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Search results 1001 to 1100 out of 1932 for Tat

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Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Strain
MGI:6446953 | B6.Cg-Apoe<tm1.1(APOE*4)Adiuj> App<em1Adiuj> Cd2ap<em1Adiuj> Trem2<em1Adiuj>/J
Attribute String: congenic, endonuclease-mediated mutation, mutant strain, targeted mutation
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Strain
MGI:6508535 | B6.Cg-Mthfr<em1Adiuj> Apoe<tm1.1(APOE*4)Adiuj> App<em1Adiuj> Trem2<em1Adiuj>/J
Attribute String: targeted mutation, mutant strain, endonuclease-mediated mutation, congenic
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Strain
MGI:6369607 | B6(SJL)-Apoe<tm1.1(APOE*4)Adiuj> Plcg2<em3Adiuj> App<em1Adiuj> Trem2<em1Adiuj>/J
Attribute String: mutant strain, targeted mutation, endonuclease-mediated mutation
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Strain
MGI:6444736 | B6.Cg-Apoe<tm1.1(APOE*4)Adiuj> Scimp<em1Adiuj> App<em1Adiuj> Trem2<em1Adiuj>/J
Attribute String: congenic, endonuclease-mediated mutation, mutant strain, targeted mutation
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Strain
MGI:7544905 | B6(SJL)-Apoe<tm1.1(APOE*4)Adiuj> Tc(HSA17)2Mdk App<em1Adiuj>/J
Attribute String: endonuclease-mediated mutation, mutant strain, targeted mutation
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Strain
MGI:6369611 | B6(SJL)-Apoe<tm1.1(APOE*4)Adiuj> Tc(HSA17)1Mdk App<em1Adiuj>/AdiujJ
Attribute String: endonuclease-mediated mutation, targeted mutation, mutant strain
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Strain
MGI:6430102 | STOCK Tyr<em19Ove>/Mmmh
Attribute String: mutant stock, endonuclease-mediated mutation
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Genotype
Genotype
Symbol: Smn1/Smn1 Tg(SMN1-SMN2*)16Cll/? Grm7/Grm7
Background: involves: 129P2/OlaHsd * C57BL/6 * FVB/N
Zygosity: cx
Has Mutant Allele: true
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Protein
O35295
Organism: Mus musculus/domesticus
Length: 324  
Fragment?: false
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Protein
Q8R4E6
Organism: Mus musculus/domesticus
Length: 350  
Fragment?: false
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Protein
Q3UTJ8
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: true
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Protein
C4PFH6
Organism: Mus musculus/domesticus
Length: 92  
Fragment?: false
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Protein
Q8BQK8
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: true
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Publication
16221580 | -
 
First Author: McCrindle SL
Year: 2005
Journal: Adv Microb Physiol
Title: Microbial dimethylsulfoxide and trimethylamine-N-oxide respiration.
Volume: 50
Pages: 147-98
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Publication
1324728 | -
First Author: Weiner JH
Year: 1992
Journal: Biochim Biophys Acta
Title: Molecular analysis of dimethylsulfoxide reductase: a complex iron-sulfur molybdoenzyme of Escherichia coli.
Volume: 1102
Issue: 1
Pages: 1-18
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Publication
14522592 | -
First Author: Lubitz SP
Year: 2003
Journal: Arch Biochem Biophys
Title: The Escherichia coli ynfEFGHI operon encodes polypeptides which are paralogues of dimethyl sulfoxide reductase (DmsABC).
Volume: 418
Issue: 2
Pages: 205-16
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Publication
12679550 | -
First Author: Lebrun E
Year: 2003
Journal: Mol Biol Evol
Title: Arsenite oxidase, an ancient bioenergetic enzyme.
Volume: 20
Issue: 5
Pages: 686-93
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Publication
8760916 | -
 
