Aldehyde dehydrogenase inhibitors: a comprehensive review of the pharmacology, mechanism of action, substrate specificity, and clinical application - Wikidata - awgldk - TriplyDB

Aldehyde dehydrogenase inhibitors: a comprehensive review of the pharmacology, mechanism of action, substrate specificity, and clinical application

Aldehyde dehydrogenase inhibitors: a comprehensive review of the pharmacology, mechanism of action, substrate specificity, and clinical application

http://www.wikidata.org/entity/Q28265682

about

Histone acetyltransferases: challenges in targeting bi-substrate enzymes Liver cancer stem cell markers: Progression and therapeutic implications Cancer Stem Cells in the Thyroid Aldehyde dehydrogenase 1A1 in stem cells and cancer Aldehyde dehydrogenase as a marker and functional mediator of metastasis in solid tumors Aldehyde Dehydrogenase 1 making molecular inroads into the differential vulnerability of nigrostriatal dopaminergic neuron subtypes in Parkinson's disease Aldehyde dehydrogenase inhibition generates a reactive dopamine metabolite autotoxic to dopamine neurons Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1 Structural basis of substrate selectivity of Δ1-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): Semialdehyde chain length Structures of Proline Utilization A Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function The Progress and Prospects of Putative Biomarkers for Liver Cancer Stem Cells in Hepatocellular Carcinoma Aldehyde dehydrogenase 2 in aplastic anemia, Fanconi anemia and hematopoietic stem cells Crystal structure of human aldehyde dehydrogenase 1A3 complexed with NAD(+) and retinoic acid Development of a high-throughput in vitro assay to identify selective inhibitors for human ALDH1A1 The cysteine proteome A transposable element insertion confers xenobiotic resistance in Drosophila Current approaches for the discovery of drugs that deter substance and drug abuse.Modulation of Ethanol-Metabolizing Enzymes by Developmental Lead Exposure: Effects in Voluntary Ethanol Consumption Combination of dasatinib and gemcitabine reduces the ALDH1A1 expression and the proliferation of gemcitabine-resistant pancreatic cancer MIA PaCa-2 cells.ALDH1A1 expression correlates with clinicopathologic features and poor prognosis of breast cancer patients: a systematic review and meta-analysis Dark Hydrazone Fluorescence Labeling Agents Enable Imaging of Cellular Aldehydic Load.Effect of various diets on the expression of phase-I drug-metabolizing enzymes in livers of mice Aldehyde dehydrogenases: from eye crystallins to metabolic disease and cancer stem cells Benomyl, aldehyde dehydrogenase, DOPAL, and the catecholaldehyde hypothesis for the pathogenesis of Parkinson's disease.Oral epithelial stem cells - implications in normal development and cancer metastasis.Targeting aldehyde dehydrogenase 2: new therapeutic opportunities.Chronic alcohol exposure differentially affects activation of female locus coeruleus neurons and the subcellular distribution of corticotropin releasing factor receptors.NEK2 mediates ALDH1A1-dependent drug resistance in multiple myeloma Characterization of two distinct structural classes of selective aldehyde dehydrogenase 1A1 inhibitors.Cisplatin-resistant cells in malignant pleural mesothelioma cell lines show ALDH(high)CD44(+) phenotype and sphere-forming capacity.Next generation of ALDH substrates and their potential to study maturational lineage biology in stem and progenitor cells A personalized medicine approach for Asian Americans with the aldehyde dehydrogenase 2*2 variant Relation of stem cell markers ALDH1 and CD44 with clinicopathological factors in urothelial carcinomas of urinary bladder.Role of aldehyde dehydrogenase in hypoxic vasodilator effects of nitrite in rats and humans Pathogen-associated molecular patterns activate expression of genes involved in cell proliferation, immunity and detoxification in the amebocyte-producing organ of the snail Biomphalaria glabrata.Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.Aldehyde dehydrogenase activity plays a Key role in the aggressive phenotype of neuroblastoma.STAT3 Blockade Inhibits Radiation-Induced Malignant Progression in Glioma.A High-Content Assay Enables the Automated Screening and Identification of Small Molecules with Specific ALDH1A1-Inhibitory Activity.

