X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (50022) 50022
Newsletter (718) 718
Book Chapter (202) 202
Publication (39) 39
Dissertation (24) 24
Book / eBook (22) 22
Conference Proceeding (22) 22
Government Document (18) 18
Magazine Article (7) 7
Web Resource (7) 7
Reference (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
animals (23124) 23124
biochemistry & molecular biology (21758) 21758
humans (18665) 18665
cysteine (16721) 16721
index medicus (15642) 15642
amino acid sequence (9220) 9220
molecular sequence data (8620) 8620
mice (6592) 6592
proteins (6213) 6213
rats (6070) 6070
cysteine - metabolism (5643) 5643
kinetics (5609) 5609
cysteine - chemistry (5513) 5513
male (5454) 5454
cysteine endopeptidases - metabolism (5123) 5123
analysis (4913) 4913
cell biology (4751) 4751
expression (4638) 4638
oxidative stress (4524) 4524
biophysics (4312) 4312
research (4248) 4248
binding sites (4155) 4155
apoptosis (4036) 4036
female (3991) 3991
protein binding (3849) 3849
oxidation-reduction (3827) 3827
models, molecular (3708) 3708
cystine (3584) 3584
physiological aspects (3568) 3568
cell line (3528) 3528
cysteine proteinase inhibitors - pharmacology (3505) 3505
protein conformation (3440) 3440
mutation (3422) 3422
mutagenesis, site-directed (3233) 3233
enzymes (3128) 3128
cells, cultured (3104) 3104
base sequence (2973) 2973
protein (2956) 2956
glutathione (2937) 2937
identification (2863) 2863
thiols (2823) 2823
proteasome endopeptidase complex (2804) 2804
activation (2801) 2801
neurosciences (2662) 2662
protein structure, tertiary (2601) 2601
cysteine - genetics (2463) 2463
escherichia-coli (2424) 2424
hydrogen-ion concentration (2360) 2360
gene expression (2325) 2325
proteases (2293) 2293
cells (2286) 2286
recombinant proteins - metabolism (2276) 2276
sequence homology, amino acid (2179) 2179
time factors (2113) 2113
signal transduction (2099) 2099
physiology (2066) 2066
crystal-structure (2054) 2054
research article (2043) 2043
substrate specificity (2037) 2037
multienzyme complexes - metabolism (1980) 1980
structure-activity relationship (1955) 1955
cloning, molecular (1941) 1941
glutathione - metabolism (1934) 1934
gene (1898) 1898
amino acids (1884) 1884
binding (1860) 1860
recombinant proteins - chemistry (1854) 1854
phosphorylation (1852) 1852
transfection (1837) 1837
apoptosis - drug effects (1822) 1822
purification (1814) 1814
life sciences (1788) 1788
cysteine endopeptidases - genetics (1779) 1779
inhibition (1772) 1772
endocrinology & metabolism (1754) 1754
biochemistry (1751) 1751
peptides (1747) 1747
cysteine - analogs & derivatives (1735) 1735
dose-response relationship, drug (1732) 1732
cysteine - pharmacology (1730) 1730
electrophoresis, polyacrylamide gel (1729) 1729
antioxidants (1704) 1704
catalysis (1687) 1687
cattle (1675) 1675
biochemical research methods (1660) 1660
blotting, western (1615) 1615
pharmacology & pharmacy (1588) 1588
mass spectrometry (1580) 1580
mechanism (1568) 1568
enzyme activation (1567) 1567
genes (1537) 1537
molecular weight (1533) 1533
metabolism (1501) 1501
immunology (1485) 1485
apoptosis - physiology (1481) 1481
microbiology (1464) 1464
protein structure, secondary (1462) 1462
plant sciences (1461) 1461
multidisciplinary sciences (1447) 1447
in-vitro (1426) 1426
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (50739) 50739
Japanese (612) 612
German (103) 103
French (48) 48
Russian (46) 46
Chinese (44) 44
Polish (31) 31
Spanish (12) 12
Dutch (7) 7
Italian (7) 7
Ukrainian (7) 7
Czech (5) 5
Portuguese (5) 5
Romanian (4) 4
Korean (2) 2
Arabic (1) 1
Swedish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Journal Article
The FEBS journal, ISSN 1742-464X, 2011, Volume 278, Issue 24, pp. 4704 - 4716
Tissue transglutaminase (TG2) is a ubiquitously expressed member of the transglutaminase family of Ca2+‐dependent crosslinking enzymes. Unlike other family... 
