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Search results 501 to 600 out of 653 for Adam10

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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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UniProt Feature
UniProt Feature
Begin: 354
Description: Cleavage; by ADAM10 and ADAM17
Type: site
End: 355
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Publication
28739265 | J:251834
First Author: Dempsey PJ
Year: 2017
Journal: Biochim Biophys Acta
Title: Role of ADAM10 in intestinal crypt homeostasis and tumorigenesis.
Volume: 1864
Issue: 11 Pt B
Pages: 2228-2239
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Publication
17072319 | J:116139
First Author: Weskamp G
Year: 2006
Journal: Nat Immunol
Title: ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23.
Volume: 7
Issue: 12
Pages: 1293-8
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Publication
24055016 | J:201818
First Author: Suh J
Year: 2013
Journal: Neuron
Title: ADAM10 missense mutations potentiate β-amyloid accumulation by impairing prodomain chaperone function.
Volume: 80
Issue: 2
Pages: 385-401
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Publication
23624141 | J:214201
 
First Author: Kitaoka K
Year: 2013
Journal: Neuropharmacology
Title: The retinoic acid receptor agonist Am80 increases hippocampal ADAM10 in aged SAMP8 mice.
Volume: 72
Pages: 58-65
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Interaction Experiment
Marcello E (2007)
Description: Synapse-associated protein-97 mediates alpha-secretase ADAM10 trafficking and promotes its activity.
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Publication
21368228 | J:170818
First Author: Gibb DR
Year: 2011
Journal: J Immunol
Title: ADAM10 overexpression shifts lympho- and myelopoiesis by dysregulating site 2/site 3 cleavage products of Notch.
Volume: 186
Issue: 7
Pages: 4244-52
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Publication
18276079 | J:135294
First Author: Clement AB
Year: 2008
Journal: Neuroscience
Title: Effects of neuron-specific ADAM10 modulation in an in vivo model of acute excitotoxic stress.
Volume: 152
Issue: 2
Pages: 459-68
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Publication
26961870 | J:234201
First Author: Franke M
Year: 2016
Journal: J Biol Chem
Title: Human and Murine Interleukin 23 Receptors Are Novel Substrates for A Disintegrin and Metalloproteases ADAM10 and ADAM17.
Volume: 291
Issue: 20
Pages: 10551-61
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Publication
34390512 | J:310377
First Author: Hsia HE
Year: 2021
Journal: FASEB J
Title: Endoglycan (PODXL2) is proteolytically processed by ADAM10 (a disintegrin and metalloprotease 10) and controls neurite branching in primary neurons.
Volume: 35
Issue: 9
Pages: e21813
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Publication
31632389 | J:297269
 
First Author: Yao Y
Year: 2019
Journal: Front Immunol
Title: Platelet-Derived Exosomal MicroRNA-25-3p Inhibits Coronary Vascular Endothelial Cell Inflammation Through Adam10 via the NF-κB Signaling Pathway in ApoE-/- Mice.
Volume: 10
Pages: 2205
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DO Term
DOID:0110050 | Alzheimer's disease 18
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Interaction Experiment
Cozzolino F (2021)
Description: ADAM10 hyperactivation acts on piccolo to deplete synaptic vesicle stores in Huntingtons disease.
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Publication
17965014 | -
First Author: Martin L
Year: 2008
Journal: J Biol Chem
Title: Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b.
Volume: 283
Issue: 3
Pages: 1644-52
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Allele
Adam10<tm1Smoc> | MGI:7288103
Name: a disintegrin and metallopeptidase domain 10; targeted mutation 1, Shanghai Model Organisms Center
Allele Type: Targeted
Attribute String: Conditional ready, No functional change
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GXD Expression
GXD Expression
Probe: MGI:6690292
Assay Type: Immunohistochemistry
Annotation Date: 2021-04-12
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1697423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:6690294
Age: embryonic day 15.5
Image: 4B
Note: Expression was detected in neurons in the substantia nigra and the ventral tegmental area and co-localized with Adam10 immunostaining.
Specimen Label: 4B
Detected: true
Specimen Num: 1
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GXD Expression
GXD Expression
Probe: MGI:3580797
Assay Type: Immunohistochemistry
Annotation Date: 2005-07-06
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1750328
Pattern: Regionally restricted
Stage: TS28
Assay Id: MGI:3580832
Age: postnatal adult
Image: 5E, 5F
Note: Expression was detected in the cell membrane. Expression overlapped with Adam10 in the cell membranes of the islets of Langerhans.
