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Search results 801 to 900 out of 1112 for Cbs

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Type Details Score
Publication      
First Author: Knejzlík Z
Year: 2022
Journal: FEBS J
Title: The mycobacterial guaB1 gene encodes a guanosine 5'-monophosphate reductase with a cystathionine-β-synthase domain.
Protein Domain
Type: Family
Description: In Methanosarcina acetivorans, MA1821 is a L-aspartate semialdehyde sulfurtransferase required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis [, ]. It contains two C-terminal cystathionine beta-synthase (CBS) domains. The CBS domains bind S-adenosyl-l-methionine (SAM) and 5'-methylthioadenosine (MTA), which induce a conformational change consistent with regulatory function. Another protein in the same pathway, MA1822, is involved in the reduction of the disulfide formed in MA1821 during the conversion of Asa (aspartate semialdehyde) to Hcy [, ].
Protein Domain
Type: Family
Description: This family of proteins restricted to the high GC Gram-positive bacteria includes GMP reductase from Mycobacterium smegmatis (GUAB1), which is involved in the purine-salvage pathway. This protein is composed of two domains: a catalytic domain with a TIM barrel structure and another that folds as a typical Bateman domain composed of two CBS domains (cystathionine-beta-synthase domain, CBS, ), which are essential for the NADPH-dependent conversion of GMP to IMP [].
HT Experiment
Series Id: GSE54286
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: ArrayExpress
HT Experiment
Series Id: GSE54287
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: ArrayExpress
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
Publication  
First Author: Guo D
Year: 2005
Journal: Mol Pain
Title: Physical interaction and functional coupling between ACDP4 and the intracellular ion chaperone COX11, an implication of the role of ACDP4 in essential metal ion transport and homeostasis.
Volume: 1
Pages: 15
Publication
First Author: Chandran U
Year: 2016
Journal: Biol Reprod
Title: Expression of Cnnm1 and Its Association with Stemness, Cell Cycle, and Differentiation in Spermatogenic Cells in Mouse Testis.
Volume: 95
Issue: 1
Pages: 7
Publication    
First Author: Wang C
Year: 2000
Journal: GenBank Submission
Title: Mus musculus ancient conserved domain protein 3 (Adcp3) mRNA, compkete cds
Pages: AF216964
Publication
First Author: Meredith TC
Year: 2006
Journal: Biochem J
Title: Characterization of Escherichia coli D-arabinose 5-phosphate isomerase encoded by kpsF: implications for group 2 capsule biosynthesis.
Volume: 395
Issue: 2
Pages: 427-32
Publication
First Author: Bohmann K
Year: 1995
Journal: J Cell Biol
Title: Mutational analysis of p80 coilin indicates a functional interaction between coiled bodies and the nucleolus.
Volume: 131
Issue: 4
Pages: 817-31
Publication
First Author: Hebert MD
Year: 2000
Journal: Mol Biol Cell
Title: Self-association of coilin reveals a common theme in nuclear body localization.
Volume: 11
Issue: 12
Pages: 4159-71
Protein Domain
Type: Domain
Description: Coilin is a nuclear phosphoprotein that concentrates within Cajal bodies (CBs) and has a role in small nuclear ribonucleoprotein (snRNP) biogenesis []. Coilin also acts to repress polymerase I activity in response to cisplatin-induced DNA damage, which could indicate a link between the DNA damage response and the inhibition of rRNA synthesis [].Conservation at the amino acid level is highest within coilin's N- and C-termini. The first N-terminal 92-amino acid domain have been shown to self-interact and to be essential for proper targeting of coilin to CBs [, ].
Publication
First Author: Maclean KN
Year: 2019
Journal: FASEB J
Title: Taurine alleviates repression of betaine-homocysteine S-methyltransferase and significantly improves the efficacy of long-term betaine treatment in a mouse model of cystathionine β-synthase-deficient homocystinuria.
Volume: 33
Issue: 5
Pages: 6339-6353
Publication
First Author: Marechal D
Year: 2015
Journal: PLoS One
Title: Dosage of the Abcg1-U2af1 region modifies locomotor and cognitive deficits observed in the Tc1 mouse model of Down syndrome.
Volume: 10
Issue: 2
Pages: e0115302
Publication
First Author: Rauch BJ
Year: 2014
Journal: Mol Microbiol
Title: Novel proteins for homocysteine biosynthesis in anaerobic microorganisms.
Volume: 94
Issue: 6
Pages: 1330-42
Publication
First Author: Allen KD
Year: 2015
Journal: Biochemistry
Title: Homocysteine is biosynthesized from aspartate semialdehyde and hydrogen sulfide in methanogenic archaea.
Volume: 54
Issue: 20
Pages: 3129-32
Publication
First Author: Resch CT
Year: 2010
Journal: Biochemistry
Title: The putative Na+/H+ antiporter of Vibrio cholerae, Vc-NhaP2, mediates the specific K+/H+ exchange in vivo.
