X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (6441) 6441
Publication (1113) 1113
Book Chapter (105) 105
Newsletter (76) 76
Book Review (61) 61
Conference Proceeding (14) 14
Dissertation (7) 7
Magazine Article (7) 7
Book / eBook (2) 2
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
s-adenosylmethionine (3492) 3492
index medicus (2514) 2514
biochemistry & molecular biology (2261) 2261
animals (2152) 2152
s-adenosylmethionine - metabolism (2008) 2008
humans (1775) 1775
methylation (1717) 1717
male (929) 929
enzymes (865) 865
molecular sequence data (813) 813
rats (813) 813
physiological aspects (786) 786
kinetics (749) 749
escherichia-coli (706) 706
amino acid sequence (696) 696
metabolism (693) 693
analysis (655) 655
methionine (630) 630
methyltransferases - metabolism (624) 624
research (622) 622
proteins (617) 617
biosynthesis (616) 616
dna methylation (594) 594
mice (589) 589
article (574) 574
female (571) 571
cell biology (542) 542
gene expression (540) 540
adenosyl-l-methionine (534) 534
expression (527) 527
s-adenosylmethionine - chemistry (520) 520
models, molecular (504) 504
s-adenosylmethionine decarboxylase (494) 494
homocysteine (486) 486
adenosylmethionine (460) 460
biophysics (458) 458
binding sites (452) 452
s-adenosylmethionine - pharmacology (446) 446
substrate specificity (446) 446
amino acids (443) 443
crystal-structure (442) 442
polyamines (429) 429
base sequence (413) 413
protein (391) 391
methyltransferase (382) 382
catalysis (380) 380
genes (374) 374
protein binding (374) 374
liver (367) 367
methionine - metabolism (363) 363
microbiology (357) 357
gene-expression (356) 356
methyltransferases (355) 355
mutation (349) 349
dna (336) 336
plant sciences (333) 333
gene (328) 328
oxidative stress (327) 327
life sciences (325) 325
liver - metabolism (325) 325
methyltransferases - chemistry (318) 318
s-adenosylhomocysteine - metabolism (318) 318
multidisciplinary sciences (306) 306
biochemistry (299) 299
pharmacology & pharmacy (298) 298
bacterial proteins - metabolism (296) 296
crystallography, x-ray (294) 294
genetic aspects (290) 290
identification (287) 287
rna (283) 283
research article (282) 282
s-adenosylmethionine synthetase (277) 277
cancer (275) 275
binding (271) 271
metabolites (271) 271
methyltransferases - genetics (271) 271
saccharomyces-cerevisiae (270) 270
protein conformation (266) 266
methionine adenosyltransferase - metabolism (263) 263
escherichia coli - enzymology (262) 262
biotechnology & applied microbiology (249) 249
cloning, molecular (241) 241
escherichia coli - genetics (238) 238
sequence homology, amino acid (238) 238
glutathione (236) 236
liver - enzymology (233) 233
genetics & heredity (232) 232
methionine adenosyltransferase - genetics (232) 232
time factors (232) 232
transferases (232) 232
neurosciences (225) 225
mechanism (222) 222
rat-liver (220) 220
s-adenosylhomocysteine (220) 220
bacterial proteins - genetics (213) 213
liver - drug effects (212) 212
sequence alignment (211) 211
polyamines - metabolism (208) 208
protein structure, tertiary (207) 207
recombinant proteins - metabolism (207) 207
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (6523) 6523
Russian (16) 16
Chinese (10) 10
Italian (10) 10
Japanese (6) 6
French (4) 4
German (3) 3
Korean (2) 2
Polish (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 Chemical Biology, ISSN 1552-4450, 08/2014, Volume 10, Issue 10, pp. 810 - 812
Approximately 25% of cytoplasmic tRNAs in eukaryotic organisms have the wobble uridine (U34) modified at C5 through a process that, according to genetic... 
DOMAIN | PROTEIN | POLYMERASE-II HOLOENZYME | BIOCHEMISTRY & MOLECULAR BIOLOGY | HISTONE ACETYLTRANSFERASE | SACCHAROMYCES-CEREVISIAE | ELONGATOR COMPLEX | EXPRESSION | SAM | Histone Acetyltransferases - chemistry | Archaeal Proteins - chemistry | Histone Acetyltransferases - genetics | Molecular Sequence Data | S-Adenosylmethionine - chemistry | Protein Subunits - metabolism | Nerve Tissue Proteins - chemistry | Histone Acetyltransferases - metabolism | Escherichia coli - metabolism | Conserved Sequence | Free Radicals - metabolism | Archaeal Proteins - genetics | RNA, Transfer - chemistry | Methanocaldococcus - chemistry | Uridine - chemistry | Protein Subunits - genetics | Archaeal Proteins - metabolism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Gene Expression | Biocatalysis | Free Radicals - chemistry | RNA, Transfer - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Escherichia coli - genetics | Methanocaldococcus - enzymology | Saccharomyces cerevisiae Proteins - metabolism | Uridine - metabolism | Protein Subunits - chemistry | Structural Homology, Protein | S-Adenosylmethionine - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Eukaryotes | Biocatalysts | Cytoplasm | Transfer RNA
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 03/2016, Volume 11, Issue 3, pp. e0152626 - e0152626
S-adenosylmethionine decarboxylase (PfAdoMetDC) from Plasmodium falciparum is a prospective antimalarial drug target. The production of recombinant PfAdoMetDC... 