First Author: Eder S
Year: 1996
Journal: Microbiology
Title: A Bacillus subtilis secreted phosphodiesterase/alkaline phosphatase is the product of a Pho regulon gene, phoD.
Volume: 142 ( Pt 8)
Pages: 2041-7
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Publication
15588701 | -
First Author: Yang H
Year: 2004
Journal: Biochim Biophys Acta
Title: Expression and characterization of a heterodimer of Streptomyces chromofuscus phospholipase D.
Volume: 1703
Issue: 1
Pages: 43-51
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Publication
17906150 | -
First Author: Apel AK
Year: 2007
Journal: Microbiology
Title: Phosphate control of phoA, phoC and phoD gene expression in Streptomyces coelicolor reveals significant differences in binding of PhoP to their promoter regions.
Volume: 153
Issue: Pt 10
Pages: 3527-37
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Publication
16517638 | -
First Author: Monds RD
Year: 2006
Journal: Appl Environ Microbiol
Title: Conservation of the Pho regulon in Pseudomonas fluorescens Pf0-1.
Volume: 72
Issue: 3
Pages: 1910-24
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Publication
18039941 | -
First Author: Prados Rosales RC
Year: 2008
Journal: Eukaryot Cell
Title: Vegetative hyphal fusion is not essential for plant infection by Fusarium oxysporum.
Volume: 7
Issue: 1
Pages: 162-71
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Publication
22289056 | -
First Author: Coulthurst SJ
Year: 2012
Journal: Biochemistry
Title: Conserved signal peptide recognition systems across the prokaryotic domains.
Volume: 51
Issue: 8
Pages: 1678-86
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Publication
16540088 | -
First Author: Chan CS
Year: 2006
Journal: Biochem Biophys Res Commun
Title: Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli.
Volume: 343
Issue: 1
Pages: 244-51
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Protein Domain
IPR018946 | PhoD-like_MPP
Type: Domain
Description: Alkaline phosphatase D (PhoD) []catalyses the reaction: phosphate monoester + H(2)O = an alcohol + phosphate. PhoD is similar to Ca(2+)-dependent phospholipase D [], which catalyses the hydrolysis of the ester bond between the phosphatidic acid and alcohol moieties of phospholipids [, ].PhoD (also known as alkaline phosphatase D/APaseD in Bacillus subtilis) is a secreted phosphodiesterase encoded by phoD of the Pho regulon in Bacillus subtilis. PhoD homologs are found in prokaryotes, eukaryotes, and archaea. PhoD contains a twin arginine (RR) motif and is transported by the Tat (Twin-arginine translocation) translocation pathway machinery (TatAyCy) [, , , ]. Proteins containing this domain also includes the Fusarium oxysporum Fso1 protein []. PhoD belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but allshare a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double β-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination [].
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Protein Domain
IPR020945 | DMSO/NO3_reduct_chaperone
Type: Family
Description: This entry represents a family of proteins which are involved in enzymes assembly and/or maturation: The TorD protein is involved in the maturation of the the trimethylamine N-oxide reductase TorA (a DMSO reductase family member) in Escherichia coli []. TorA is a molybdenum-containing enzyme which requires the the insertion of a bis(molybdopterin guanine dinucleotide) molybdenum (bis(MGD)Mo) cofactor in its catalytic site to be active and translocated to the periplasm. TorD acts as a chaperone, binding to apoTorA and promoting efficient incorporation of the cofactor into the protein.Nitrate reductase delta subunit (NarJ). This subunit is not part of the nitrate reductase enzyme but is a chaperone required for proper molybdenum cofactor insertion and final assembly of the nitrate reductase [, , ]. NarJ exhibits sequence homology to chaperones involved in maturation and cofactor insertion of E. coli redox enzymes that are mediated by twin-arginine translocase (Tat) dependent translocation []. The archetypal Tat proofreading chaperones belong to the TorD family [].Twin-arginine leader-binding protein DmsD, which could be required for the biogenesis of DMSO reductase rather than for the targeting of DmsA to the inner membrane [, , ].Dimethyl sulphide dehydrogenase protein DdhD. This protein is thought to function as chaperone protein in the assembly of an active dimethyl sulphide dehydrogenase DdhABC [].
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Protein Domain
IPR034217 | SART3_RRM1
Type: Domain