Specimen Label: 5E, 5F
Detected: true
Specimen Num: 2
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GXD Expression
GXD Expression
Probe: MGI:3580778
Assay Type: Immunohistochemistry
Annotation Date: 2005-07-06
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1706616
Pattern: Regionally restricted
Stage: TS16
Assay Id: MGI:3580821
Age: embryonic day 10.0
Image: 1G, 1J
Note: Expression was detected at the pancreatic anterior-posterior level. Expression overlapped with Adam10 at low or nearly absent levels.
Specimen Label: 1G, 1J
Detected: true
Specimen Num: 2
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Publication
30599067 | -
First Author: Reinhardt S
Year: 2019
Journal: Cell Mol Life Sci
Title: Transcriptional repression of the ectodomain sheddase ADAM10 by TBX2 and potential implication for Alzheimer's disease.
Volume: 76
Issue: 5
Pages: 1005-1025
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Publication
17557115 | -
First Author: Kirkin V
Year: 2007
Journal: Cell Death Differ
Title: The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells.
Volume: 14
Issue: 9
Pages: 1678-87
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Publication
21402705 | -
First Author: Bouillot S
Year: 2011
Journal: J Biol Chem
Title: Protocadherin-12 cleavage is a regulated process mediated by ADAM10 protein: evidence of shedding up-regulation in pre-eclampsia.
Volume: 286
Issue: 17
Pages: 15195-204
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Publication
12714508 | -
First Author: Hundhausen C
Year: 2003
Journal: Blood
Title: The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion.
Volume: 102
Issue: 4
Pages: 1186-95
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Publication
10415747 | -
 
First Author: Killar L
Year: 1999
Journal: Ann N Y Acad Sci
Title: Adamalysins. A family of metzincins including TNF-alpha converting enzyme (TACE).
Volume: 878
Pages: 442-52
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Protein Domain
IPR034025 | ADAM10_ADAM17
Type: Domain
Description: This entry includes proteins with reprolysin-like metallopeptidase domains and includes ADAM10 (also known as myelin-associated metalloendopeptidase, MEROPS identifier M12.210), ADAM17 (also known as tumour necrosis factor alpha-convertase, MEROPS identifier M12.217), kuzbanian (MEROPS identifiers M12.211 and M12.322) and ADM-4 (MEROPS identifier M12.329) [].
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Protein
B3SRB2
Organism: Mus musculus/domesticus
Length: 49  
Fragment?: true
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Publication
12475894 | -
First Author: Gutwein P
Year: 2003
Journal: FASEB J
Title: ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles.
Volume: 17
Issue: 2
Pages: 292-4
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Protein Domain
IPR027053 | ADAM_10
Type: Family
Description: Disintegrin and metalloproteinase domain-containing protein 10 (also known as ADAM10 or Kuzbanian; MEROPS identifier M12.210) is an endopeptidase () []. In humans and mice, it cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. It is responsible for the proteolytic release of several other cell-surface proteins. It controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis []. The Drosophila orthologue is classified separately in the MEROPS database as M12.211.
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Protein
D3Z1E6
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
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Publication
18429929 | -
First Author: Kitt KN
Year: 2008
Journal: Traffic
Title: Rab14 regulates apical targeting in polarized epithelial cells.
Volume: 9
Issue: 7
Pages: 1218-31
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Publication
24694596 | -
First Author: Lu R
Year: 2014
Journal: Mol Biol Cell
Title: Rab14 regulation of claudin-2 trafficking modulates epithelial permeability and lumen morphogenesis.
Volume: 25
Issue: 11
Pages: 1744-54
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Publication
25644001 | J:229649
First Author: Okai B
Year: 2015
Journal: Infect Immun
Title: Rab14 regulates maturation of macrophage phagosomes containing the fungal pathogen Candida albicans and outcome of the host-pathogen interaction.
Volume: 83
Issue: 4
Pages: 1523-35
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Publication
24119134 | -
First Author: Garg A
Year: 2014
Journal: Cell Microbiol
Title: Drosophila Rab14 mediates phagocytosis in the immune response to Staphylococcus aureus.
