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Aldehyde dehydrogenase 3 family, member B1

ALDH3B1, ALDH7, Aldehyde Dehydrogenase 3B1, ALDH3B
The aldehyde dehydrogenases are a family of isozymes that may play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. This particular gene spans about 20 kb of genomic DNA and is composed of 9 coding exons. The gene is highly expressed in kidney and lung. The functional significance of this gene as well as the cellular localization of its product are presently unknown. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2009] (from NCBI)
Top mentioned proteins: ALDH8, antiquitin, ACID, POLYMERASE, Aldehyde Dehydrogenase
Papers on ALDH3B1
Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.
Tanner et al., Columbia, United States. In Biochemistry, Oct 2015
Five crystal structures and small-angle X-ray scattering data are reported, including the first crystal structure of any ALDH7 family member complexed with α-aminoadipate.
TraeALDH7B1-5A, encoding aldehyde dehydrogenase 7 in wheat, confers improved drought tolerance in Arabidopsis.
Zhang et al., Beijing, China. In Planta, Jul 2015
MAIN CONCLUSION: TraeALDH7B1 - 5A , encoding aldehyde dehydrogenase 7 in wheat, conferred significant drought tolerance to Arabidopsis , supported by molecular biological and physiological experiments.
Role and structural characterization of plant aldehyde dehydrogenases from family 2 and family 7.
Kopečný et al., Olomouc, Czech Republic. In Biochem J, Jun 2015
In the present study, we provide a detailed biochemical characterization of plant ALDH2 and ALDH7 families by analysing maize and pea ALDH7 (ZmALDH7 and PsALDH7) and four maize cytosolic ALDH(cALDH)2 isoforms RF2C, RF2D, RF2E and RF2F [the first maize ALDH2 was discovered as a fertility restorer (RF2A)].
Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via two C-terminal tryptophan residues and lipid modification.
Kihara et al., Sapporo, Japan. In Biochem J, 2015
Of the 21 ALDHs in mice, it is the ALDH3 family members (ALDH3A1, ALDH3A2, ALDH3B1, ALDH3B2 and ALDH3B3) that are responsible for the removal of lipid-derived aldehydes.
BRAFV600E-Associated Gene Expression Profile: Early Changes in the Transcriptome, Based on a Transgenic Mouse Model of Papillary Thyroid Carcinoma.
Jarzab et al., Gliwice, Poland. In Plos One, 2014
CONCLUSION: The study identified 7 BRAF-induced genes that are specific for BRAF V600E-driven PTC and not previously reported as related to BRAF mutation or thyroid carcinoma: MMD, ITPR3, AACS, LAD1, PVRL3, ALDH3B1, and RASA1.
Sequence and functional analyses of the aldehyde dehydrogenase 7B4 gene promoter in Arabidopsis thaliana and selected Brassicaceae: regulation patterns in response to wounding and osmotic stress.
Bartels et al., Bonn, Germany. In Planta, 2014
Despite the high conservation of the plant ALDH7 proteins and their importance in stress responses, their regulation has not been investigated.
Admixture mapping and subsequent fine-mapping suggests a biologically relevant and novel association on chromosome 11 for type 2 diabetes in African Americans.
Crawford et al., Nashville, United States. In Plos One, 2013
We identified 13 independent associations between TCIRG1, CHKA, and ALDH3B1 genes on chromosome 11 and T2D.
Substrate specificity, plasma membrane localization, and lipid modification of the aldehyde dehydrogenase ALDH3B1.
Kihara et al., Sapporo, Japan. In Biochim Biophys Acta, 2013
In the present study, we have identified that ALDH3B1 is also active in vitro toward C16 aldehydes and demonstrated that overexpression of ALDH3B1 restores the sphingolipid metabolism in the ALDH3A2-deficient cells.
Potential monovalent cation-binding sites in aldehyde dehydrogenases.