HEAT-SHOCK-PROTEIN-70 | LIMITED PROTEOLYSIS | IN-VITRO | MOLECULAR CHAPERONE DNAK | SUBSTRATE-BINDING | MECHANISM | GENE | TRIGGER FACTOR | MULTIDISCIPLINARY SCIENCES | ORNITHINE-DECARBOXYLASE | HETEROLOGOUS EXPRESSION | HSP40 Heat-Shock Proteins - metabolism | Molecular Chaperones - metabolism | HSP40 Heat-Shock Proteins - genetics | Adenosylmethionine Decarboxylase - metabolism | Bacterial Proteins - genetics | Molecular Chaperones - genetics | Escherichia coli Proteins - metabolism | HSP70 Heat-Shock Proteins - genetics | Adenosylmethionine Decarboxylase - genetics | Recombinant Proteins - biosynthesis | HSP70 Heat-Shock Proteins - metabolism | Recombinant Proteins - isolation & purification | Plasmodium falciparum - genetics | Escherichia coli - metabolism | Escherichia coli Proteins - genetics | Protein Binding | Bacterial Proteins - metabolism | Usage | Gene mutations | Analysis | Escherichia coli | Heat shock proteins | Genetic aspects | Research | Gene expression | Recombinant proteins | S-adenosylmethionine | Adenosylmethionine | Erythrocytes | Biochemistry | Chaperones | Parasites | Hydrophobicity | Polyamines | Proteins | Adenosylmethionine decarboxylase | E coli | Protein folding | Proteolysis | Quality | Cooperation | DnaK protein | Constitution | Recombinant | Binding | Malaria | Hsp70 protein | RNA polymerase | S-Adenosylmethionine | Substrates | Heat | Mutagenesis | Antimalarial agents | Site-directed mutagenesis | Adenosine triphosphatase | Heat shock | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2015, Volume 290, Issue 1, pp. 423 - 434
Background: Many proteins are modified by lysine methylation. Results: It is shown that the previously uncharacterized enzyme METTL20 methylates electron... 
Electron Transfer Flavoprotein | METHYLATION | COA DEHYDROGENASE | Enzyme Catalysis | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | Post-translational Modification (PTM) | RAT-LIVER MITOCHONDRIA | IDENTIFICATION | Protein Methylation | SET DOMAIN | MEDIUM-CHAIN | SUBSTRATE | Protein Targeting | PURIFICATION | PROTEINS | Mitochondrial Metabolism | Electron-Transferring Flavoproteins - chemistry | Glutaryl-CoA Dehydrogenase - metabolism | Mitochondria - enzymology | Humans | Methyltransferases - metabolism | Methyltransferases - genetics | Molecular Sequence Data | Mitochondrial Proteins - genetics | Acyl-CoA Dehydrogenases - genetics | Protein Subunits - metabolism | Mitochondrial Proteins - metabolism | Escherichia coli - metabolism | HEK293 Cells | Lysine - metabolism | Mitochondria - chemistry | Glutaryl-CoA Dehydrogenase - genetics | Protein Subunits - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Electron-Transferring Flavoproteins - genetics | Methyltransferases - chemistry | Gene Expression | Protein Structure, Secondary | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Electron-Transferring Flavoproteins - metabolism | Acyl-CoA Dehydrogenases - metabolism | Sequence Alignment | Escherichia coli - genetics | Mitochondrial Proteins - chemistry | Protein Processing, Post-Translational | Protein Subunits - chemistry | HeLa Cells | Methylation | S-Adenosylmethionine - metabolism | Enzymology
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 7, pp. 2558 - 2572
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 02/2014, Volume 136, Issue 5, pp. 1754 - 1757
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2016, Volume 113, Issue 34, pp. 9446 - 9450
Lipoyl synthase (LipA) catalyzes the insertion of two sulfur atoms at the unactivated C6 and C8 positions of a protein-bound octanoyl chain to produce the... 