Volume: 16
Issue: 2
Pages: 296-310
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Publication
22595666 | -
First Author: Prekeris R
Year: 2012
Journal: Dev Cell
Title: The art of "cut and run": the role of Rab14 GTPase in regulating N-cadherin shedding and cell motility.
Volume: 22
Issue: 5
Pages: 909-10
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Publication
22569897 | -
First Author: Thi EP
Year: 2012
Journal: J Leukoc Biol
Title: Phosphatidylinositol 3-kinases and their roles in phagosome maturation.
Volume: 92
Issue: 3
Pages: 553-66
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Protein Domain
IPR030702 | Rab14
Type: Family
Description: Ras-related protein Rab14 is a small GTPase that mediates endocytic recycling and functions in phagosome maturation [, ]. Rab14 and its exchange factor FAM116 regulates the specific endocytic transport of ADAM10 and thereby N-cadherin shedding and cell motility [, ]. Rab14 regulates claudin-2 trafficking, which is required for epithelial morphogenesis []. It regulates apical targeting in polarised epithelial cells []. Rab14 also regulates the interaction of phagosomes with early endocytic compartments and the maturation of macrophage phagosomes containing the fungal pathogen Candida albicans []. Drosophila Rab14 mediates phagocytosis in the immune response to Staphylococcus aureus [].
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Publication
22595670 | -
First Author: Linford A
Year: 2012
Journal: Dev Cell
Title: Rab14 and its exchange factor FAM116 link endocytic recycling and adherens junction stability in migrating cells.
Volume: 22
Issue: 5
Pages: 952-66
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Publication
17873332 | -
First Author: Rengaraj D
Year: 2007
Journal: Endocrine
Title: Expression and regulation of type II integral membrane protein family members in mouse male reproductive tissues.
Volume: 31
Issue: 2
Pages: 193-201
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Publication
19747390 | -
 
First Author: Hedlund J
Year: 2009
Journal: BMC Res Notes
Title: BRICHOS - a superfamily of multidomain proteins with diverse functions.
Volume: 2
Pages: 180
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Publication
24099305 | -
First Author: Knight SD
Year: 2013
Journal: Biochemistry
Title: The BRICHOS domain, amyloid fibril formation, and their relationship.
Volume: 52
Issue: 43
Pages: 7523-31
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Publication
24831988 | J:217351
First Author: Tai TS
Year: 2014
Journal: PLoS One
Title: Itm2a, a target gene of GATA-3, plays a minimal role in regulating the development and function of T cells.
Volume: 9
Issue: 5
Pages: e96535
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Publication
25557390 | -
First Author: Baron BW
Year: 2015
Journal: Biochim Biophys Acta
Title: The ITM2B (BRI2) gene is a target of BCL6 repression: Implications for lymphomas and neurodegenerative diseases.
Volume: 1852
Issue: 5
Pages: 742-8
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Publication
16027166 | -
First Author: Fotinopoulou A
Year: 2005
Journal: J Biol Chem
Title: BRI2 interacts with amyloid precursor protein (APP) and regulates amyloid beta (Abeta) production.
Volume: 280
Issue: 35
Pages: 30768-72
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Publication
20036644 | -
First Author: Peng S
Year: 2010
Journal: Biochem Biophys Res Commun
Title: The extracellular domain of Bri2 (ITM2B) binds the ABri peptide (1-23) and amyloid beta-peptide (Abeta1-40): Implications for Bri2 effects on processing of amyloid precursor protein and Abeta aggregation.
Volume: 393
Issue: 3
Pages: 356-61
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Publication
19366692 | -
First Author: Matsuda S
Year: 2009
Journal: J Biol Chem
Title: BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2.
Volume: 284
Issue: 23
Pages: 15815-25
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Protein Domain
IPR040145 | ITM2
Type: Family
Description: The family of type 2 integral membrane protein (ITM2) consists of three members, ITM2A, ITM2B and ITM2C []. Members of this family contain a BRICHOS domain, which possesses chaperone activity [,].ITM2A is a target gene of GATA-3, a T cell-specific transcription factor [].ITM2B is proteolytically cleaved at three locations; cleavage by furin in the C-terminal region generates a 23-residue peptide (ABri23), processing by ADAM10 results in release of the BRICHOS domain from the membrane-bound N-terminal part and intramembrane cleavage by SPPL2a/2b liberates the intracellular domain []. ITM2B (BRI2) is a target of BCL6 transcriptional repression and a short form of the ITM2B protein, similarly to other targets of BCL6, induces apoptosis in hematopoietic cell lines []. ITM2B interacts with amyloid precursor protein (APP) and regulates amyloid beta (Abeta) production [, ]. ITM2C (BRI3) also inhibits amyloid precursor protein processing, but through a different mechanism to ITM2B [].
