X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (36859) 36859
Newsletter (1767) 1767
Book Chapter (237) 237
Dissertation (62) 62
Publication (41) 41
Book / eBook (25) 25
Newspaper Article (17) 17
Magazine Article (10) 10
Conference Proceeding (8) 8
Reference (4) 4
Transcript (4) 4
Book Review (3) 3
Government Document (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
heme (15765) 15765
biochemistry & molecular biology (14202) 14202
animals (12838) 12838
humans (8669) 8669
heme - metabolism (5480) 5480
heme - chemistry (4984) 4984
oxidative stress (4649) 4649
oxidation-reduction (4550) 4550
kinetics (4296) 4296
proteins (4285) 4285
research (4229) 4229
analysis (4049) 4049
biophysics (3836) 3836
heme oxygenase-1 (3748) 3748
male (3549) 3549
mice (3523) 3523
models, molecular (3497) 3497
rats (3486) 3486
enzymes (3320) 3320
protein binding (3107) 3107
iron (2962) 2962
binding sites (2958) 2958
protein conformation (2954) 2954
cell biology (2814) 2814
hemoglobin (2706) 2706
expression (2659) 2659
amino acid sequence (2587) 2587
molecular sequence data (2510) 2510
myoglobin (2489) 2489
chemistry, multidisciplinary (2367) 2367
ligands (2312) 2312
physiological aspects (2282) 2282
heme oxygenase (2178) 2178
biochemistry (2115) 2115
nitric oxide (2103) 2103
heme oxygenase-1 - metabolism (2054) 2054
crystal-structure (1995) 1995
protein (1977) 1977
binding (1973) 1973
escherichia-coli (1917) 1917
hydrogen-ion concentration (1912) 1912
catalysis (1905) 1905
chemistry (1872) 1872
activation (1858) 1858
spectrophotometry (1850) 1850
female (1723) 1723
nitric-oxide (1715) 1715
oxidation (1694) 1694
iron - metabolism (1692) 1692
carbon-monoxide (1685) 1685
antioxidants (1672) 1672
mechanism (1640) 1640
chemistry, inorganic & nuclear (1623) 1623
apoptosis (1602) 1602
cytochrome c (1596) 1596
gene expression (1583) 1583
heme-proteins (1561) 1561
pharmacology & pharmacy (1558) 1558
inflammation (1551) 1551
chemical properties (1513) 1513
research article (1473) 1473
carbon monoxide (1456) 1456
mutation (1439) 1439
peroxidase (1422) 1422
electron transport (1405) 1405
microbiology (1399) 1399
crystallography, x-ray (1395) 1395
electron spin resonance spectroscopy (1393) 1393
chemistry, physical (1379) 1379
nf-e2-related factor 2 - metabolism (1343) 1343
heme oxygenase-1 - genetics (1335) 1335
multidisciplinary sciences (1325) 1325
oxygen (1301) 1301
cell line (1271) 1271
cells, cultured (1271) 1271
life sciences (1264) 1264
heme oxygenase - metabolism (1252) 1252
hydrogen-peroxide (1234) 1234
cells (1207) 1207
metabolism (1207) 1207
induction (1204) 1204
endocrinology & metabolism (1200) 1200
identification (1194) 1194
cattle (1192) 1192
bacterial proteins - metabolism (1190) 1190
gene-expression (1189) 1189
thermodynamics (1182) 1182
oxygen - metabolism (1179) 1179
molecular structure (1172) 1172
bacterial proteins - chemistry (1165) 1165
oxidative stress - drug effects (1154) 1154
porphyrins (1144) 1144
nrf2 (1143) 1143
signal transduction (1139) 1139
reactive oxygen species - metabolism (1111) 1111
nitric oxide - metabolism (1096) 1096
spectroscopy (1092) 1092
protein structure, tertiary (1057) 1057
inhibition (1053) 1053
iron - chemistry (1049) 1049
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (38799) 38799
Japanese (342) 342
Chinese (85) 85
German (71) 71
Russian (56) 56
French (40) 40
Korean (10) 10
Portuguese (7) 7
Polish (5) 5
Spanish (5) 5
Dutch (4) 4
Swedish (4) 4
Czech (2) 2
Italian (2) 2
Finnish (1) 1
Greek (1) 1
Latin (1) 1
Norwegian (1) 1
Ukrainian (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Angewandte Chemie (International ed.), ISSN 1433-7851, 2018, Volume 57, Issue 16, pp. 4143 - 4148
Journal Article
FEBS Letters, ISSN 0014-5793, 2013, Volume 587, Issue 14, pp. 2214 - 2218
•Cytochrome bd from E. coli displays a notable catalase activity.•Thermal denaturation or complete reduction of cytochrome bd abolishes this activity.•Activity... 
