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Search results 1401 to 1500 out of 1501 for Tnfrsf1a

0.046s
Type Details Score
Allele
Name: tumor necrosis factor receptor superfamily, member 1a; endonuclease-mediated mutation 4, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
Allele
Name: tumor necrosis factor receptor superfamily, member 1a; targeted mutation 1, Immunex Research and Development Corporation
Allele Type: Targeted
Attribute String: Null/knockout
Allele
Name: tumor necrosis factor receptor superfamily, member 1a; targeted mutation 1, Richard M Siegel
Allele Type: Targeted
Attribute String: Humanized sequence
Allele
Name: tumor necrosis factor receptor superfamily, member 1a; targeted mutation 2.1, Richard M Siegel
Allele Type: Targeted
Attribute String: Humanized sequence
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a
Background: involves: 129S7/SvEvBrd * C57BL/6
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a<+>
Background: B6.Cg-Tnfrsf1a
Zygosity: ht
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a<+>
Background: B6.Cg-Tnfrsf1a
Zygosity: ht
Has Mutant Allele: true
DO Term
Allele
Name: tumor necrosis factor receptor superfamily, member 1a; endonuclease-mediated mutation 2, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Allele
Name: tumor necrosis factor receptor superfamily, member 1b; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Publication
First Author: Efimova EV
Year: 2004
Journal: Oncogene
Title: IG20, in contrast to DENN-SV, (MADD splice variants) suppresses tumor cell survival, and enhances their susceptibility to apoptosis and cancer drugs.
Volume: 23
Issue: 5
Pages: 1076-87
Publication
First Author: Schievella AR
Year: 1997
Journal: J Biol Chem
Title: MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase.
Volume: 272
Issue: 18
Pages: 12069-75
Publication
First Author: Iwasaki K
Year: 1997
Journal: Neuron
Title: aex-3 encodes a novel regulator of presynaptic activity in C. elegans.
Volume: 18
Issue: 4
Pages: 613-22
Protein Domain
Type: Family
Description: MAP kinase-activating death domain protein (MADD) regulates cell proliferation, survival and death through alternative mRNA splicing. Different isoforms have different effects: isoform 5 increases cell proliferation whereas isoform 2 decreases it; isoform 1 is susceptible to inducing apoptosis, isoform 5 is resistant []. MADD activates RAB3A, RAB3C and RAB3D by converting them from GDP-bound inactive forms to GTP-bound active forms []. MADD is a component of the TNFRSF1A signaling complex, linking the type 1 tumor necrosis factor receptor TNFRSF1A with MAP kinase activation []. MADD contains a tripartite DENN domain. In the nematode Caenorhabditis elegans, MADD is also known as regulator of presynaptic activity aex-3 [].
Publication
First Author: Cabal-Hierro L
Year: 2012
Journal: Cell Signal
Title: Signal transduction by tumor necrosis factor receptors.
Volume: 24
Issue: 6
Pages: 1297-305
Publication
First Author: Rittore C
Year: 2014
Journal: Ann Rheum Dis
Title: Identification of a new exon 2-skipped TNFR1 transcript: regulation by three functional polymorphisms of the TNFR-associated periodic syndrome (TRAPS) gene.
Volume: 73
Issue: 1
Pages: 290-7
Publication
First Author: Diniz BS
Year: 2010
Journal: J Alzheimers Dis
Title: Higher serum sTNFR1 level predicts conversion from mild cognitive impairment to Alzheimer's disease.
Volume: 22
Issue: 4
Pages: 1305-11
Publication
First Author: Hope S
Year: 2013
Journal: Schizophr Res
Title: Interleukin 1 receptor antagonist and soluble tumor necrosis factor receptor 1 are associated with general severity and psychotic symptoms in schizophrenia and bipolar disorder.
Volume: 145
Issue: 1-3
Pages: 36-42
Publication
First Author: Espín R
Year: 2013
Journal: Dis Model Mech
Title: TNF receptors regulate vascular homeostasis in zebrafish through a caspase-8, caspase-2 and P53 apoptotic program that bypasses caspase-3.
Volume: 6
Issue: 2
Pages: 383-96
Publication
First Author: Maier O
Year: 2013
Journal: Biochem Biophys Res Commun
Title: TNF receptor 2 protects oligodendrocyte progenitor cells against oxidative stress.
Volume: 440
Issue: 2
Pages: 336-41
Publication
First Author: Hu X
Year: 2014
Journal: J Immunol
Title: Transmembrane TNF-α promotes suppressive activities of myeloid-derived suppressor cells via TNFR2.
Volume: 192
Issue: 3
Pages: 1320-31
Publication
First Author: Tartaglia LA
Year: 1993
Journal: J Biol Chem
Title: Ligand passing: the 75-kDa tumor necrosis factor (TNF) receptor recruits TNF for signaling by the 55-kDa TNF receptor.