Volume: 49
Issue: 11
Pages: 2520-8
Publication
First Author: Wang CY
Year: 2004
Journal: BMC Genomics
Title: Molecular cloning and characterization of the mouse Acdp gene family.
Volume: 5
Issue: 1
Pages: 7
Publication
First Author: Fanourgakis G
Year: 2016
Journal: PLoS Genet
Title: Chromatoid Body Protein TDRD6 Supports Long 3' UTR Triggered Nonsense Mediated mRNA Decay.
Volume: 12
Issue: 5
Pages: e1005857
Publication
First Author: Yabuta Y
Year: 2011
Journal: J Cell Biol
Title: TDRD5 is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis in mice.
Volume: 192
Issue: 5
Pages: 781-95
Publication
First Author: Kabil O
Year: 2016
Journal: J Biol Chem
Title: Heme-dependent Metabolite Switching Regulates H2S Synthesis in Response to Endoplasmic Reticulum (ER) Stress.
Volume: 291
Issue: 32
Pages: 16418-16423
Publication
First Author: Anania C
Year: 2022
Journal: Nat Genet
Title: In vivo dissection of a clustered-CTCF domain boundary reveals developmental principles of regulatory insulation.
Volume: 54
Issue: 7
Pages: 1026-1036
Pseudogene
Type: pseudogene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein
Organism: Mus musculus/domesticus
Length: 570  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 573  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 572  
Fragment?: false
Publication
First Author: Gilder AS
Year: 2011
Journal: Mol Biol Cell
Title: Coilin participates in the suppression of RNA polymerase I in response to cisplatin-induced DNA damage.
Volume: 22
Issue: 7
Pages: 1070-9
Protein Domain
Type: Domain
Description: Synonym(s): Inosine-5'-monophosphate dehydrogenase, Inosinic acid dehydrogenase; Synonym(s): Guanosine 5'-monophosphate oxidoreductase This entry contains two related enzymes: IMP dehydrogenase and GMP reductase. These enzymes adopt a TIM barrel structure.IMP dehydrogenase () (IMPDH) catalyses the rate-limiting reaction of de novoGTP biosynthesis, the NAD-dependent reduction of IMP into XMP [].Inosine 5-phosphate + NAD++ H2O = xanthosine 5-phosphate + NADHIMP dehydrogenase is associated with cell proliferation and is a possible target for cancer chemotherapy. Mammalian and bacterial IMPDHs are tetramers of identical chains. There are two IMP dehydrogenase isozymes in humans []. IMP dehydrogenase nearly always contains a long insertion that has two CBS domains within it.GMP reductase () catalyses the irreversible and NADPH-dependent reductive deamination of GMP into IMP [].NADPH + guanosine 5-phosphate = NADP++ inosine 5-phosphate + NH3It converts nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and maintains intracellular balance of A and G nucleotides.
Protein Domain
Type: Conserved_site
Description: Synonym(s): Inosine-5'-monophosphate dehydrogenase, Inosinic acid dehydrogenase; Synonym(s): Guanosine 5'-monophosphate oxidoreductase This entry contains two related enzymes: IMP dehydrogenase and GMP reductase. These enzymes adopt a TIM barrel structure.IMP dehydrogenase () (IMPDH) catalyses the rate-limiting reaction of de novoGTP biosynthesis, the NAD-dependent reduction of IMP into XMP [].Inosine 5-phosphate + NAD++ H2O = xanthosine 5-phosphate + NADHIMP dehydrogenase is associated with cell proliferation and is a possible target for cancer chemotherapy. Mammalian and bacterial IMPDHs are tetramers of identical chains. There are two IMP dehydrogenase isozymes in humans []. IMP dehydrogenase nearly always contains a long insertion that has two CBS domains within it.GMP reductase () catalyses the irreversible and NADPH-dependent reductive deamination of GMP into IMP [].NADPH + guanosine 5-phosphate = NADP++ inosine 5-phosphate + NH3It converts nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and maintains intracellular balance of A and G nucleotides.
Publication
First Author: Andrews SC
Year: 1988
Journal: Biochem J
Title: Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12.
Volume: 255
Issue: 1
Pages: 35-43
Publication
First Author: Collart FR
Year: 1988
Journal: J Biol Chem
Title: Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs.
Volume: 263
Issue: 30
Pages: 15769-72
Publication
First Author: Natsumeda Y
Year: 1990
Journal: J Biol Chem
Title: Two distinct cDNAs for human IMP dehydrogenase.
Volume: 265
Issue: 9
Pages: 5292-5
Publication
First Author: Gibson MM
Year: 1991
Journal: Mol Microbiol
Title: Magnesium transport in Salmonella typhimurium: the influence of new mutations conferring Co2+ resistance on the CorA Mg2+ transport system.
Volume: 5
Issue: 11
Pages: 2753-62
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory