Relationships within the aldehyde dehydrogenase extended family. - Wikidata - awgldk - TriplyDB

Relationships within the aldehyde dehydrogenase extended family.

Relationships within the aldehyde dehydrogenase extended family.

http://www.wikidata.org/entity/Q36281208

about

A new and unified nomenclature for male fertility restorer (RF) proteins in higher plants Geraniol and geranial dehydrogenases induced in anaerobic monoterpene degradation by Castellaniella defragrans Expression and initial characterization of human ALDH3B1 Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolution The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity Conserved Catalytic Residues of the ALDH1L1 Aldehyde Dehydrogenase Domain Control Binding and Discharging of the Coenzyme Structural Basis for a Cofactor-dependent Oxidation Protection and Catalysis of Cyanobacterial Succinic Semialdehyde Dehydrogenase Structure and activity of the NAD(P)+-dependent succinate semialdehyde dehydrogenase YneI from Salmonella typhimurium Mutations in antiquitin in individuals with pyridoxine-dependent seizures Biodegradation of aromatic compounds by Escherichia coli A gatekeeper helix determines the substrate specificity of Sjögren-Larsson Syndrome enzyme fatty aldehyde dehydrogenase The bifunctional Entamoeba histolytica alcohol dehydrogenase 2 (EhADH2) protein is necessary for amebic growth and survival and requires an intact C-terminal domain for both alcohol dahydrogenase and acetaldehyde dehydrogenase activity Fatty aldehydes in cyanobacteria are a metabolically flexible precursor for a diversity of biofuel products Structural shifts of aldehyde dehydrogenase enzymes were instrumental for the early evolution of retinoid-dependent axial patterning in metazoans Methanopyrus kandleri glutamyl-tRNA reductase.Characterization of Sphingomonas aldehyde dehydrogenase catalyzing the conversion of various aromatic aldehydes to their carboxylic acids.Regulation of the aldehyde dehydrogenase gene (aldA) and its role in the control of the coinducer level necessary for induction of the ethanol utilization pathway in Aspergillus nidulans.Aldehyde dehydrogenase. Maintaining critical active site geometry at motif 8 in the class 3 enzyme.Identification and characterization of Thermoplasma acidophilum glyceraldehyde dehydrogenase: a new class of NADP+-specific aldehyde dehydrogenase.Metabolic fate of L-lactaldehyde derived from an alternative L-rhamnose pathway.RNAi-directed downregulation of OsBADH2 results in aroma (2-acetyl-1-pyrroline) production in rice (Oryza sativa L.).Modeling-dependent protein characterization of the rice aldehyde dehydrogenase (ALDH) superfamily reveals distinct functional and structural features MPI-PHYLIP: parallelizing computationally intensive phylogenetic analysis routines for the analysis of large protein families Different specificities of two aldehyde dehydrogenases from Saccharomyces cerevisiae var. boulardii.Genotypic and phenotypic spectrum of pyridoxine-dependent epilepsy (ALDH7A1 deficiency).Families of retinoid dehydrogenases regulating vitamin A function: production of visual pigment and retinoic acid.The ald gene, encoding a coenzyme A-acylating aldehyde dehydrogenase, distinguishes Clostridium beijerinckii and two other solvent-producing clostridia from Clostridium acetobutylicum Identification of a transcriptional activator (ChnR) and a 6-oxohexanoate dehydrogenase (ChnE) in the cyclohexanol catabolic pathway in Acinetobacter sp. Strain NCIMB 9871 and localization of the genes that encode them.The molecular basis of Sjögren-Larsson syndrome: mutation analysis of the fatty aldehyde dehydrogenase gene.Modulation of ethanol stress tolerance by aldehyde dehydrogenase in the mycorrhizal fungus Tricholoma vaccinum.Metabolic conversion as a pre-receptor control mechanism for lipophilic hormones.Use of RNA fingerprinting to identify fungal genes specifically expressed during ectomycorrhizal interaction.Crystallographic and spectroscopic snapshots reveal a dehydrogenase in action.Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633.Prevalence of ALDH7A1 mutations in 18 North American pyridoxine-dependent seizure (PDS) patients.Alanyl-phosphatidylglycerol synthase: mechanism of substrate recognition during tRNA-dependent lipid modification in Pseudomonas aeruginosa.Genetic and biochemical characterization of a pathway for the degradation of 2-aminoethylphosphonate in Sinorhizobium meliloti 1021.The Class D beta-lactamase family: residues governing the maintenance and diversity of function TraeALDH7B1-5A, encoding aldehyde dehydrogenase 7 in wheat, confers improved drought tolerance in Arabidopsis.

