Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors - Wikidata - awgldk - TriplyDB

Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors

Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors

http://www.wikidata.org/entity/Q33530669

about

Structural genomics of histone tail recognition Current status and future prospects for epigenetic psychopharmacology Flavin-dependent enzymes in cancer prevention KDM1 class flavin-dependent protein lysine demethylases LSD1 inhibition: a therapeutic strategy in cancer?LSD1 Histone Demethylase Assays and Inhibition Impairment of prostate cancer cell growth by a selective and reversible lysine-specific demethylase 1 inhibitor.Activation of HIV transcription by the viral Tat protein requires a demethylation step mediated by lysine-specific demethylase 1 (LSD1/KDM1).Chemical and biochemical approaches in the study of histone methylation and demethylation Methods for Activity Analysis of the Proteins that Regulate Histone Methylation Targeting histone lysine demethylases - progress, challenges, and the future Structural insights into histone lysine demethylation.Mutations in epigenetic modifiers in the pathogenesis and therapy of acute myeloid leukemia.Lysine-specific demethylase 1-selective inactivators: protein-targeted drug delivery mechanism.Balancing histone methylation activities in psychiatric disorders.Inhibition of LSD1 sensitizes glioblastoma cells to histone deacetylase inhibitors Histones: at the crossroads of peptide and protein chemistry.MassSQUIRM: An assay for quantitative measurement of lysine demethylase activity Targeting protein lysine methylation and demethylation in cancers.Extranucleosomal DNA enhances the activity of the LSD1/CoREST histone demethylase complex.Brain-penetrant LSD1 inhibitors can block memory consolidation.Is targeted therapy feasible in acute myelogenous leukemia?Inhibition of the LSD1 (KDM1A) demethylase reactivates the all-trans-retinoic acid differentiation pathway in acute myeloid leukemia.Facile synthesis and altered ionization efficiency of diverse Nε-alkyllysine-containing peptides Lysine-specific histone demethylase 1 inhibitors control breast cancer proliferation in ERα-dependent and -independent manners.3-(Piperidin-4-ylmethoxy)pyridine Containing Compounds Are Potent Inhibitors of Lysine Specific Demethylase 1.Inhibition of Lysine-Specific Demethylase-1 (LSD1/KDM1A) Promotes the Adipogenic Differentiation of hESCs Through H3K4 Methylation.Epigenetics, nervous system tumors, and cancer stem cells.Chromatin-modifying agents for epigenetic reprogramming and endogenous neural stem cell-mediated repair in stroke.Triazole-dithiocarbamate based selective lysine specific demethylase 1 (LSD1) inactivators inhibit gastric cancer cell growth, invasion, and migration.Epigenetic therapy in urologic cancers: an update on clinical trials.Chemical biology of lysine demethylases.Tipping the lysine methylation balance in disease The promise and failures of epigenetic therapies for cancer treatment Small molecule epigenetic inhibitors targeted to histone lysine methyltransferases and demethylases.Epigenetic molecular recognition: a biomolecular modeling perspective.Epigenetic pathway targets for the treatment of disease: accelerating progress in the development of pharmacological tools: IUPHAR Review 11.Targeting Histone Demethylases: A New Avenue for the Fight against Cancer.KDM1 histone lysine demethylases as targets for treatments of oncological and neurodegenerative disease.Inhibitors of Protein Methyltransferases and Demethylases.

P2860

Q24634351-2D87391E-700D-4B77-A627-06F4BE6BA94B Q26825464-F5DB38BD-0FF3-4416-8FCE-B26F6AE60171 Q27023514-81BE13EE-860E-46B8-9278-0EB6E0A897B4 Q28084876-04EE5003-B858-4F28-95D0-EF4A80AEAC53 Q28274561-B63B4A39-6794-4C77-A4B7-07E9FE690D8B Q28818766-8B1E5853-78A6-4E11-BB23-D6F8C5C8A7F4 Q30414643-87BA7265-84F6-4467-A58A-FFFF0B2B36AC Q34005293-6787E53E-925F-4C70-AAB4-1BD2081D346E Q34030702-17695406-E577-47CD-8DB0-61F472CAC9F9 Q34037729-27650F96-493E-486E-8AA3-4E54D9B070C3 Q34421279-957630BD-61A7-414E-99FB-F5FE047F73CE Q34441278-2BFE1230-FAD1-4E4C-8453-A57B4CCBE3F3 Q34651312-B70F517D-AB5B-423B-BB0B-2BECF291A30C Q34793685-E2C00102-FDDB-4214-9333-57638DFD426A Q35100274-F3837789-6803-4C5C-B244-A58AD0735804 Q35133399-2573CE5A-E7E4-4E32-A80E-421C1832884E Q35229609-25D841A5-C857-424A-A760-06992D65B7AE Q35592159-FEDC8F42-3706-41B8-B22C-2F78DCC15A58 Q35629831-46C1FA03-9212-455B-99C0-605AFC7C3428 Q35656807-D2ADAD83-5461-4E53-8FFB-612BB50132EC Q36057705-AD9201A7-2792-4A75-AAC4-428079CF8C19 Q36416358-15E022CA-397D-4509-8442-B788C5C3B338 Q36515569-67C6C4FC-05F3-471A-AA9A-21D0D18A5192 Q36613455-E70C0303-8D30-47F7-9809-FF84B56D7500 Q36639638-8038ADEB-0092-4993-BC01-F51E97A04B62 Q36930863-AEA00047-EEBD-4034-90F0-D11B0019A1A6 Q36932782-DA4E89E5-6098-4F2F-8198-980F9376CE44 Q37137442-7B93D69A-7F75-499E-B3C1-1B326CFB87F3 Q37151715-D16F9234-7C12-40AD-AB9F-C53073B09739 Q37436085-2FC940B0-6FDE-433D-A31D-210EAFBB22BF Q37707110-7703C90B-3F9C-4706-9A4F-B4DDCA70D107 Q37941686-72F69FD1-AF06-47E5-BF9E-37843D9095D5 Q38061868-266A877C-40E6-46D0-9EBA-6991BDAC08D1 Q38119782-3936EF08-6D11-406E-982D-D82A60D275C5 Q38132808-9BC575D2-8212-404E-A8F5-043EF6A8C09E Q38195005-4E86EB77-F1B3-47AC-A377-58807F76CED1 Q38233723-EB9AA3E8-5F90-433B-A315-B32F3961773D Q38459037-7971C67A-160F-4DFB-8C48-B44B6CC9C174 Q38537765-4D07C3A5-58A3-4B2C-9498-4A7061B74DF2 Q38740496-85C88C21-3E0C-432A-ACE3-329C0BF82A68