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Publication
23427141 | J:197268
First Author: Kaushal GP
Year: 2013
Journal: Am J Physiol Renal Physiol
Title: Meprin A metalloproteinase and its role in acute kidney injury.
Volume: 304
Issue: 9
Pages: F1150-8
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Publication
21693781 | -
First Author: Becker-Pauly C
Year: 2011
Journal: Mol Cell Proteomics
Title: Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates.
Volume: 10
Issue: 9
Pages: M111.009233
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Publication
25150980 | J:219383
First Author: Shimoda M
Year: 2014
Journal: Nat Cell Biol
Title: Loss of the Timp gene family is sufficient for the acquisition of the CAF-like cell state.
Volume: 16
Issue: 9
Pages: 889-901
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Publication
24907271 | J:216006
First Author: He W
Year: 2014
Journal: J Biol Chem
Title: β-site amyloid precursor protein cleaving enzyme 1(BACE1) regulates Notch signaling by controlling the cleavage of Jagged 1 (Jag1) and Jagged 2 (Jag2) proteins.
Volume: 289
Issue: 30
Pages: 20630-7
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Publication
31076514 | J:277779
 
First Author: Schäffler H
Year: 2019
Journal: J Cell Sci
Title: The cancer-associated meprin β variant G32R provides an additional activation site and promotes cancer cell invasion.
Volume: 132
Issue: 11
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Publication
18355449 | J:134154
First Author: Galichet A
Year: 2008
Journal: Biochem Biophys Res Commun
Title: Calcium-regulated intramembrane proteolysis of the RAGE receptor.
Volume: 370
Issue: 1
Pages: 1-5
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Publication
31308530 | J:281638
First Author: Esteve P
Year: 2019
Journal: Nat Neurosci
Title: Elevated levels of Secreted-Frizzled-Related-Protein 1 contribute to Alzheimer's disease pathogenesis.
Volume: 22
Issue: 8
Pages: 1258-1268
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Publication
17018528 | J:117665
First Author: Hikita A
Year: 2006
Journal: J Biol Chem
Title: Negative regulation of osteoclastogenesis by ectodomain shedding of receptor activator of NF-kappaB ligand.
Volume: 281
Issue: 48
Pages: 36846-55
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Publication
35984475 | J:330857
 
First Author: Mishra R
Year: 2022
Journal: J Exp Med
Title: Augmenting neurogenesis rescues memory impairments in Alzheimer's disease by restoring the memory-storing neurons.
Volume: 219
Issue: 9
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Publication
30819724 | J:275231
First Author: Mentrup T
Year: 2019
Journal: J Exp Med
Title: Atherogenic LOX-1 signaling is controlled by SPPL2-mediated intramembrane proteolysis.
Volume: 216
Issue: 4
Pages: 807-830
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Publication
20655472 | J:163978
First Author: Donmez G
Year: 2010
Journal: Cell
Title: SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10.
Volume: 142
Issue: 2
Pages: 320-32
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Publication
24338630 | J:211857
First Author: Morales JK
Year: 2014
Journal: J Leukoc Biol
Title: Myeloid-derived suppressor cells enhance IgE-mediated mast cell responses.
Volume: 95
Issue: 4
Pages: 643-50
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Publication
28084316 | J:244044
 
First Author: Hurst LA
Year: 2017
Journal: Nat Commun
Title: TNFα drives pulmonary arterial hypertension by suppressing the BMP type-II receptor and altering NOTCH signalling.
