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Search results 301 to 339 out of 339 for Wwox

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Type Details Score
Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Allele
Wwox<tm1Ria> | MGI:3704944
Name: WW domain-containing oxidoreductase; targeted mutation 1, Rami I Aqeilan
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
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Publication
19465938 | J:153468
First Author: Bouteille N
Year: 2009
Journal: Oncogene
Title: Inhibition of the Wnt/beta-catenin pathway by the WWOX tumor suppressor protein.
Volume: 28
Issue: 28
Pages: 2569-80
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HT Experiment
GSE215425 | WWOX P47T loss-of-function mutation induces epilepsy, progressive neuroinflammation, and cerebellar degeneration
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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Publication
21115974 | J:170371
First Author: Fu J
Year: 2011
Journal: Blood
Title: The tumor suppressor gene WWOX links the canonical and noncanonical NF-κB pathways in HTLV-I Tax-mediated tumorigenesis.
Volume: 117
Issue: 5
Pages: 1652-61
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Publication
16061658 | J:177160
First Author: Aqeilan RI
Year: 2005
Journal: Cancer Res
Title: WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function.
Volume: 65
Issue: 15
Pages: 6764-72
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Publication
25678599 | J:227365
First Author: El-Hage P
Year: 2015
Journal: Mol Cancer Res
Title: The Tumor-Suppressor WWOX and HDAC3 Inhibit the Transcriptional Activity of the β-Catenin Coactivator BCL9-2 in Breast Cancer Cells.
Volume: 13
Issue: 5
Pages: 902-12
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Publication
24899407 | -
First Author: Zhang H
Year: 2014
Journal: Int J Oncol
Title: Upregulation of the putative oncogene COTE1 contributes to human hepatocarcinogenesis through modulation of WWOX signaling.
Volume: 45
Issue: 2
Pages: 719-31
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Interaction Experiment
Aqeilan RI (2008)
Description: The WWOX tumor suppressor is essential for postnatal survival and normal bone metabolism.
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Allele
Wwox<Gt(W088C04)Wrst> | MGI:4123234
Name: WW domain-containing oxidoreductase; gene trap W088C04, German Gene Trap Consortium
Allele Type: Gene trapped
Attribute String: Null/knockout, Reporter
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Strain
MGI:5496411 | B6.129S2-Wwox<Gt(W088C04)Wrst>/Ieg
Attribute String: congenic, mutant strain, gene trap
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Allele
Wwox<em1Mald> | MGI:7541100
Name: WW domain-containing oxidoreductase; endonuclease-mediated mutation 1, Marcelo Aldaz
Allele Type: Endonuclease-mediated
Attribute String: Humanized sequence
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DO Term
DOID:0080060 | autosomal recessive spinocerebellar ataxia 12
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Genotype
Genotype
Symbol: Wwox/Wwox
Background: FVB/N-Wwox
Zygosity: hm
Has Mutant Allele: true
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DO Term
DOID:0080452 | developmental and epileptic encephalopathy 28
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Protein
Q4FZH1
Organism: Mus musculus/domesticus
Length: 290  
Fragment?: false
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Protein
B2RVD7
Organism: Mus musculus/domesticus
Length: 139  
Fragment?: false
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Protein
D3YX96
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: true
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Protein
D3Z5C1
Organism: Mus musculus/domesticus
Length: 38  
Fragment?: true
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Protein
Q8BMZ6
Organism: Mus musculus/domesticus
Length: 54  
Fragment?: true
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Protein Domain
IPR030431 | FAM189
Type: Family
Description: This entry represents a family of uncharacterised proteins designated as FAM189 (family with sequence similarity 189). It consist of FAM189A1, FAM189A2 (protein X123) and FAM189B (protein COTE1). COTE1 contributes to hepatocellular carcinoma tumourigenesis by regulating cell proliferation through modulating WWOX signalling [].
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Protein
Q5HZJ5
Organism: Mus musculus/domesticus
Length: 669  
Fragment?: false
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Protein
Q6A044
Organism: Mus musculus/domesticus
Length: 515  
Fragment?: false
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Protein
D6RDQ0
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: false
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Protein
D6RFB2
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
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Protein
E9Q6P6
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
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Protein
D3Z6Z5
Organism: Mus musculus/domesticus
Length: 173  
Fragment?: true
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Protein
E9Q6C9
Organism: Mus musculus/domesticus
Length: 650  
Fragment?: false
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Protein
E9QP68
Organism: Mus musculus/domesticus
Length: 596  
Fragment?: false
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Publication
23028374 | J:190448
First Author: Arlt MF
Year: 2012
Journal: PLoS Genet
Title: De novo CNV formation in mouse embryonic stem cells occurs in the absence of Xrcc4-dependent nonhomologous end joining.
Volume: 8
Issue: 9
Pages: e1002981
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Publication
36498839 | J:334303
 
First Author: Lin YH
Year: 2022
Journal: Int J Mol Sci
Title: Zfra Inhibits the TRAPPC6AΔ-Initiated Pathway of Neurodegeneration.
Volume: 23
Issue: 23
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Publication
19708029 | -
First Author: Del Mare S
Year: 2009
Journal: J Cell Biochem
Title: WWOX: its genomics, partners, and functions.
Volume: 108
Issue: 4
Pages: 737-45
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Publication
25538133 | -
First Author: Schrock MS
Year: 2015
Journal: Exp Biol Med (Maywood)
Title: WWOX: a fragile tumor suppressor.
Volume: 240
Issue: 3
Pages: 296-304
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Protein Domain
IPR042732 | WWOX_SDR_c-like
Type: Domain
Description: This entry represents the classical-like SDR domain of human WWOX and related proteins. Proteins in this entry share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser [, ]. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central β-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction [, , , ].
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Protein
Q91WL8
Organism: Mus musculus/domesticus
Length: 414  
Fragment?: false
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Publication
12368099 | -
First Author: Kleiger G
Year: 2002
Journal: J Mol Biol
Title: GXXXG and GXXXA motifs stabilize FAD and NAD(P)-binding Rossmann folds through C(alpha)-H... O hydrogen bonds and van der waals interactions.
Volume: 323
Issue: 1
Pages: 69-76
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Publication
12604210 | -
 
First Author: Oppermann U
Year: 2003
Journal: Chem Biol Interact
Title: Short-chain dehydrogenases/reductases (SDR): the 2002 update.
Volume: 143-144
Pages: 247-53
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Publication
19011750 | -
First Author: Kavanagh KL
Year: 2008
Journal: Cell Mol Life Sci
Title: 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.
Volume: 65
Issue: 24
Pages: 3895-906
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Publication
7742302 | -
First Author: Jörnvall H
Year: 1995
Journal: Biochemistry
Title: Short-chain dehydrogenases/reductases (SDR).
Volume: 34
Issue: 18
Pages: 6003-13
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