Volume: 268
Issue: 25
Pages: 18542-8
Publication
First Author: Speeckaert MM
Year: 2012
Journal: Am J Nephrol
Title: Tumor necrosis factor receptors: biology and therapeutic potential in kidney diseases.
Volume: 36
Issue: 3
Pages: 261-70
Protein Domain
Type: Domain
Description: This subfamily of tumor necrosis factor receptor 1A (TNFRSF1, also known as type I TNFR, TNFR1, DR1, TNFRSF1A, CD120a, p55) is found in teleosts. It binds TNF-alpha, through the death domain (DD), and activates NF-kappaB, mediates apoptosis and activates signaling pathways controlling inflammatory, immune, and stress responses. It mediates signal transduction by interacting with antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRAF2 and TRADD that play regulatory roles [, ].Knockout studies in zebrafish embryos have shown that a signaling balance between TNFRSF1A and TNFRSF1B is required for endothelial cell integrity. TNFRSF1A signals apoptosis through caspase-8, whereas TNFRSF1B signals survival via NF-kappaB in endothelial cells. Thus, this apoptotic pathway seems to be evolutionarily conserved, as TNFalpha promotes apoptosis of human endothelial cells and triggers caspase-2 and P53 activation in these cells via TNFRSF1A [].This entry represents the N-terminal domain of TNFR1A from teleosts. TNF-receptors are modular proteins. The N-terminal extracellular part contains a cysteine-rich region responsible for ligand-binding. This region is composed of small modules of about 40 residues containing 6 conserved cysteines; the number and type of modules can vary in different members of the family [, , ].
Protein Domain
Type: Domain
Description: Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B, also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1) []. It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells []. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes []. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation []. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism) [].This entry represents the N-terminal domain of TNFR1B. TNF-receptors are modular proteins. The N-terminal extracellular part contains a cysteine-rich region responsible for ligand-binding. This region is composed of small modules of about 40 residues containing 6 conserved cysteines; the number and type of modules can vary in different members of the family [, , ].
Protein Domain
Type: Domain
Description: Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A, also known as type I TNFR, TNFR1, DR1, CD120a, p55) binds TNF-alpha, through the death domain (DD), and activates NF-kappaB, mediates apoptosis and activates signaling pathways controlling inflammatory, immune, and stress responses. It mediates signal transduction by interacting with antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRAF2 and TRADD that play regulatory roles [, ].The human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS), or periodic fever syndrome, is associated with germline mutations of the extracellular domains of this receptor, possibly due to impaired receptor clearance []. TNFRSF1A polymorphisms rs1800693 and rs4149584 are associated with elevated risk of multiple sclerosis []. Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder, and high levels are also associated with cognitive impairment and dementia [, ]. Patients with idiopathic recurrent acute pericarditis (IRAP), presumed to be an autoimmune process, have also been shown to carry rare mutations (R104Q and D12E) in the TNFRSF1A gene [].This entry represents the N-terminal domain of TNFR1A. TNF-receptors are modular proteins. The N-terminal extracellular part contains a cysteine-rich region responsible for ligand-binding. This region is composed of small modules of about 40 residues containing 6 conserved cysteines; the number and type of modules can vary in different members of the family [, , ].
Publication
First Author: Chen G
Year: 2002
Journal: Science
Title: TNF-R1 signaling: a beautiful pathway.
Volume: 296
Issue: 5573
Pages: 1634-5
Publication
First Author: Ponnuraj EM
Year: 2002
Journal: Clin Exp Immunol
Title: Requirement for TNF-Tnfrsf1 signalling for sclerosing cholangitis in mice chronically infected by Cryptosporidium parvum.
Volume: 128
Issue: 3
Pages: 416-20
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Genotype
Symbol: Tnfaip8l1/Tnfaip8l1 Tnfrsf1a/Tnfrsf1a Tnfrsf1b/Tnfrsf1b
Background: C57BL/6-Tnfrsf1b Tnfrsf1a Tnfaip8l1
Zygosity: cx
Has Mutant Allele: true
Publication
First Author: Chui YL
Year: 2010
Journal: Biochem Biophys Res Commun
Title: BRE over-expression promotes growth of hepatocellular carcinoma.
Volume: 391
Issue: 3
Pages: 1522-5
Publication
First Author: Pfeuffer T
Year: 2000
Journal: Cell Microbiol
Title: LaXp180, a mammalian ActA-binding protein, identified with the yeast two-hybrid system, co-localizes with intracellular Listeria monocytogenes.
Volume: 2
Issue: 2
Pages: 101-14
Publication
First Author: Kwon HJ
Year: 2004
Journal: Mol Cell Biol
Title: Tumor necrosis factor alpha induction of NF-kappaB requires the novel coactivator SIMPL.