P2860

Q21562123-79A28585-F869-49BB-92CA-36CA78457A6C Q24617205-5A38F7A3-7C39-42B8-873D-2AAECB364328 Q24683659-E9E09DB6-EF41-4EC8-BE2D-46F63EA98180 Q27625404-3D921ADE-0314-4BE3-92D4-DDAE36C1D2B5 Q27642894-A7891723-D1B4-49B6-A2DD-1BD8796D47F5 Q27651513-A124D86D-B491-4F4E-9F58-E512DEF623D1 Q27667677-866D3AFB-4D9D-46CA-A094-AFB884819DD1 Q27677380-141E23C2-1F68-4467-8F99-A58C7CBA6107 Q27683578-CB66470A-D9D8-43EB-89C3-8E3908C75D98 Q28118156-E2F8AA1A-FEEF-419C-A73E-215750695356 Q28208239-5C0F4C97-6904-4B07-AC46-583888518CD9 Q28244383-21B1105D-DDCF-41A7-A87D-26944F6EAE38 Q28361546-372DF349-ECBD-42F4-9CEF-691C5669C854 Q28704073-F4B1CDD2-2CB2-4138-B05E-E9933B41B201 Q30497836-8E9FBD00-71D1-49B6-B0FC-4512C61358C0 Q30791389-B6E60689-25D2-4ED7-9DE0-0F9645AB1AFF Q31157669-B0D815EA-4755-4A36-B44D-DBD7030CDF73 Q31644831-D81F416E-4F8C-45FB-B650-8CE2FFA6828F Q31897287-49B5AAA9-25EE-4917-906A-68EDE5291748 Q33237746-B60F3990-3C96-4F85-B8BB-4925BAD9AEFD Q33369531-4C007A20-401C-44B3-82CB-EABDAAC4C053 Q33374442-C3BEC2E3-E237-4F6D-83AF-222E5632A044 Q33633971-0F061F16-5AB3-4CA8-9DC0-3F2DD1F3C0AB Q33749899-59F7FE4B-442D-4F79-AABC-810E39316041 Q33832897-26D341DE-1F99-4E5D-BD97-630AC1C6BAAD Q33944232-08F3536E-42B0-4CB6-B5E3-2FC1F356BCD0 Q33958544-89A09B52-16B2-4F68-93CB-E79EBB39BEEA Q33986017-DFA9280E-CDBE-461E-846B-07890C75E64D Q33986072-FF0B4B60-029E-459B-9AA4-FB56F01E0863 Q34146285-451D8EFD-DE92-4D5A-99A3-5FF876B843AC Q34239981-699A450B-9D7B-4B14-B977-CA3E4A5E99A7 Q34328117-42177A7F-ECC3-47BD-ACDC-F153B0257099 Q34569949-64858A8F-0F3C-492A-9015-3B874726EE4D Q34865894-CABF0188-B2F4-4A6B-B194-135F5E62A0DF Q34891664-A6766DAA-5D03-4042-B5AB-A75512BA70F1 Q34917047-5C5A12D5-7DE5-4F3B-B95E-4ADE8EC4138B Q35034095-4B195E78-9732-4CEF-8A83-74B4F276E562 Q35063079-0BAE309F-8795-47A1-BDFB-3F8CD4310801 Q35205723-9414984E-BFF0-481D-97F6-E626350E5D3F Q35609841-6EDAB80E-6F16-4255-A8B1-97E347EAF050

