X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (13698) 13698
Publication (1354) 1354
Book Review (1317) 1317
Book Chapter (113) 113
Conference Proceeding (42) 42
Book / eBook (9) 9
Web Resource (4) 4
Dissertation (2) 2
Magazine Article (2) 2
Newspaper Article (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (13199) 13199
multienzyme complexes - metabolism (7808) 7808
biochemistry & molecular biology (6896) 6896
animals (5543) 5543
humans (4119) 4119
multienzyme complexes - genetics (3220) 3220
molecular sequence data (3071) 3071
multienzyme complexes - chemistry (3007) 3007
proteasome endopeptidase complex (2918) 2918
amino acid sequence (2806) 2806
cysteine endopeptidases - metabolism (2128) 2128
kinetics (2099) 2099
cell biology (1695) 1695
rats (1592) 1592
escherichia-coli (1527) 1527
enzymes (1518) 1518
multienzyme complexes (1430) 1430
mice (1384) 1384
base sequence (1336) 1336
proteins (1319) 1319
biophysics (1315) 1315
binding sites (1286) 1286
research (1246) 1246
models, molecular (1146) 1146
male (1109) 1109
mutation (1102) 1102
protein binding (1082) 1082
multienzyme complexes - antagonists & inhibitors (1066) 1066
phosphorylation (1058) 1058
cell line (1024) 1024
multienzyme complexes - isolation & purification (1016) 1016
substrate specificity (1006) 1006
expression (988) 988
protein conformation (973) 973
microbiology (948) 948
cloning, molecular (937) 937
molecular weight (899) 899
oxidation-reduction (889) 889
protein (877) 877
analysis (838) 838
sequence homology, amino acid (837) 837
physiological aspects (820) 820
escherichia coli - enzymology (817) 817
purification (811) 811
catalysis (787) 787
biosynthesis (753) 753
escherichia coli - genetics (751) 751
protein structure, tertiary (733) 733
recombinant proteins - metabolism (708) 708
saccharomyces-cerevisiae (707) 707
amp-activated protein kinases (705) 705
proteasome (700) 700
degradation (686) 686
female (675) 675
genes (674) 674
biotechnology & applied microbiology (672) 672
cattle (671) 671
enzyme activation (661) 661
biochemistry (653) 653
gene (648) 648
protein-serine-threonine kinases - metabolism (639) 639
electrophoresis, polyacrylamide gel (635) 635
crystal-structure (618) 618
cells, cultured (615) 615
identification (614) 614
models, biological (612) 612
sequence alignment (570) 570
structure-activity relationship (565) 565
nadh, nadph oxidoreductases - metabolism (564) 564
cells (563) 563
complex (558) 558
genetics & heredity (558) 558
bacterial proteins - metabolism (552) 552
transfection (546) 546
multienzyme complexes - physiology (540) 540
gene expression (539) 539
macromolecular substances (530) 530
article (529) 529
multienzyme complex (527) 527
crystallography, x-ray (523) 523
ubiquitin (510) 510
ubiquitins - metabolism (505) 505
multidisciplinary sciences (504) 504
signal transduction (495) 495
time factors (495) 495
oxidoreductases - metabolism (490) 490
metabolism (487) 487
cysteine endopeptidases - chemistry (486) 486
enzyme inhibitors - pharmacology (480) 480
bacterial proteins - genetics (478) 478
bacteria (477) 477
blotting, western (475) 475
escherichia coli (471) 471
hydrogen-ion concentration (466) 466
mutagenesis, site-directed (464) 464
saccharomyces cerevisiae - genetics (460) 460
genetic aspects (459) 459
tumor cells, cultured (457) 457
hydrolysis (453) 453
ubiquitin - metabolism (436) 436
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (13643) 13643
Japanese (26) 26
Russian (23) 23
Chinese (15) 15
French (8) 8
German (6) 6
Polish (3) 3
Ukrainian (3) 3
Arabic (1) 1
Danish (1) 1
Dutch (1) 1
Italian (1) 1
Spanish (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, 08/2015, Volume 524, Issue 7564, pp. 186 - 191
Journal Article
Nature Nanotechnology, ISSN 1748-3387, 2014, Volume 9, Issue 7, pp. 531 - 536
Swinging arms are a key functional component of multistep catalytic transformations in many naturally occurring multienzyme complexes(1). This arm is typically... 
NANOSCIENCE & NANOTECHNOLOGY | NANOSTRUCTURES | MATERIALS SCIENCE, MULTIDISCIPLINARY | DEHYDROGENASE | Nanostructures - chemistry | DNA - chemistry | Oxidoreductases - chemistry | Multienzyme Complexes - chemistry | Index Medicus | Electrodes | Enzymes | Channelling | Cellular | Deoxyribonucleic acid | Cascade control | Transformations | Nanostructure
Journal Article
2009, 1, Metal ions in life sciences, ISBN 1847559158, Volume 6., xxvii, 510
Metal Ions in Life Sciences links coordination chemistry and biochemistry in their widest sense and thus increases our understanding of the relationship... 
chemistry | Coenzymes | Multienzyme Complexes | Organometallic compounds | Vitamin B 12 | Oxidoreductases | Metalloenzymes | Vitamin B12
Book
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 09/2014, Volume 111, Issue 38, pp. E3948 - E3956
Journal Article
Nature chemical biology, ISSN 1552-4450, 2014, Volume 10, Issue 2, pp. 93 - 95
Journal Article
Journal Article
Science, ISSN 0036-8075, 11/2016, Volume 354, Issue 6314, pp. 890 - 893
Journal Article
Journal Article
Cell, ISSN 0092-8674, 08/2013, Volume 154, Issue 3, pp. 556 - 568
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 | SYSTEM | COMPLEX | REPLICATION | PROTEIN | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | S PHASE | SACCHAROMYCES-CEREVISIAE | 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 | Index Medicus
Journal Article
Journal Article
The EMBO Journal, ISSN 0261-4189, 11/2011, Volume 30, Issue 22, pp. 4652 - 4664
Journal Article