Muñoz-Clares et al., Mexico. In Chem Biol Interact, 2013
Among the ALDH enzymes studied, and according to our analyses, potential intra-subunit cation-binding sites seem to be present in most members of ALDH2, ALDH1L, ALDH4, ALDH5, ALDH7, ALDH10, and ALDH25 families, as well as in the bacterial and fungal members of the ALDH9 family and in a few ALDH1, ALDH6, ALDH11 and ALDH26 enzymes; potential inter-subunit sites in members of ALDH1L, ALDH3, ALDH4 from bacillales, ALDH5, ALDH7, ALDH9, ALDH10, ALDH11 and ALDH25 families; and potential central-cavity sites only in some bacterial and animal ALDH9s and in most members of the ALDH1L family.
Mutation of OsALDH7 causes a yellow-colored endosperm associated with accumulation of oryzamutaic acid A in rice.
Wan et al., Nanjing, China. In Planta, 2012
Aldehyde dehydrogenase proteins consist of a superfamily and the family 7 (ALDH7) is a typical group with highly conserved proteins across species.
The enzymatic activity of human aldehyde dehydrogenases 1A2 and 2 (ALDH1A2 and ALDH2) is detected by Aldefluor, inhibited by diethylaminobenzaldehyde and has significant effects on cell proliferation and drug resistance.
Chang et al., Gainesville, United States. In Chem Biol Interact, 2012
Furthermore, our TLDA results revealed that ALDH1, ALDH7, ALDH3 and ALDH8 are expressed in K562 cells.
The genome-wide expression profile of 1,2,3,4,6-penta-O-galloyl-β-D-glucose-treated MDA-MB-231 breast cancer cells: molecular target on cancer metabolism.
Kim et al., Seoul, South Korea. In Mol Cells, 2011
Through the Beadstudio v3 micro assay program to compare the identified genes expressed in PGG-treated MDA-MB-231 cells with untreated control, we found several unique genes that are closely associated with pyruvate metabolism, glycolysis/gluconeogenesis and tyrosine metabolism, including PC, ACSS2, ACACA, ACYP2, ALDH3B1, FBP1, PRMT2 and COMT.
Comparative studies of vertebrate aldehyde dehydrogenase 3: sequences, structures, phylogeny and evolution. Evidence for a mammalian origin for the ALDH3A1 gene.
Hempel et al., Brisbane, Australia. In Chem Biol Interact, 2011
Mammalian ALDH3 genes (ALDH3A1, ALDH3A2, ALDH3B1 and ALDH3B2) encode enzymes of peroxidic and fatty aldehyde metabolism.
Human antiquitin: structural and functional studies.
Fong et al., Hong Kong, Hong Kong. In Chem Biol Interact, 2011
Antiquitin (ALDH7) is a member of the aldehyde dehydrogenase superfamily which oxidizes various aldehydes to form the corresponding carboxylic acids.
Molecular characterization, expression analysis, and role of ALDH3B1 in the cellular protection against oxidative stress.
Vasiliou et al., Aurora, United States. In Free Radic Biol Med, 2010
protects cells from the damaging effects of oxidative stress
Aldehyde dehydrogenase 3B1 (ALDH3B1): immunohistochemical tissue distribution and cellular-specific localization in normal and cancerous human tissues.
Vasiliou et al., Aurora, United States. In J Histochem Cytochem, 2010
The specificity of ALDH3B1 distribution may prove to be directly related to the functional role of this enzyme in human tissues.
Evidence of epistasis between the catechol-O-methyltransferase and aldehyde dehydrogenase 3B1 genes in paranoid schizophrenia.
Shen et al., Beijing, China. In Biol Psychiatry, 2009
These findings provided convincing evidence that epistasis between the catechol-O-methyltransferase and aldehyde dehydrogenase 3B1 genes plays an important role in the pathogenesis of schizophrenia
Expression and initial characterization of human ALDH3B1.
Vasiliou et al., Denver, United States. In Biochem Biophys Res Commun, 2007
This study shows for the first time the functionality, expression and protective role of ALDH3B1 and indicates a potential physiological role of ALDH3B1 against oxidative stress.
Human aldehyde dehydrogenase gene family.
Chang et al., Duarte, United States. In Eur J Biochem, 1998
Metabolic disorders and clinical problems associated with mutations of ALDH1, ALDH2, ALDH4, ALDH10 and succinic semialdehyde (SSDH) genes have been emerged.
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