Lipoic acid | Radical SAM enzyme | Iron-sulfur cluster | FERREDOXIN | iron-sulfur cluster | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | LIGATION | INSIGHT | BIOTIN SYNTHASE | radical SAM enzyme | BIOSYNTHESIS | SUBSTRATE | lipoic acid | CLUSTER | ELECTRONIC-STRUCTURE | Bacterial Proteins - chemistry | Iron-Sulfur Proteins - genetics | Substrate Specificity | Crystallography, X-Ray | S-Adenosylmethionine - chemistry | Iron-Sulfur Proteins - chemistry | Peptides - metabolism | Cloning, Molecular | Escherichia coli - metabolism | Mycobacterium tuberculosis - chemistry | Protein Interaction Domains and Motifs | Sulfur - chemistry | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Sulfur - metabolism | Catalytic Domain | Gene Expression | Genetic Vectors - chemistry | Peptides - chemistry | Iron - chemistry | Bacterial Proteins - genetics | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Iron - metabolism | Amino Acid Motifs | Protein Conformation, beta-Strand | Escherichia coli - genetics | Mycobacterium tuberculosis - enzymology | Protein Binding | Bacterial Proteins - metabolism | Iron-Sulfur Proteins - metabolism | Kinetics | S-Adenosylmethionine - metabolism | Enzymes | Chemical properties | Crystallography | Methods | Biological Sciences | Physical Sciences | iron–sulfur cluster
Journal Article
FEBS Letters, ISSN 0014-5793, 09/2012, Volume 586, Issue 19, pp. 3448 - 3451
► Heterozygous EZH2 A687 V mutation is associated with lymphoma. ► A687 V EZH2 mutant shown to be active with altered substrate specificity. ► Mutation changes... 
Genetically altered enzyme | Histone Methyltransferase | Gain-of-function mutation | H3K27 | Lymphoma | EZH2 | Hypertrimethylation | CPM | DLBCL | PKMT | S-adenosylhomocysteine | diffuse large B-cell lymphoma | protein lysine methyltransferase | S-adenosylmethionine | histone H3 lysine 27 | NHL | counts per minute | SAM bearing tritiated methyl group | GCB | Polycomb Repressive Complex 2 | PRC2 | 3H-SAM | SAH | germinal Center B-cell-like | SAM | non-Hogdkin lymphoma | METHYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | B-CELL LYMPHOMAS | HISTONE-MODIFYING GENES | CANCER | SOMATIC MUTATIONS | CELL BIOLOGY | LYSINE 27 | BIOPHYSICS | GROUP PROTEIN EZH2 | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Polycomb Repressive Complex 2 - genetics | Histones - chemistry | Humans | Mutant Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Neoplasm Proteins - chemistry | Lymphoma, Non-Hodgkin - enzymology | Recombinant Proteins - genetics | Lymphoma, Non-Hodgkin - genetics | Neoplasm Proteins - metabolism | Polycomb Repressive Complex 2 - chemistry | Enhancer of Zeste Homolog 2 Protein | Point Mutation | Mutant Proteins - chemistry | Heterozygote | Histones - metabolism | Kinetics | Methylation | Neoplasm Proteins - genetics | Polycomb Repressive Complex 2 - metabolism | Methyltransferases | Lysine | Histones | Professional hockey | Lymphomas | Genetic aspects
Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 6/2016, Volume 85, pp. 485 - 514
Radical S -adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Of... 
tRNA modifications | radicals | Elongator | iron-sulfur cluster | adenosylmethionine | viperin | lipoic acid | molybdenum cofactor | Lipoic acid | Molybdenum cofactor | Viperin | TRNA modifications | Iron-sulfur cluster | S-adenosylmethionine | Radicals | IRON-SULFUR PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIAL TRANSFER-RNAS | ANTIVIRAL PROTEIN VIPERIN | AMYOTROPHIC-LATERAL-SCLEROSIS | ADENOSYL-L-METHIONINE | LIPOIC ACID BIOSYNTHESIS | HEPATITIS-C VIRUS | PHENYLALANINE TRANSFER-RNA | MOLYBDENUM COFACTOR DEFICIENCY | GENOME-WIDE ASSOCIATION | Diabetes Mellitus, Type 2 - genetics | Humans | Histone Acetyltransferases - genetics | Iron-Sulfur Proteins - genetics | Intracellular Signaling Peptides and Proteins - metabolism | Thioctic Acid - metabolism | Heart Defects, Congenital - genetics | tRNA Methyltransferases - genetics | Heart Defects, Congenital - enzymology | Histone Acetyltransferases - metabolism | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | tRNA Methyltransferases - metabolism | Gene Expression | Metal Metabolism, Inborn Errors - genetics | Neurodegenerative Diseases - pathology | Oxidoreductases - metabolism | Oxidoreductases - genetics | Diabetes Mellitus, Type 2 - enzymology | Heart Defects, Congenital - pathology | Metal Metabolism, Inborn Errors - pathology | Neurodegenerative Diseases - genetics | Nuclear Proteins - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Proteins - genetics | Proteins - metabolism | Metal Metabolism, Inborn Errors - enzymology | Iron-Sulfur Proteins - metabolism | Diabetes Mellitus, Type 2 - pathology | Mutation | S-Adenosylmethionine - metabolism | Neurodegenerative Diseases - enzymology | Health aspects | Methionine
Journal Article