Volume: 24
Issue: 21
Pages: 9317-26
Publication
First Author: Nakamura M
Year: 2009
Journal: Br J Dermatol
Title: A novel missense mutation in tumour necrosis factor receptor superfamily 1A (TNFRSF1A) gene found in tumour necrosis factor receptor-associated periodic syndrome (TRAPS) manifesting adult-onset Still disease-like skin eruptions: report of a case and review of the Japanese patients.
Volume: 161
Issue: 4
Pages: 968-70
Publication
First Author: Rezaei N
Year: 2006
Journal: Clin Rheumatol
Title: TNF-receptor-associated periodic syndrome (TRAPS): an autosomal dominant multisystem disorder.
Volume: 25
Issue: 6
Pages: 773-7
Protein Domain
Type: Domain
Description: This entry represents the death domain (DD) found in tumor necrosis factor receptor-1 (TNFR-1). TNFR-1 has many names including TNFRSF1A, CD120a, p55, p60, and TNFR60. It activates two major intracellular signaling pathways that lead to the activation of the transcription factor NF-kB and the induction of cell death. Upon binding of its ligand TNF, TNFR-1 trimerizes which leads to the recruitment of an adaptor protein named TNFR-associated death domain protein (TRADD) through a DD/DD interaction []. Mutations in the TNFRSF1A gene causes TNFR-associated periodic syndrome (TRAPS), a rare disorder characterized recurrent fever, myalgia, abdominal pain, conjunctivitis and skin eruptions [, ].DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes [, ].
Protein Domain
Type: Family
Description: This entry represents a family of proteins from bacteria, archaea and animals, including Interleukin-1 receptor-associated kinase 1-binding protein 1 from mouse, which has been named SIMPL (signalling molecule that associates with mouse pelle-like kinase). SIMPL is a component of the IRAK1-dependent TNFRSF1A signaling pathway that leads to NF-kappa-B activation and is required for cell survival. It functions by enhancing RelA transcriptional activity [, ]. Separate experiments demonstrate that a mouse family member (named LaXp180) binds the Listeria monocytogenes surface protein ActA, which is a virulence factor that induces actin polymerisation. It may also bind stathmin, a protein involved in signal transduction and in the regulation of microtubule dynamics []. In bacteria its function is unknown, but it is thought to be located in the periplasm or outer membrane.
Publication  
First Author: Shi G
Year: 2023
Journal: Cancers (Basel)
Title: TNFR1 and TNFR2, Which Link NF-κB Activation, Drive Lung Cancer Progression, Cell Dedifferentiation, and Metastasis.
Volume: 15
Issue: 17
Protein
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 459  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
Allele
Name: tumor necrosis factor receptor superfamily, member 1a; targeted mutation 1, Horst Bluethmann
Allele Type: Targeted
Attribute String: Null/knockout
Publication
First Author: Vig E
Year: 2001
Journal: J Biol Chem
Title: SIMPL is a tumor necrosis factor-specific regulator of nuclear factor-kappaB activity.
Volume: 276
Issue: 11
Pages: 7859-66
Protein
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: false
Publication
First Author: Graham SC
Year: 2007
Journal: J Mol Biol
Title: Structure of CrmE, a virus-encoded tumour necrosis factor receptor.
Volume: 372
Issue: 3
Pages: 660-71
Publication
First Author: Sedger LM
Year: 2006
Journal: J Virol
Title: Poxvirus tumor necrosis factor receptor (TNFR)-like T2 proteins contain a conserved preligand assembly domain that inhibits cellular TNFR1-induced cell death.
Volume: 80
Issue: 18
Pages: 9300-9
Publication
First Author: Hu FQ
Year: 1994
Journal: Virology
Title: Cowpox virus contains two copies of an early gene encoding a soluble secreted form of the type II TNF receptor.
Volume: 204
Issue: 1
Pages: 343-56
Publication
First Author: Xu X
Year: 2000
Journal: Virus Genes
Title: Myxoma virus expresses a TNF receptor homolog with two distinct functions.