endosomal recycling | protein–phospholipid interaction | transglutaminase | signaling | cell–ECM interactions | endocytosis | syndecan | integrin | membrane trafficking | non‐classical protein secretion | cell-ECM interactions | protein-phospholipid interaction | non-classical protein secretion | MATRIX | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CROSS-LINKING | CELL-ADHESION | 3T3 FIBROBLASTS | S-NITROSYLATION | SURFACE TISSUE TRANSGLUTAMINASE | FIBRONECTIN | HEPARAN-SULFATE PROTEOGLYCANS | Low Density Lipoprotein Receptor-Related Protein-6 - physiology | Macrophages - physiology | Low Density Lipoprotein Receptor-Related Protein-5 - physiology | GTP-Binding Proteins - physiology | Humans | Protein Conformation - drug effects | Extracellular Matrix - metabolism | Protein Transport - physiology | Integrins - metabolism | Fibronectins - metabolism | Syndecan-4 - physiology | Cross-Linking Reagents - metabolism | Receptors, Growth Factor - physiology | GTP-Binding Proteins - secretion | Cell Adhesion - physiology | Transglutaminases - secretion | Transglutaminases - physiology | Signal Transduction - physiology | Cysteine - metabolism | beta Catenin - physiology | Enzyme Activation | Matrix Metalloproteinases, Membrane-Associated - metabolism | Mesenchymal Stem Cell Transplantation | Enzymes | Crosslinked polymers | Integrins
Journal Article
The Journal of experimental medicine, ISSN 1540-9538, 2011, Volume 208, Issue 3, pp. 593 - 604
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 31, pp. 12744 - 12753
Fe-S cofactors are composed of iron and inorganic sulfur in various stoichiometries. A complex assembly pathway conducts their initial synthesis and subsequent... 
HSPA9 | iron-response element (IRE) | mitochondrial respiratory chain complex | RESPIRATORY-CHAIN | ELEMENT-BINDING-PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | FE-S CLUSTERS | ESCHERICHIA-COLI | HSC20 | metalloenzyme | HEAVY-SUBUNIT | RESPONSIVE ELEMENT | CYSTEINE DESULFURASE | MESSENGER-RNA | iron-sulfur protein | iron-sulfur cluster biogenesis | SCAFFOLD PROTEIN | TARGETED DELETION | energy metabolism | ISCU | Iron Regulatory Protein 1 - physiology | Electron Transport | Humans | Protein Multimerization | Homeostasis | Succinate Dehydrogenase - biosynthesis | Iron-Binding Proteins - chemistry | Iron-Regulatory Proteins - biosynthesis | Succinate Dehydrogenase - chemistry | Iron-Sulfur Proteins - chemistry | Molecular Chaperones - chemistry | Apoenzymes - metabolism | Iron-Regulatory Proteins - physiology | Iron-Regulatory Proteins - chemistry | Iron-Sulfur Proteins - biosynthesis | Carbon-Sulfur Lyases - physiology | HSP70 Heat-Shock Proteins - chemistry | Protein Interaction Domains and Motifs | HSP70 Heat-Shock Proteins - biosynthesis | Molecular Chaperones - biosynthesis | Iron-Binding Proteins - physiology | Response Elements | Iron Regulatory Protein 1 - chemistry | Carbon-Sulfur Lyases - biosynthesis | Mitochondrial Proteins - physiology | Models, Molecular | Mitochondrial Proteins - biosynthesis | Molecular Chaperones - physiology | Iron-Binding Proteins - biosynthesis | Protein Folding | Iron-Sulfur Proteins - physiology | Gene Expression Regulation, Enzymologic | Animals | Iron - physiology | Mitochondrial Proteins - chemistry | Apoenzymes - chemistry | HSP70 Heat-Shock Proteins - physiology | Succinate Dehydrogenase - physiology | Carbon-Sulfur Lyases - chemistry | Iron Regulatory Protein 1 - biosynthesis | Minireviews
Journal Article
FEMS Microbiology Letters, ISSN 0378-1097, 03/2006, Volume 256, Issue 1, pp. 1 - 15
Abstract In the course of evolution, Gram-positive bacteria, defined here as prokaryotes from the domain Bacteria with a cell envelope composed of one... 
