The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative - Wikidata - awgldk - TriplyDB

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

http://www.wikidata.org/entity/Q24620663

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative High-affinity inhibitors of human NAD-dependent 15-hydroxyprostaglandin dehydrogenase: mechanisms of inhibition and structure-activity relationships Gene family matters: expanding the HGNC resource Identification and Roles of Photosystem II Assembly, Stability, and Repair Factors in Arabidopsis Insights in 17beta-HSD1 enzyme kinetics and ligand binding by dynamic motion investigation Structural Insight into Substrate Differentiation of the Sugar-metabolizing Enzyme Galactitol Dehydrogenase from Rhodobacter sphaeroides D Crystal Structure of Uronate Dehydrogenase from Agrobacterium tumefaciens Crystal structure of the enzyme CapF of Staphylococcus aureus reveals a unique architecture composed of two functional domains Biochemical and structural characterization of recombinant short-chain NAD(H)-dependent dehydrogenase/reductase from Sulfolobus acidocaldarius highly enantioselective on diaryl diketone benzil Dual catalysis mode for the dicarbonyl reduction catalyzed by diketoreductase Structural insights into the role of Bacillus subtilis YwfH (BacG) in tetrahydrotyrosine synthesis Enzymatic Metabolism of Vitamin A in Developing Vertebrate Embryos A subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase--extensive moonlighting in mitochondrial tRNA biogenesis Species used for drug testing reveal different inhibition susceptibility for 17beta-hydroxysteroid dehydrogenase type 1 Structural basis for substrate specificity in human monomeric carbonyl reductases SRP-35, a newly identified protein of the skeletal muscle sarcoplasmic reticulum, is a retinol dehydrogenase Isolation and biochemical characterization of a glucose dehydrogenase from a hay infusion metagenome Structural and Biochemical Characterization of the Early and Late Enzymes in the Lignin β-Aryl Ether Cleavage Pathway from Sphingobium sp. SYK-6 In silico structure-function analysis of pathological variation in the HSD11B2 gene sequence Potential Antiosteoporotic Natural Product Lead Compounds That Inhibit 17β-Hydroxysteroid Dehydrogenase Type 2.Insights into the evolution of sorbitol metabolism: phylogenetic analysis of SDR196C family Signatures of Archaic Adaptive Introgression in Present-Day Human Populations.Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum In vitro gene regulatory networks predict in vivo function of liver Molecular basis for enantioselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases, a unique pair of stereoselective short-chain dehydrogenases/reductases involved in aliphatic epoxide carboxylation.Functions of Intracellular Retinoid Binding-Proteins.The functions of key residues in the inhibitor, substrate and cofactor sites of human 3beta-hydroxysteroid dehydrogenase type 1 are validated by mutagenesis.The Vein Patterning 1 (VEP1) gene family laterally spread through an ecological network Substrate binding process and mechanistic functioning of type 1 11β-hydroxysteroid dehydrogenase from enhanced sampling methods.Polyphenism in social insects: insights from a transcriptome-wide analysis of gene expression in the life stages of the key pollinator, Bombus terrestris.Selective inhibition of human 3β-hydroxysteroid dehydrogenase type 1 as a potential treatment for breast cancer.15-Oxoeicosatetraenoic acid is a 15-hydroxyprostaglandin dehydrogenase-derived electrophilic mediator of inflammatory signaling pathways.The plant short-chain dehydrogenase (SDR) superfamily: genome-wide inventory and diversification patterns.Homozygous and compound-heterozygous mutations in TGDS cause Catel-Manzke syndrome.The catalytic roles of P185 and T188 and substrate-binding loop flexibility in 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni.The amyloid-β-SDR5C1(ABAD) interaction does not mediate a specific inhibition of mitochondrial RNase P.Crystallization and preliminary X-ray crystallographic analysis of the short-chain dehydrogenase/reductase-type DDB_G0291732 protein from Dictyostelium discoideum.Evidence for expression of 11β-hydroxysteroid dehydrogenase type3 (HSD11B3/HSD11B1L) in neonatal pig testis.Submicroscopic deletions at 13q32.1 cause congenital microcoria.Ancient origin of the biosynthesis of lignin precursors

P2860

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P2860

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

http://www.wikidata.org/entity/Q24620663

description

2009 nî lūn-bûn

@nan

2009 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի մարտին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

@ast

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

@en

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

@nl

type

label

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

@ast

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

@en

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

@nl

prefLabel

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

@ast

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

@en

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

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P1433

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P356

J.CBI.2008.10.040

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Chemico-biological Interactions

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The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

@en

P2093

Angelo D Favia

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

Edmund Maser

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

Hans Jörnvall

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Kathryn L Kavanagh

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Michael Kisiela

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

Rebekka Mindnich

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

Roser Gonzalez Duarte

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

Stephen L Dellaporta

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

Yvonne Kallberg

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

P2860

The Sorcerer II Global Ocean Sampling Expedition: metagenomic characterization of viruses within aquatic microbial samples

The Universal Protein Resource (UniProt)

The Pfam protein families database

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes

Multiple sequence alignment with the Clustal series of programs

NCBI reference sequences (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins

The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases

Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein

Short-chain dehydrogenases/reductases (SDR)

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94-8

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P31

scholarly article

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4632639

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10.1016/J.CBI.2008.10.040

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P407

P433

1-3

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178

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P50

Elspeth A Bruford

Natalia Y. Kedishvili

Trevor M Penning

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2009-03-16T00:00:00Z

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23491639

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19027726

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2896744

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