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histone-lysine n-methyltransferase - metabolism (2512) 2512
humans (2496) 2496
animals (2049) 2049
methylation (1972) 1972
histones - metabolism (1670) 1670
histone-lysine n-methyltransferase - genetics (1662) 1662
biochemistry & molecular biology (1246) 1246
mice (1187) 1187
cell biology (1135) 1135
chromatin (1067) 1067
histone-lysine n-methyltransferase (820) 820
dna methylation (788) 788
gene expression (775) 775
proteins (682) 682
research (667) 667
histones (653) 653
female (649) 649
male (631) 631
epigenetics (583) 583
lysine - metabolism (569) 569
genetic aspects (554) 554
expression (549) 549
genetics & heredity (545) 545
cell line, tumor (532) 532
cancer (524) 524
transcription (522) 522
dna-binding proteins - metabolism (519) 519
methyltransferases (518) 518
protein binding (505) 505
gene-expression (494) 494
oncology (479) 479
dna-binding proteins - genetics (475) 475
transcription factors - metabolism (475) 475
epigenesis, genetic (471) 471
genes (470) 470
lysine (459) 459
mutation (442) 442
histones - genetics (435) 435
molecular sequence data (416) 416
chromatin - metabolism (415) 415
histone methyltransferase (408) 408
nuclear proteins - metabolism (408) 408
amino acid sequence (401) 401
myeloid-lymphoid leukemia protein - genetics (400) 400
physiological aspects (399) 399
transcription, genetic (397) 397
methyltransferase (396) 396
multidisciplinary sciences (390) 390
cell line (379) 379
gene (377) 377
histone h3 (375) 375
histone-lysine n-methyltransferase - chemistry (371) 371
myeloid-lymphoid leukemia protein - metabolism (371) 371
transcription factors - genetics (371) 371
protein (360) 360
gene expression regulation (349) 349
repressor proteins - metabolism (349) 349
nuclear proteins - genetics (343) 343
gene silencing (341) 341
analysis (335) 335
protein methyltransferases (335) 335
leukemia (318) 318
dna (315) 315
histone methylation (307) 307
transcription factors (307) 307
promoter regions, genetic (306) 306
histone-lysine n-methyltransferase - antagonists & inhibitors (305) 305
research article (303) 303
acetylation (297) 297
genetics (295) 295
developmental biology (292) 292
histones - chemistry (292) 292
biology (289) 289
molecular biology (289) 289
gene expression regulation, neoplastic (282) 282
cells, cultured (276) 276
complex (270) 270
epigenetic inheritance (268) 268
protein structure, tertiary (262) 262
hematology (261) 261
cell proliferation (254) 254
mice, inbred c57bl (252) 252
repressor proteins - genetics (252) 252
protein processing, post-translational (238) 238
phosphorylation (237) 237
signal transduction (235) 235
binding sites (234) 234
hela cells (233) 233
histone methyltransferases (231) 231
methyltransferases - metabolism (230) 230
cells (228) 228
apoptosis (226) 226
genomics (226) 226
rna interference (226) 226
stem cells (226) 226
heterochromatin (224) 224
binding (216) 216
saccharomyces-cerevisiae (216) 216
differentiation (212) 212
hek293 cells (212) 212
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Journal Article
Journal Article
Nature (London), ISSN 1476-4687, 2010, Volume 464, Issue 7290, pp. 927 - 931
Journal Article
Molecular Oncology, ISSN 1574-7891, 12/2016, Volume 10, Issue 10, pp. 1497 - 1515
Histone methyltransferases (HMTs) catalyze the methylation of lysine and arginine residues on histone tails and non-histone targets. These important... 
Histone methyltransferase | Chromatin | Breast cancer | Inhibitors | Transcription | SELECTIVE-INHIBITION | DNA METHYLATION | TUMOR-SUPPRESSOR GENE | TRANSCRIPTIONAL REPRESSION | CELL-PROLIFERATION | MESENCHYMAL TRANSITION | POTENT ANTITUMOR-ACTIVITY | LYSINE METHYLTRANSFERASE | ONCOLOGY | POOR-PROGNOSIS | PROTEIN ARGININE METHYLTRANSFERASES | Humans | Transcriptional Activation - drug effects | Protein-Arginine N-Methyltransferases - antagonists & inhibitors | Antineoplastic Agents - therapeutic use | Histone-Lysine N-Methyltransferase - analysis | Molecular Targeted Therapy | Breast Neoplasms - metabolism | Histone-Lysine N-Methyltransferase - antagonists & inhibitors | Histone Code - drug effects | Female | Antineoplastic Agents - pharmacology | Epigenesis, Genetic - drug effects | Protein-Arginine N-Methyltransferases - genetics | Gene Expression Regulation, Neoplastic - drug effects | Breast - pathology | Histone-Lysine N-Methyltransferase - genetics | Protein-Arginine N-Methyltransferases - analysis | Enzyme Inhibitors - pharmacology | Breast Neoplasms - drug therapy | Drug Discovery | Enzyme Inhibitors - therapeutic use | Protein-Arginine N-Methyltransferases - metabolism | Animals | Breast Neoplasms - genetics | Histone-Lysine N-Methyltransferase - metabolism | Breast - drug effects | Breast Neoplasms - pathology | Care and treatment | Methyltransferases | Lysine | Stem cells | Genetic transcription | Methylation | Cancer | CRISPR | Medical research | Genomes | Gene expression | Arginine | DNA methylation | Tumorigenesis | Binding sites | Deoxyribonucleic acid--DNA | Tumors | Review
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2013, Volume 110, Issue 42, pp. 16778 - 16783
Protein methyltransferase (PMT)-mediated posttranslational modification of histone and nonhistone substrates modulates stability, localization, and interacting... 
Proteins | Enzymes | DNA | Proteomics | Reagents | Histones | Biochemistry | Predetermined motion time systems | Methylation | Chemicals | Bump-hole | Posttranslation | Epigenetic | AZIDES | proteomics | SPECIFICITY | epigenetic | MULTIDISCIPLINARY SCIENCES | GLP | ALKYNES | HISTONES | G9A | ADENOSYL-L-METHIONINE | LYSINE METHYLTRANSFERASE | BIOLOGY | bump-hole | posttranslation | BINDING | Histocompatibility Antigens - genetics | Neoplasms - metabolism | Humans | Histocompatibility Antigens - chemistry | Substrate Specificity | Intracellular Signaling Peptides and Proteins - metabolism | S-Adenosylmethionine - chemistry | Neoplasm Proteins - metabolism | Neoplasms - chemistry | Neoplasms - genetics | HEK293 Cells | Protein-Arginine N-Methyltransferases - genetics | S-Adenosylmethionine - genetics | Histocompatibility Antigens - metabolism | Neoplasm Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Protein-Arginine N-Methyltransferases - chemistry | Histone-Lysine N-Methyltransferase - genetics | Neoplasm Proteins - chemistry | Protein-Arginine N-Methyltransferases - metabolism | Histone-Lysine N-Methyltransferase - chemistry | Histone-Lysine N-Methyltransferase - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Hydrophobic and Hydrophilic Interactions | S-Adenosylmethionine - metabolism | Post-translational modification | Physiological aspects | Protein biosynthesis | Research | Biological Sciences | Physical Sciences
Journal Article