Description: This entry represents the RNA recognition motif 1 (RRM1) of SART3 (also known as Tip110), which is an RNA-binding protein expressed in the nucleus of the majority of proliferating cells, including normal cells and malignant cells, but not in normal tissues except for the testes and fetal liver []. It is involved in the regulation of mRNA splicing probably via its complex formation with RNPS1 (an RNA-binding protein with a serine-rich domain), a pre-mRNA-splicing factor []. SART3 has also been identified as a nuclear Tat-interacting protein that regulates Tat transactivation activity through direct interaction and functions as an important cellular factor for HIV-1 gene expression and viral replication []. In addition, SART3 is required for U6 snRNP targeting to Cajal bodies []. It binds specifically and directly to the U6 snRNA, interacts transiently with the U6 and U4/U6 snRNPs, and promotes the reassembly of U4/U6 snRNPs after splicing in vitro [].SART3 contains an N-terminal HAT (half-a-tetratricopeptide repeat)-rich domain, a nuclearlocalization signal (NLS) domain, and two C-terminal RNA recognition motifs (RRMs).
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Protein Domain
IPR034218 | SART3_RRM2
Type: Domain
Description: This entry represents the RNA recognition motif 2 (RRM2) of SART3 (also known as Tip110), which is an RNA-binding protein expressed in the nucleus of the majority of proliferating cells, including normal cells and malignant cells, but not in normal tissues except for the testes and fetal liver []. It is involved in the regulation of mRNA splicing probably via its complex formation with RNPS1 (an RNA-binding protein with a serine-rich domain), a pre-mRNA-splicing factor []. SART3 has also been identified as a nuclear Tat-interacting protein that regulates Tat transactivation activity through direct interaction and functions as an important cellular factor for HIV-1 gene expression and viral replication []. In addition, SART3 is required for U6 snRNP targeting to Cajal bodies []. It binds specifically and directly to the U6 snRNA, interacts transiently with the U6 and U4/U6 snRNPs, and promotes the reassembly of U4/U6 snRNPs after splicing in vitro [].SART3 contains a HAT (N-terminal half-a-tetratricopeptide repeat)-rich domain, a nuclearlocalization signal (NLS) domain, and two C-terminal RNA recognition motifs (RRMs).
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Protein Domain
IPR011888 | Anaer_DMSO_reductase
Type: Family
Description: Many bacterial species are capable of anaerobic growth by using dimethylsulphoxide (DMSO) as the terminal electron acceptor, with DMSO reductase as the terminal elctron transfer enzyme. In Escherichia coli and many other Gram-negative bacteria DMSO reductase is a membrane-bound enzyme composed of three subunits; a catalytic molybdenum-containing subunit (DmsA), an electron transfer subunit containing a [4Fe-4S]cluster (DmsB), and a hydrophobic membrane-spanning anchor subunit which attaches the enzyme to the cytoplasmic membrane (DmsC) [, ]. It is generally thought now that DmsAB faces the periplasm, contradicting previous results suggesting a cytoplasmic location. The N-terminal region of DmsA contains a "twin-arginine"signal sequence, suggesting export to the periplasm occurs via the TAT secretion pathway.This entry represents known and predicted bacterial DmsA polypeptides. Several species contain one or more paralogs of DmsA. In E. coli, the two paralogs of DmsA, YnfE and YnfF, are encoded within the ynfEFGHI operon []. YnfE and YnfF cannot form a functional complex with DmsBC, but YnfFGH can restore growth on DMSO when DmABC is deleted. The function of YnfE is not known and it appears to prevent formation of the YnfFGH complex if present.
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Publication
7914432 | J:19784
First Author: Tomomura M
Year: 1994
Journal: Biochim Biophys Acta
Title: Abnormal gene expression and regulation in the liver of jvs mice with systemic carnitine deficiency.
Volume: 1226
Issue: 3
Pages: 307-14
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Publication
11013122 | J:127812
First Author: Karliner JS
Year: 2000
Journal: J Mol Cell Cardiol
Title: Neonatal mouse cardiac myocytes exhibit cardioprotection induced by hypoxic and pharmacologic preconditioning and by transgenic overexpression of human Cu/Zn superoxide dismutase.
Volume: 32
Issue: 10
Pages: 1779-86
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Publication
21527739 | J:185690
First Author: Smeele KM
Year: 2011
Journal: Circ Res
Title: Disruption of hexokinase II-mitochondrial binding blocks ischemic preconditioning and causes rapid cardiac necrosis.
Volume: 108
Issue: 10
Pages: 1165-9
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Publication
36361598 | J:331443
 