P2860

Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors

http://www.wikidata.org/entity/Q33530669

description

2010 nî lūn-bûn

@nan

2010 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մարտին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Comparative analysis of small ...... lysine demethylase inhibitors

@ast

Comparative analysis of small ...... lysine demethylase inhibitors

@en

Comparative analysis of small ...... lysine demethylase inhibitors.

@nl

type

label

Comparative analysis of small ...... lysine demethylase inhibitors

@ast

Comparative analysis of small ...... lysine demethylase inhibitors

@en

Comparative analysis of small ...... lysine demethylase inhibitors.

@nl

prefLabel

Comparative analysis of small ...... lysine demethylase inhibitors

@ast

Comparative analysis of small ...... lysine demethylase inhibitors

@en

Comparative analysis of small ...... lysine demethylase inhibitors.

@nl

P1433

Q33530669-DF9D67F2-E9DC-425B-9D5E-65AA54D1909F

P1476

Q33530669-D52E2473-9AA7-4B46-9C93-5C6DA1C3108C

P2093

Q33530669-14F86B0F-C7FB-4A1F-905F-FF13AC9AAE8C

Q33530669-1DDDD5CF-220E-4E07-881D-0DA717650BAE

Q33530669-DC6BED92-C2C6-49B1-81AE-25E8F7F69F1A

P2860

Q33530669-1517C237-4E35-4318-AD31-B48C911E1A45

Q33530669-240B777A-C93A-4A0D-8D8D-F4569E85E160

Q33530669-28DFD80B-924A-4D0B-A48C-55CAC8D3F402

Q33530669-2F493781-1727-41BF-8258-127DA8BCDE60

Q33530669-3911D776-0678-4518-8868-56B4607CB010

Q33530669-3D17029B-93C6-4637-AF24-4A5B3D779319

Q33530669-443E6569-2CE1-4F39-9884-B2B75A701529

Q33530669-45B3D73F-28A8-4736-86F8-C1FE7B1C1FC0

Q33530669-53D8CF0D-BBDB-428A-B24C-C429135C1A1C

Q33530669-5853BE34-B0F7-4F2C-BEAF-0AB34DD9E73A

P304

Q33530669-7E4959E3-F337-407B-AF19-EA180D72C1C3

P31

Q33530669-362A1062-D8CD-44BE-B524-6236D2CE9717

P356

Q33530669-D5CA712E-12DF-4641-81F5-5CAC1DC54A86

P407

Q33530669-C9B213C5-6A9A-41EC-BE0F-664D38F539A6

P433

Q33530669-37600DE6-C59E-4BFE-B745-ABAA9C7457F7

P478

Q33530669-D17D42AC-17D6-477A-AC46-1467196F9B2A

P50

Q33530669-976ACA0B-8501-4350-9DCB-CCE72F23AE0E

P577

Q33530669-6426FE39-5430-40A4-9D6D-F7EB6293704B

P5875

Q33530669-350309FF-A15D-4AAE-81DF-2BD0AFFB0E2A

P698

Q33530669-A958E25B-1B58-45E1-A87C-AD530CCC3D6D

P932

Q33530669-D1B2A78B-E8D5-4AB7-AABB-B9A4A4712E84

P356

P1433

Journal of the American Chemical Society

P1476

Comparative analysis of small ...... lysine demethylase inhibitors

@en

P2093

Dongqing Wang

http://www.w3.org/2001/XMLSchema#string

Jeffrey C Culhane

http://www.w3.org/2001/XMLSchema#string

Philip A Cole

http://www.w3.org/2001/XMLSchema#string

P2860

Histone demethylation mediated by the nuclear amine oxidase homolog LSD1

Structural basis of histone demethylation by LSD1 revealed by suicide inactivation

Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine

Histone demethylation by a family of JmjC domain-containing proteins.

Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1

Coordinated histone modifications mediated by a CtBP co-repressor complex

CoREST is an integral component of the CoREST- human histone deacetylase complex

A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes

Observation of two different chromophores in the resting state of monoamine oxidase B by fluorescence spectroscopy

The epigenomics of cancer

P304

3164-3176

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/JA909996P

http://www.w3.org/2001/XMLSchema#string

P407

P433

9

http://www.w3.org/2001/XMLSchema#string

P478

132

http://www.w3.org/2001/XMLSchema#string

P50

P577

2010-03-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

41422971

http://www.w3.org/2001/XMLSchema#string

P698

20148560

http://www.w3.org/2001/XMLSchema#string

P932

2843942

http://www.w3.org/2001/XMLSchema#string