Volume: 21
Issue: 1-2
Pages: 97-109
Protein Domain
Type: Domain
Description: Viral TNFR homologues include vaccinia virus (VACV) cytokine response modifier E (CrmE) [], an encoded TNFR that shares significant sequence similarity with mammalian type 2 TNF receptors (TNFSFR1B, p75, TNFR type 2) [], a cowpox virus encoded cytokine-response modifier B (CrmB) [], which is a secreted form of TNF receptor that can contribute to the modification of TNF-mediated antiviral processes, and a myxoma virus (MYXV) T2 (M-T2) protein that binds and inhibits rabbit TNF-alpha []. The CrmE structure confirms that the canonical TNFR fold is adopted, but only one of the two "ligand-binding"loops of TNFRSF1A is conserved, suggesting a mechanism for the higher affinity of poxvirusTNFRs for TNFalpha over lymphotoxin-alpha []. CrmB protein specifically binds TNF-alpha and TNF-beta indicating that cowpox virus seeks to invade antiviral processes mediated by TNF. Intracellular M-T2 blocks virus-induced lymphocyte apoptosis via a highly conserved viral preligand assembly domain (vPLAD), which controls receptor signaling competency prior to ligand binding [].This entry represents the N-terminal domain of viral TNFRs. TNF-receptors are modular proteins. The N-terminal extracellular part contains a cysteine-rich region responsible for ligand-binding. This region is composed of small modules of about 40 residues containing 6 conserved cysteines; the number and type of modules can vary in different members of the family [, , ].
Protein
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
Strain
Attribute String: targeted mutation, mutant strain, congenic
Strain
Attribute String: mutant strain, congenic, targeted mutation
Strain
Attribute String: congenic, mutant strain, targeted mutation, transgenic
Strain
Attribute String: mutant stock, targeted mutation, transgenic
Strain
Attribute String: transgenic, targeted mutation, mutant stock
Strain
Attribute String: targeted mutation, mutant strain, congenic
Strain
Attribute String: congenic, mutant strain, targeted mutation
Strain
Attribute String: mutant stock, transgenic, targeted mutation
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a
Background: involves: 129P2/OlaHsd * C57BL/6
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Tnf/Tnf Tnfrsf1a/Tnfrsf1a
Background: involves: 129P2/OlaHsd * 129S/SvEv * C57BL/6
Zygosity: cx
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a
Background: C.129P2-Tnfrsf1a
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a
Background: B6.129P2-Tnfrsf1a
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a Tg(Cr2-cre)3Cgn/?
Background: involves: 129P2/OlaHsd * 129S/SvEv
Zygosity: cn
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a
Background: involves: 129/Sv * 129P2/OlaHsd * C57BL/6
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Tg(Gfap-TNF*)K21Gkl/? Tnfrsf1a/Tnfrsf1a<+>
Background: involves: 129P2/OlaHsd * C57BL/6 * CBA
Zygosity: cx
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a Tnfrsf1b/Tnfrsf1b
Background: involves: 129P2/OlaHsd * 129S2/SvPas * C57BL/6
Zygosity: cx
Has Mutant Allele: true
Genotype
Symbol: Ifng/Ifng Tnfrsf1a/Tnfrsf1a Tnfrsf1b/Tnfrsf1b
Background: involves: 129P2/OlaHsd * 129S2/SvPas * 129S7/SvEvBrd * C57BL/6
Zygosity: cx
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a<+>
Background: involves: 129P2/OlaHsd
Zygosity: ht
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a
Background: involves: 129P2/OlaHsd
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a Tnfrsf1b/Tnfrsf1b
Background: involves: 129P2/OlaHsd * 129S2/SvPas * C57BL/6NTac
Zygosity: cx
Has Mutant Allele: true
Genotype
Symbol: Tnfrsf1a/Tnfrsf1a Tnfrsf1b/Tnfrsf1b Zfp36/Zfp36
Background: involves: 129P2/OlaHsd * 129S2/SvPas * C57BL/6NTac
Zygosity: cx
Has Mutant Allele: true
Strain
Attribute String: congenic, mutant strain, spontaneous mutation, targeted mutation
Protein
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 440  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 440  
Fragment?: true
Publication
First Author: Yoshimura S
Year: 2010
Journal: J Cell Biol
Title: Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors.
Volume: 191
Issue: 2
Pages: 367-81
Protein
Organism: Mus musculus/domesticus
Length: 1577  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1627  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1602  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1574  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1577  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1562  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1632  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1573  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1541  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1558  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1115  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1554  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1593  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1475  
Fragment?: false
Publication
First Author: Naismith JH
Year: 1998
Journal: Trends Biochem Sci
Title: Modularity in the TNF-receptor family.
Volume: 23
Issue: 2
Pages: 74-9
Publication
First Author: Bodmer JL
Year: 2002
Journal: Trends Biochem Sci
Title: The molecular architecture of the TNF superfamily.
Volume: 27
Issue: 1
Pages: 19-26
Publication
First Author: Banner DW
Year: 1993
Journal: Cell
Title: Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation.
Volume: 73
Issue: 3
Pages: 431-45
Publication
First Author: Feinstein E
Year: 1995
Journal: Trends Biochem Sci
Title: The death domain: a module shared by proteins with diverse cellular functions.
Volume: 20
Issue: 9
Pages: 342-4
Publication  
First Author: Park HH
Year: 2007
Journal: Annu Rev Immunol
Title: The death domain superfamily in intracellular signaling of apoptosis and inflammation.
Volume: 25
Pages: 561-86