First Author: Raïch I
Year: 2022
Journal: Int J Mol Sci
Title: Antagonization of OX(1) Receptor Potentiates CB(2) Receptor Function in Microglia from APP(Sw/Ind) Mice Model.
Volume: 23
Issue: 21
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Publication
11526494 | J:71109
First Author: Yang HW
Year: 2001
Journal: Oncogene
Title: Genomic structure and mutational analysis of the human KIF1B gene which is homozygously deleted in neuroblastoma at chromosome 1p36.2.
Volume: 20
Issue: 36
Pages: 5075-83
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Publication
19366212 | J:152210
First Author: Lothrop AP
Year: 2009
Journal: Biochemistry
Title: No selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue.
Volume: 48
Issue: 26
Pages: 6213-23
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Publication
26721320 | J:259407
 
First Author: Cimini S
Year: 2016
Journal: Neurobiol Dis
Title: The cell-permeable Aβ1-6A2VTAT(D) peptide reverts synaptopathy induced by Aβ1-42wt.
Volume: 89
Pages: 101-11
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Publication
35216197 | J:321514
 
First Author: Brocca-Cofano E
Year: 2022
Journal: Int J Mol Sci
Title: Kaposi's Sarcoma Lesion Progression in BKV-Tat Transgenic Mice Is Increased by Inflammatory Cytokines and Blocked by Treatment with Anti-Tat Antibodies.
Volume: 23
Issue: 4
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Protein
O35047
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
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Protein
C4PFH5
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
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Publication
11477570 | -
First Author: Harada K
Year: 2001
Journal: Int J Cancer
Title: Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation.
Volume: 93
Issue: 5
Pages: 623-8
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Publication
31727625 | J:282775
 
First Author: Puri RV
Year: 2019
Journal: Dis Model Mech
Title: Notch4 activation aggravates NF-κB-mediated inflammation in HIV-1-associated nephropathy.
Volume: 12
Issue: 12
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Protein
P42669
Organism: Mus musculus/domesticus
Length: 321  
Fragment?: false
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Protein
Q8C6E9
Organism: Mus musculus/domesticus
Length: 321  
Fragment?: false
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Publication
12894583 | -
First Author: Johnson EM
Year: 2003
Journal: Anticancer Res
Title: The Pur protein family: clues to function from recent studies on cancer and AIDS.
Volume: 23
Issue: 3A
Pages: 2093-100
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Publication
9917067 | -
First Author: Cavaillé J
Year: 1999
Journal: RNA
Title: The yeast Saccharomyces cerevisiae YDL112w ORF encodes the putative 2'-O-ribose methyltransferase catalyzing the formation of Gm18 in tRNAs.
Volume: 5
Issue: 1
Pages: 66-81
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Publication
34215855 | -
First Author: Reyes-Umana V
Year: 2022
Journal: ISME J
Title: Genetic and phylogenetic analysis of dissimilatory iodate-reducing bacteria identifies potential niches across the world's oceans.
Volume: 16
Issue: 1
Pages: 38-49
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Publication
12519726 | -
First Author: Zambonelli C
Year: 2003
Journal: J Biol Chem
Title: An iron-dependent bacterial phospholipase D reminiscent of purple acid phosphatases.
Volume: 278
Issue: 16
Pages: 13706-11
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Publication
10574912 | -
First Author: Fu TJ
Year: 1999
Journal: J Biol Chem
Title: Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription.
Volume: 274
Issue: 49
Pages: 34527-30
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Protein Coding Gene
MGP_CAROLIEiJ_G0022439 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_CAROLIEiJ_G0027968 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0024596 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_129S1SvImJ_G0030319 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0024563 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0030288 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0024534 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0030220 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0024561 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0030305 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0024330 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0030016 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1926953 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_87904 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0025008 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0030750 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0023803 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0029421 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0024300 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0029986 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0024430 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0030136 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0024396 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0030091 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0024514 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0030222 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0024426 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0030122 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0025057 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0030790 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0023548 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0029136 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0023865 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0029495 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0019167 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_PahariEiJ_G0024540 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0023354 | -
Type: protein_coding_gene
Organism: Mus spretus
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Protein Coding Gene
MGP_SPRETEiJ_G0028972 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
3754329 | J:8248
First Author: Tokunaga K
Year: 1986
Journal: Nucleic Acids Res
Title: Nucleotide sequence of a full-length cDNA for mouse cytoskeletal beta-actin mRNA.
Volume: 14
Issue: 6
Pages: 2829
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Publication
3182774 | J:9445
First Author: Sadano H
Year: 1988
Journal: J Biol Chem
Title: cDNA cloning and sequence of a new type of actin in mouse B16 melanoma.
Volume: 263
Issue: 31
Pages: 15868-71
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Publication
33408128 | J:320982
 
First Author: Qiao F
Year: 2021
Journal: Biol Open
Title: Ctdp1 deficiency leads to early embryonic lethality in mice and defects in cell cycle progression in MEFs.
Volume: 10
Issue: 1
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Publication
17987666 | J:129105
First Author: Jägle U
Year: 2007
Journal: Genesis
Title: Conditional transgene expression mediated by the mouse beta-actin locus.
Volume: 45
Issue: 11
Pages: 659-66
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Publication
9608737 | J:46634
First Author: Shawlot W
Year: 1998
Journal: Transgenic Res
Title: Restricted beta-galactosidase expression of a hygromycin-lacZ gene targeted to the beta-actin locus and embryonic lethality of beta-actin mutant mice.
Volume: 7
Issue: 2
Pages: 95-103
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Publication
9635195 | J:67904
First Author: Zinyk DL
Year: 1998
Journal: Curr Biol
Title: Fate mapping of the mouse midbrain-hindbrain constriction using a site-specific recombination system.
Volume: 8
Issue: 11
Pages: 665-8
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Publication
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