bacterial protein secretion | bacterial surface organelle | cell surface display | S‐layer protein | cell wall anchoring | membrane protein | Gram‐positive bacteria | Membrane protein | Bacterial protein secretion | Bacterial surface organelle | Cell wall anchoring | S-layer protein | Gram-positive bacteria | Cell surface display | LISTERIA-MONOCYTOGENES | EVOLUTIONARY RELATIONSHIPS | MICROBIOLOGY | STREPTOCOCCUS-PNEUMONIAE | BACILLUS-SUBTILIS | WALL POLYMER | STAPHYLOCOCCUS-AUREUS | MOLECULAR-CLONING | MEMBRANE-PROTEINS | LAYER HOMOLOGY DOMAINS | CLOSTRIDIUM-CELLULOLYTICUM | Choline - metabolism | Flagella - physiology | Gram-Positive Bacteria - physiology | Gram-Positive Bacteria - chemistry | Membrane Glycoproteins - chemistry | Bacterial Proteins - chemistry | Molecular Sequence Data | Cell Membrane - physiology | Cysteine Endopeptidases - physiology | Membrane Glycoproteins - physiology | Membrane Proteins - physiology | Flagella - chemistry | Protein Structure, Quaternary - physiology | Amino Acid Sequence | Fimbriae, Bacterial - chemistry | Lipoproteins - chemistry | Cell Wall - chemistry | Cellulosomes - physiology | Bacterial Proteins - physiology | Cellulosomes - chemistry | Lipoproteins - physiology | Membrane Proteins - chemistry | Mucoproteins - chemistry | Fimbriae, Bacterial - physiology | Cell Wall - metabolism | Aminoacyltransferases - physiology | Gram-Positive Bacteria - ultrastructure | Mucoproteins - metabolism | Protein Binding - physiology | Proteins | Cell walls | Prokaryotes | Macromolecules | Peptidoglycans | Cell surface | Teichoic acids | Membrane proteins | Lipoproteins | Molecular modelling | Bacteria | Protein structure | Life Sciences | Microbiology and Parasitology
Journal Article
Genes & development, ISSN 0890-9369, 1998, Volume 12, Issue 6, pp. 806 - 819
Caspases are fundamental components of the mammalian apoptotic machinery, but the precise contribution of individual caspases is controversial. CPP32 (caspase... 
MEFs | CYSTEINE PROTEASE | ACTIVATION | cell death | apoptosis | DEVELOPMENTAL BIOLOGY | CLEAVAGE | caspase | P53 | CELL BIOLOGY | PROGRAMMED CELL-DEATH | ICE/CED-3 PROTEASE | CAENORHABDITIS-ELEGANS | GENE | CPP32 | GENETICS & HEREDITY | CED-3 | GRANZYME-B | Enzymes | Chemotherapy | Cell death | Structure-activity relationship | Analysis | Causes of | Aging | Genetic aspects | Fibroblast growth factors | Cell nuclei | Cells | Immunological research
Journal Article
The Journal of neuroscience, ISSN 1529-2401, 2010, Volume 30, Issue 7, pp. 2547 - 2558
Journal Article
Journal of Neuroscience, ISSN 0270-6474, 12/2004, Volume 24, Issue 48, pp. 10963 - 10973