P2860

Q26745642-F715F88E-1944-4D89-904E-A1515910F8A9 Q26751026-E39D7ED7-45F7-4E6E-92D6-58043A6F925F Q26765947-F6ADEB33-95B6-43E5-A3DE-271193C28181 Q26771185-B9563128-2432-4DAE-8003-35587D7512B1 Q26786476-F41AD343-6E48-409A-9407-73BE79A86EB6 Q26850502-EDB84A11-9A2F-4C2F-A4D8-8786FF64EE43 Q26852122-CAD6313D-DCC0-44AC-86AE-89A93E0BA8D9 Q27024524-662E596C-FCE5-4D3E-90E3-A3D157AE9C2B Q27675774-48459925-2773-45C1-BD38-E1B52E88C02E Q27679462-E8F3C75F-EEB6-4DD9-9126-9E5BD9D28973 Q27728132-BFFC9FBD-710E-4C25-B113-0E7D6DC17471 Q28071619-E9F90194-21C1-461B-B1F4-FDC7BFC1768B Q28078884-0E8787A5-0611-415F-B755-191F54038211 Q28115266-84493740-EBA0-41CE-B2CD-AD3686EAD13F Q28117499-29E41695-CA7F-4D06-B388-404DC3679272 Q28395817-72D1158F-2871-4E6B-BC34-965D2E74F875 Q28541894-ED669F2A-7B46-4B61-B23A-952D3947DEA4 Q28973615-4A22FDAD-B1B2-421C-8B81-28CB47D14DA1 Q33715211-C5956482-BAE5-4944-A8F4-5E231F20B4C6 Q33778101-DCB7AD77-2473-4691-ADF9-7D87B29A8153 Q33804523-6BA029C4-FEB3-44B7-AE46-1A7982F82DEB Q33887825-8FDFF221-FEC1-4242-879D-16A46D60187F Q33894107-BB0C48A8-3D03-4545-A940-E9F86C249CB3 Q34026132-F16C315C-7CAD-4426-A88A-676B8AD911DB Q34065897-F728C791-A8DE-4183-BC71-30B87904F561 Q34147649-57FF55B1-8B59-4D11-A619-67394806BBA7 Q34395219-0177FA58-7425-4EEE-84E2-3A324199860A Q34647295-9885A3D6-C763-4AE8-909B-B1F620D9A99E Q35067960-81B43A0B-32BF-4303-A9D6-55FDCF7CCEDE Q35130660-4C4090F9-37CB-48BA-AA88-4ADF800BFC9E Q35177969-B80FF507-F26C-4FB9-A3FF-88E874F23E20 Q35274173-D024BC11-04FB-42FC-BFA1-E0A5697474FE Q35619842-BC1F9656-22C8-4F95-86C3-686862B130E0 Q35643960-3F96121F-2A18-489B-B2D4-81F2BCA6A7AD Q35846201-9E40279D-C222-42A7-B466-4CB8AD9DB0A4 Q35848242-766F0C65-8AB2-440A-A824-DD4D7A289C82 Q36045705-6ACD0234-B08B-4253-A26E-562DA724B01B Q36159646-5565D1C3-DB1E-4C43-B2D1-22D60D8B709D Q36172612-4B61ADAA-5C3C-435B-AD15-E3A36BF0F3DF Q36262477-30E9B0D1-3C04-417D-B3E5-56D8724E02EB

P2860

Aldehyde dehydrogenase inhibitors: a comprehensive review of the pharmacology, mechanism of action, substrate specificity, and clinical application

http://www.wikidata.org/entity/Q28265682

description

2012 nî lūn-bûn

@nan

2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Aldehyde dehydrogenase inhibit ...... city, and clinical application