P2860

Relationships within the aldehyde dehydrogenase extended family.

http://www.wikidata.org/entity/Q36281208

description

1999 nî lūn-bûn

@nan

1999年の論文

@ja

1999年学术文章

@wuu

1999年学术文章

@zh-cn

1999年学术文章

@zh-hans

1999年学术文章

@zh-my

1999年学术文章

@zh-sg

1999年學術文章

@yue

1999年學術文章

@zh

1999年學術文章

@zh-hant

name

Relationships within the aldehyde dehydrogenase extended family.

@ast

Relationships within the aldehyde dehydrogenase extended family.

@en

type

label

Relationships within the aldehyde dehydrogenase extended family.

@ast

Relationships within the aldehyde dehydrogenase extended family.

@en

prefLabel

Relationships within the aldehyde dehydrogenase extended family.

@ast

Relationships within the aldehyde dehydrogenase extended family.

@en

P1433

Q36281208-F8A61F50-6E59-41A5-9910-42E0B3CAE34F

P1476

Q36281208-DFEA7278-9CCF-42D4-9064-E90297440663

P2093

Q36281208-1D1C9068-F741-4740-818A-692A3BDEB7CC

Q36281208-2C6A84EC-4D93-4837-B0BD-0CE1F725C202

Q36281208-4E357DA3-34EB-47E0-91A6-D853263F3CD8

Q36281208-78DC263B-4992-4736-A13A-79E02E7FD7F7

Q36281208-B62373F2-F4EC-479D-9076-D69AFBF5BFD2

P2860

Q36281208-039974E9-6526-4BFD-AD1E-4A2EF8727BE1

Q36281208-1A59BAF5-7D3D-4AD7-9C12-F54F69850344

Q36281208-1A84B3B8-347F-4696-A025-63BB5C4D023C

Q36281208-38AF18AC-684F-41F8-9810-398C4933C1E3

Q36281208-41FC1B00-1F8B-4C79-BFAF-20876E5F79AB

Q36281208-467006E3-BF6D-4330-8B66-F52398B9459F

Q36281208-4785A51D-E9A1-40D7-B14A-C6A86F329946

Q36281208-4D8D4B3C-2BB7-436E-95C0-3B93E4DB271C

Q36281208-4E8A0E6A-C0CA-4193-AA2A-D2EC5DA12DD4

Q36281208-5ACE4694-13B1-4230-B273-7A2458E5FE5D

P304

Q36281208-7010F399-B618-4F5A-B23A-D60B8E93FBAC

P31

Q36281208-545C9684-C8C8-4D12-9207-27E026062D6D

P356

Q36281208-A51BD511-004C-40F9-9674-B11D715B0E3B

P433

Q36281208-686B4CA2-3D48-491B-907E-0EB81952455A

P478

Q36281208-95D59CAF-2E62-40E7-8E74-A60C06009049

P577

Q36281208-B0497E99-FC66-4E0A-91E5-962EDC152D3A

P5875

Q36281208-48F5E2C8-0DB7-442D-B976-7CF09CC1AB2E

P698

Q36281208-B7C5E19B-ABA7-43EE-9549-6CD1F9899ED5

P932

Q36281208-5B443346-8566-48AB-A946-6B289846E956

P356

P1433

Protein Science

P1476

Relationships within the aldehyde dehydrogenase extended family.

@en

P2093

B C Wang

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

H Nicholas

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

J Hempel

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

J Perozich

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

R Lindahl

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

P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution

Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

SAGA: sequence alignment by genetic algorithm

Structure of betaine aldehyde dehydrogenase at 2.1 A resolution

Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida

Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate

Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway

The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold

P304

137-146

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

P31

scholarly article

P356

10.1110/PS.8.1.137

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

P433

1

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

P478

8

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

P577

1999-01-01T00:00:00Z

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

P5875

13088530

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

P698

10210192

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

P932

2144113

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