Graham) - Oversize (1) 1
UofT at Mississauga - Reference (1) 1
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (1138) 1138
Spanish (10) 10
Czech (2) 2
Arabic (1) 1
German (1) 1
Italian (1) 1
Japanese (1) 1
Portuguese (1) 1
Russian (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Nature, ISSN 0028-0836, 02/2017, Volume 542, Issue 7641, pp. 377 - 380
The spliceosome excises introns from pre-mRNAs in two sequential transesterifications-branching and exon ligation(1)-catalysed at a single catalytic metal site... 
2ND STEP | ANGSTROM RESOLUTION | ELECTRON CRYOMICROSCOPY | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | FUNCTIONAL INTERACTIONS | CATALYTIC CENTER | CRYO-EM STRUCTURE | SPLICING FACTOR | SITE CHOICE | PRE-MESSENGER-RNA | RNA Helicases - metabolism | Spliceosomes - chemistry | Saccharomyces cerevisiae - genetics | Cell Cycle Proteins - ultrastructure | Ribonucleoprotein, U5 Small Nuclear - metabolism | RNA Splicing Factors - chemistry | Saccharomyces cerevisiae - ultrastructure | Ribonucleoprotein, U4-U6 Small Nuclear - metabolism | Ribonucleoprotein, U4-U6 Small Nuclear - ultrastructure | RNA Helicases - ultrastructure | RNA Splicing Factors - metabolism | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Spliceosomes - metabolism | RNA Splicing | Ribonucleoproteins, Small Nuclear - ultrastructure | RNA, Small Nuclear - genetics | Protein Domains | Ribonucleoprotein, U5 Small Nuclear - ultrastructure | Adenosine Triphosphatases - ultrastructure | DEAD-box RNA Helicases - metabolism | DEAD-box RNA Helicases - chemistry | Saccharomyces cerevisiae Proteins - ultrastructure | Catalytic Domain | Biocatalysis | RNA Splice Sites - genetics | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Exons - genetics | Spliceosomes - ultrastructure | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | DNA-Binding Proteins - ultrastructure | RNA-Binding Proteins - ultrastructure | RNA Splicing Factors - ultrastructure | Ribonuclease H - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Adenosine - metabolism | Protein Binding | DEAD-box RNA Helicases - ultrastructure | RNA-Binding Proteins - metabolism | Ribonucleoproteins, Small Nuclear - metabolism | Saccharomyces cerevisiae Proteins - chemistry | RNA sequencing | Methods | Mutation | Catalysis | Ribonucleic acid--RNA | Binding sites | Crystal structure
Journal Article
NATURE, ISSN 0028-0836, 06/2014, Volume 510, Issue 7504, pp. 293 - 293
Efficient duplication of the genome requires the concerted action of helicase and DNA polymerases at replication forks(1) to avoid stalling of the replication... 
SISTER-CHROMATID COHESION | MCM2-7 HELICASE | COMPLEX | ACTIVATION | REPLICATION | PROTEIN | METABOLISM | GINS | MULTIDISCIPLINARY SCIENCES | STOICHIOMETRY | PROGRESSION | Minichromosome Maintenance Proteins - metabolism | Protein Multimerization | Molecular Sequence Data | Multienzyme Complexes - metabolism | Crystallography, X-Ray | Saccharomyces cerevisiae - ultrastructure | DNA Helicases - ultrastructure | DNA-Directed DNA Polymerase - chemistry | Minichromosome Maintenance Proteins - chemistry | Protein Subunits - metabolism | DNA-Binding Proteins - metabolism | Protein Structure, Quaternary | Conserved Sequence | Saccharomyces cerevisiae Proteins - ultrastructure | Amino Acid Sequence | DNA Helicases - chemistry | Catalytic Domain | Models, Molecular | DNA Replication | Nuclear Proteins - metabolism | DNA Polymerase I - chemistry | Microscopy, Electron | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Saccharomyces cerevisiae - chemistry | Amino Acid Motifs | Multienzyme Complexes - chemistry | DNA-Binding Proteins - ultrastructure | DNA Helicases - metabolism | DNA Polymerase I - ultrastructure | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Subunits - chemistry | DNA-Directed DNA Polymerase - metabolism | DNA Polymerase I - metabolism | Saccharomyces cerevisiae Proteins - chemistry
Journal Article
Journal Article
Nature Communications, ISSN 2041-1723, 02/2016, Volume 7, Issue 1, p. 10708
Journal Article
Nature, ISSN 0028-0836, 05/2016, Volume 533, Issue 7603, pp. 359 - 365
In eukaryotic transcription initiation, a large multi-subunit pre-initiation complex (PIC) that assembles at the core promoter is required for the opening of... 