@ast

Aldehyde dehydrogenase inhibit ...... city, and clinical application

@en

Aldehyde dehydrogenase inhibit ...... city, and clinical application

@nl

type

label

Aldehyde dehydrogenase inhibit ...... city, and clinical application

@ast

Aldehyde dehydrogenase inhibit ...... city, and clinical application

@en

Aldehyde dehydrogenase inhibit ...... city, and clinical application

@nl

prefLabel

Aldehyde dehydrogenase inhibit ...... city, and clinical application

@ast

Aldehyde dehydrogenase inhibit ...... city, and clinical application

@en

Aldehyde dehydrogenase inhibit ...... city, and clinical application

@nl

P1433

Q28265682-4DA32235-AF0C-40F6-916C-3400F6285115

P1476

Q28265682-9D556FC5-6A73-4C85-B978-89602BB21408

P2093

Q28265682-0B4D113F-5578-47DA-980B-EB295B99F616

Q28265682-0F4988AE-FC2E-4117-ABA0-435DA0848DCC

Q28265682-5684CB09-3DE5-4AA5-9368-5FAE2CAAD0A7

Q28265682-738DC552-332A-4374-A350-B6074B4C1F7E

Q28265682-78851C0C-08EB-4B9A-AD20-39A0E73B0AF2

Q28265682-D02C6413-3CA4-4671-9295-C8F33912BC08

Q28265682-D546E607-0CCF-4FD0-B555-CC9656F07EEB

Q28265682-E67E6C32-A78A-4702-BE26-3444C2897CD0

Q28265682-F044A555-C151-49D0-AEAE-877D3CDDF3CC

P2860

Q28265682-04536907-2F05-4CE6-95E1-78A0B764DB1B

Q28265682-045B299D-31BC-4A35-988A-4E40D3FAF814

Q28265682-06A8351F-BA7F-4FD3-932E-8F04EE3ABFA8

Q28265682-077B8A62-ACC7-442B-A0A7-E42658F84E84

Q28265682-09F7A8EF-8AC7-4A8F-92DD-C93475293A83

Q28265682-0AB61B5E-351D-45BE-B777-23B26DC3B478

Q28265682-0EACE362-B9A3-4CD7-98AC-DD00D5E9193D

Q28265682-0ECC6038-6E86-434B-8E96-464FBCB7EEB9

Q28265682-0FF53334-CA06-401C-A410-2E098EB10801

Q28265682-113CF425-F13A-45E7-B3C0-65E4B98853DF

P304

Q28265682-A2133CFB-086D-40CB-B42A-55B40B7296EB

P31

Q28265682-3B8B7401-F275-477F-A92C-7F6BF2840894

P3181

Q28265682-90D672B7-9DD3-4CF9-A36B-8211A56B1152

P356

Q28265682-C761DD23-4980-4D67-83D4-AE8F2D9CCA44

P407

Q28265682-5EE79050-BFFC-4D15-8EB1-58C55CD5E0FE

P433

Q28265682-78EE6D42-9992-40E5-BBEF-B0311D02F62C

P478

Q28265682-4C72E59E-2130-4E31-B1C6-553FE0CC2F56

P50

Q28265682-7A59F90D-5CF2-4683-BBA4-18BCE052CAEE

P577

Q28265682-73C9AFFC-7A89-46B2-BACD-7E5FFEFB72CB

P5875

Q28265682-F9FEB727-B321-4012-BF57-91538E4BBF9B

P698

Q28265682-F1507114-17CF-446F-B6D9-07FF4BDE1018

P921

Q28265682-E1EE76C2-1B35-4882-9BDF-E9A577B8E516

P932

Q28265682-4CB8CDC1-7E68-42E5-B104-DC1D3B1CAAF7

P3181

P356

P1433

Pharmacological Reviews

P1476

Aldehyde dehydrogenase inhibit ...... city, and clinical application

@en

P2093

David C Thompson

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

Dennis Petersen

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

Kyriacos C Nicolaou

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

Manuel Ellermann

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

Richard A Deitrich

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

Risto O Juvonen

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

Thomas D Hurley

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

Vindhya Koppaka

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

Ying Chen

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

P2860

Structural and functional modifications of corneal crystallin ALDH3A1 by UVB light

Distinct expression levels and patterns of stem cell marker, aldehyde dehydrogenase isoform 1 (ALDH1), in human epithelial cancers

Actual Causes of Death in the United States, 2000

Opioid antagonists for alcohol dependence

Aldehyde dehydrogenase 7A1 (ALDH7A1) attenuates reactive aldehyde and oxidative stress induced cytotoxicity

Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress

Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily

4-(N,N-dipropylamino)benzaldehyde inhibits the oxidation of all-trans retinal to all-trans retinoic acid by ALDH1A1, but not the differentiation of HL-60 promyelocytic leukemia cells exposed to all-trans retinal

Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans

Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase

P304

520-39

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

P31

scholarly article

P3181

1276739

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

P356

10.1124/PR.111.005538

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

P407

P433

3

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

P478

64

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

P50

Vasilis Vasiliou

P577

2012-07-01T00:00:00Z

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

P5875

224868487

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

P698

22544865

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

P921

P932

3400832

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