Oxidative stress | Reactive oxygen species | Respiratory chain | Hemeprotein | Bacteria–host interaction | Microbial metabolism | N-ethylmaleimide | dithiothreitol | DTT | NEM | ROS | reactive oxygen species | 2,3-dimethoxy-5-methyl-6-(3-methyl-2-butenyl)-1,4-benzoquinone | Bacteria-host interaction | AEROBIC RESPIRATORY-CHAIN | OXYGEN-REDUCING SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DI-HEME | HIGH-AFFINITY | TERMINAL OXIDASE | CELL BIOLOGY | BIOPHYSICS | QUINOL OXIDASE | CARBON-MONOXIDE | NITRIC-OXIDE | HYDROGEN-PEROXIDE | C-OXIDASE | Oxidoreductases - antagonists & inhibitors | Cytochromes - chemistry | Oxidative Stress | Hydroquinones - chemistry | Sodium Cyanide - chemistry | Oxidoreductases - chemistry | Hydrogen Peroxide - chemistry | NAD - chemistry | Cattle | Enzyme Inhibitors - chemistry | Oxygen - chemistry | Electron Transport Chain Complex Proteins - antagonists & inhibitors | Dithiothreitol - chemistry | Escherichia coli Proteins - antagonists & inhibitors | Reducing Agents - chemistry | NAD(P)H Dehydrogenase (Quinone) - chemistry | Cytochromes - antagonists & inhibitors | Escherichia coli - enzymology | Oxidants - chemistry | Rats | Electron Transport Chain Complex Proteins - chemistry | Animals | Kinetics | Escherichia coli Proteins - chemistry | Catalase - chemistry | Proteins | Oxidases | Denaturation | Nitric oxide | Escherichia coli | Oxygen | Enzyme Inhibitors | Hydrogen Peroxide | Biochemistry, Molecular Biology | Sodium Cyanide | Reducing Agents | NAD(P)H Dehydrogenase (Quinone) | NAD | Life Sciences | Hydroquinones | Escherichia coli Proteins | Catalase | Oxidants | Cytochromes | Oxidoreductases | Dithiothreitol | Electron Transport Chain Complex Proteins
Journal Article
Inorganic Chemistry, ISSN 0020-1669, 07/2010, Volume 49, Issue 14, pp. 6267 - 6282
The focus of this Forum Article highlights work from our own laboratories and those of others in the area of biochemical and biologically inspired inorganic chemistry dealing with nitric oxide [nitrogen monoxide, •NO(g... 
Forum | Copper - chemistry | Heme - chemistry | Nitric Oxide - chemistry | Oxidation-Reduction | Oxygenases - metabolism | Models, Molecular | Oxygenases - chemistry | Peroxynitrous Acid - chemistry | Nitric oxide | Analysis | Heme | Organometallic compounds | Oxidation-reduction reaction | Chemical properties | Copper | Structure
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2018, Volume 293, Issue 43, pp. 16778 - 16790
Cytochromes c are ubiquitous proteins, essential for life in most organisms. Their distinctive characteristic is the covalent attachment of heme to their... 
post-translational modification (PTM) | CHAPERONE CCME | cytochrome c maturation | BACTERIA | APOCYTOCHROME-C | heme | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | CcmE | ESCHERICHIA-COLI | TRAFFICKING | CcmC | protein-protein interactions | BIOGENESIS SYSTEM | PATHWAY | nuclear magnetic resonance (NMR) | Gram-negative bacteria | System I | cytochrome c | BINDING SITE | LIGATION COMPLEX | Apoproteins - chemistry | Hemeproteins - genetics | Heme - metabolism | Crystallography, X-Ray | Cytochromes c - genetics | Cytochromes c - chemistry | Heme - chemistry | Heme - genetics | Hemeproteins - chemistry | Escherichia coli - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Escherichia coli - growth & development | Binding Sites | Apoproteins - metabolism | Bacterial Outer Membrane Proteins - genetics | Mutagenesis, Site-Directed | Hemeproteins - metabolism | Membrane Proteins - genetics | Cytochromes c - metabolism | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Escherichia coli - genetics | Apoproteins - genetics | Escherichia coli Proteins - genetics | Protein Conformation | Escherichia coli Proteins - chemistry | Amino Acid Substitution | Index Medicus | Bioenergetics
Journal Article
Accounts of Chemical Research, ISSN 0001-4842, 08/2018, Volume 51, Issue 8, pp. 1850 - 1857
Journal Article
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2017, Volume 292, Issue 31, pp. 12764 - 12771
Eukaryotic cells contain hundreds of metalloproteins that are supported by intracellular systems coordinating the uptake and distribution of metal cofactors.... 
metalloprotein | HUMAN BOLA2 | HEME-BIOSYNTHESIS | DEOXYHYPUSINE HYDROXYLASE | BolA2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | glutaredoxin | SACCHAROMYCES-CEREVISIAE | iron metabolism | molecular chaperone | PHP4 FUNCTION | FERRITIN DEGRADATION | poly C-binding protein | IN-VIVO | GENE-EXPRESSION | iron | iron-sulfur protein | SULFUR CLUSTER | MONOTHIOL GLUTAREDOXIN | Molecular Chaperones - metabolism | Humans | Protein Multimerization | Iron-Sulfur Proteins - chemistry | Molecular Chaperones - chemistry | Nuclear Receptor Coactivators - chemistry | Autophagy | Apoferritins - metabolism | Ferritins - metabolism | Cation Transport Proteins - metabolism | Apoenzymes - metabolism | Carrier Proteins - chemistry | Dimerization | Nuclear Receptor Coactivators - metabolism | Erythroid Precursor Cells - cytology | RNA-Binding Proteins - chemistry | Heterogeneous-Nuclear Ribonucleoproteins - metabolism | Models, Molecular | Apoferritins - chemistry | Iron - metabolism | Protein Transport | Animals | Carrier Proteins - metabolism | Proteins - metabolism | Models, Biological | Heterogeneous-Nuclear Ribonucleoproteins - chemistry | Apoenzymes - chemistry | Erythroid Precursor Cells - metabolism | Cytosol - metabolism | Iron-Sulfur Proteins - metabolism | Proteins - chemistry | Cation Transport Proteins - chemistry | Ferritins - chemistry | RNA-Binding Proteins - metabolism | iron–sulfur protein | Minireviews
Journal Article