RNA-POLYMERASE-II | GENERAL TRANSCRIPTION | ABORTIVE INITIATION | CONFORMATIONAL-CHANGES | SWI2/SNF2 ATPASE | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | ELONGATION COMPLEX | MULTIDISCIPLINARY SCIENCES | BINDING DOMAIN | PREINITIATION COMPLEX | Humans | RNA Polymerase II - ultrastructure | DNA - ultrastructure | DNA Helicases - ultrastructure | RNA Polymerase II - metabolism | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Transcription Factors, TFII - ultrastructure | Multiprotein Complexes - metabolism | Transcription Initiation, Genetic | RNA Polymerase II - chemistry | DNA Helicases - chemistry | Promoter Regions, Genetic | Movement | Models, Molecular | DNA - metabolism | DNA-Binding Proteins - chemistry | Saccharomyces cerevisiae - chemistry | Transcription Elongation, Genetic | Cryoelectron Microscopy | DNA-Binding Proteins - ultrastructure | DNA Helicases - metabolism | Multiprotein Complexes - ultrastructure | Transcription Factors, TFII - chemistry | DNA - chemistry | Multiprotein Complexes - chemistry | Transcription Factors, TFII - metabolism | Protein Conformation | HeLa Cells | Genetic research | Promoters (Genetics) | Genetic transcription | Research | Cryoelectron microscopy | Methods | Studies | Eukaryotes | Yeast | Microscopy | RNA polymerase | Deoxyribonucleic acid--DNA | Crystal structure
Journal Article
Conference Proceeding
Nature, ISSN 0028-0836, 06/2017, Volume 546, Issue 7660, pp. 617 - 621
Intron removal requires assembly of the spliceosome on precursor mRNA (pre-mRNA) and extensive remodelling to form the spliceosome's catalytic centre. Here we... 
U4/U6.U5 TRI-SNRNP | COMPLEX | PROTEIN | MESSENGER-RNA | MULTIDISCIPLINARY SCIENCES | MOLECULAR ARCHITECTURE | U2 SNRNP | CRYO-EM STRUCTURE | REQUIRES ATP | RNA Helicases - metabolism | Ribonucleoprotein, U2 Small Nuclear - chemistry | Spliceosomes - chemistry | Saccharomyces cerevisiae - genetics | Ribonucleoprotein, U5 Small Nuclear - metabolism | RNA Splicing Factors - chemistry | RNA Helicases - chemistry | Ribonucleoprotein, U4-U6 Small Nuclear - metabolism | RNA Helicases - ultrastructure | RNA Splicing Factors - metabolism | Spliceosomes - metabolism | RNA Splicing | Ribonucleoprotein, U2 Small Nuclear - metabolism | Base Sequence | Protein Domains | RNA Precursors - metabolism | Ribonucleoproteins, Small Nuclear - chemistry | Protein Stability | Ribonucleoprotein, U5 Small Nuclear - chemistry | Saccharomyces cerevisiae Proteins - ultrastructure | Catalytic Domain | Biocatalysis | Introns - genetics | RNA Splice Sites - genetics | Models, Molecular | Nuclear Proteins - metabolism | RNA Precursors - genetics | Spliceosomes - ultrastructure | Nuclear Proteins - chemistry | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | RNA Precursors - ultrastructure | Models, Biological | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Ribonucleoprotein, U4-U6 Small Nuclear - chemistry | RNA, Small Nuclear - chemistry | RNA, Small Nuclear - metabolism | Ribonucleoproteins, Small Nuclear - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Yeast | Ribonucleoproteins (small nuclear) | Molecular structure | mRNA | Saccharomyces | Ribonucleoproteins (U2 small nuclear) | Electron microscopy | Ribonucleic acid--RNA | snRNA | Proteins | DNA helicase | Transmission electron microscopy | Ribonucleic acids | Catalysis | Atomic structure | Saccharomyces cerevisiae
Journal Article
Nature, ISSN 0028-0836, 04/2018, Volume 556, Issue 7701, pp. 386 - 390
In the eukaryotic nucleus, DNA is packaged in the form of nucleosomes, each of which comprises about 147 base pairs of DNA wrapped around a histone protein... 
VISUALIZATION | SYSTEM | NUCLEOSOMES | DNA | MULTIDISCIPLINARY SCIENCES | EM STRUCTURE DETERMINATION | MECHANISMS | SWITCH | PROTEINS | H2A.Z | SWR-C | Histones - chemistry | Nucleosomes - chemistry | Humans | DNA - ultrastructure | Structure-Activity Relationship | DNA Helicases - ultrastructure | Multiprotein Complexes - metabolism | Adenosine Triphosphate - metabolism | Nucleosomes - ultrastructure | Amino Acid Sequence | DNA Helicases - chemistry | Chromosomal Proteins, Non-Histone - metabolism | Histones - ultrastructure | Chromatin Assembly and Disassembly | Models, Molecular | Nucleosomes - metabolism | Chaetomium - enzymology | Fungal Proteins | DNA - metabolism | Cryoelectron Microscopy | DNA Helicases - metabolism | Multiprotein Complexes - ultrastructure | DNA - chemistry | Multiprotein Complexes - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Histones - metabolism | Chromosomal Proteins, Non-Histone - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Chromatin | Research | Gene expression | Muscle proteins | Analysis | Adenosine triphosphatase | Translocation | Histone H2A | Superhelical DNA | Base pairs | Motor activity | Macromolecules | Editing | Electron microscopy | Remodeling | Nuclei | DNA repair | Chromatin remodeling | DNA biosynthesis | Proteins | Fungi | Microscopy | Nucleosomes | ATP | Deoxyribonucleic acid--DNA
Journal Article