Volume: 8
Pages: 14079
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Protein
Q91VK4
Organism: Mus musculus/domesticus
Length: 269  
Fragment?: false
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Protein
Q61500
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
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Protein
O89051
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
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Protein
Q3TVJ0
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
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Protein
Q9JME4
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
Q9D1Q3
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
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Protein
A0A087WRM2
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
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Protein
A0A2I3BPW7
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
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Protein
Q3U0F3
Organism: Mus musculus/domesticus
Length: 269  
Fragment?: false
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Protein
Q3UCT9
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
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Protein Domain
IPR034301 | Meprin_alpha
Type: Family
Description: This entry includes the alpha subunit of meprin (MEROPS identifier M12.002).Meprins are metazoan zinc metallopeptidases belonging to MEROPS peptidase family M12 (clan MA(M)), subfamily M12A (astacin family). They are complex and structurally unique homo- or heterotetrameric glycoproteins composed of evolutionarily related alpha and/or beta subunits that contain disulphide-bridged dimers. The two subunits are differentially expressed and processed to yield latent and active proteases as well as membrane-associated and secreted forms. They are excellent models of homo- and hetero-oligomeric enzymes that are regulated at the transcriptional and post translational levels []. Each chain contains an astacin domain, MAM, MATH, and AM (after MATH) domains [], and an EGF-like domain.The astacin domain is a Zn-metalloprotease domain characterised by a unique 18-amino acid signature sequence, HEXXHXXGFXHEXXRXDR [], which begins with the zinc binding motif HEXXH. The MAM domain is necessary for correct folding and transport through the secretory pathway. The MATH domain is required for folding of an activatable zymogen, and the AM domain is important for activity against proteins and efficient secretion of the protein. Meprin is able to cleave a variety of substrates and has a role in matrix remodeling, inflammation, and cell-cell and cell-matrix processes []. Known substrates include FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10 and tenascin-C [].
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Protein Domain
IPR008294 | Meprin
Type: Family
Description: Meprins are metazoan zinc metallopeptidases belonging to MEROPS peptidase family M12 (clan MA(M)), subfamily M12A (astacin family). They are complex and structurally unique homo- or heterotetrameric glycoproteins composed of evolutionarily related alpha and/or beta subunits that contain disulphide-bridged dimers. The two subunits are differentially expressed and processed to yield latent and active proteases as well as membrane-associated and secreted forms. They are excellent models of homo- and hetero-oligomeric enzymes that are regulated at the transcriptional and post translational levels []. Each chain contains an astacin domain, MAM, MATH, and AM (after MATH) domains [], and an EGF-like domain.The astacin domain is a Zn-metalloprotease domain characterised by a unique 18-amino acid signature sequence, HEXXHXXGFXHEXXRXDR [], which begins with the zinc binding motif HEXXH. The MAM domain is necessary for correct folding and transport through the secretory pathway. The MATH domain is required for folding of an activatable zymogen, and the AM domain is important for activity against proteins and efficient secretion of the protein. Meprin is able to cleave a variety of substrates and has a role in matrix remodeling, inflammation, and cell-cell and cell-matrix processes []. Known substrates include FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10 and tenascin-C [].
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Protein Domain
IPR034302 | Meprin_beta
Type: Family
Description: This entry represents the meprin beta subunit (MEROPS identifier M12.004).Meprins are metazoan zinc metallopeptidases belonging to MEROPS peptidase family M12 (clan MA(M)), subfamily M12A (astacin family). They are complex and structurally unique homo- or heterotetrameric glycoproteins composed of evolutionarily related alpha and/or beta subunits that contain disulphide-bridged dimers. The two subunits are differentially expressed and processed to yield latent and active proteases as well as membrane-associated and secreted forms. They are excellent models of homo- and hetero-oligomeric enzymes that are regulated atthe transcriptional and post translational levels []. Each chain contains an astacin domain, MAM, MATH, and AM (after MATH) domains [], and an EGF-like domain.The astacin domain is a Zn-metalloprotease domain characterised by a unique 18-amino acid signature sequence, HEXXHXXGFXHEXXRXDR [], which begins with the zinc binding motif HEXXH. The MAM domain is necessary for correct folding and transport through the secretory pathway. The MATH domain is required for folding of an activatable zymogen, and the AM domain is important for activity against proteins and efficient secretion of the protein. Meprin is able to cleave a variety of substrates and has a role in matrix remodeling, inflammation, and cell-cell and cell-matrix processes []. Known substrates include FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10 and tenascin-C [].
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Publication
8387703 | -
First Author: Beckmann G
Year: 1993
Journal: Trends Biochem Sci
Title: An adhesive domain detected in functionally diverse receptors.
Volume: 18
Issue: 2
Pages: 40-1
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Publication
9857066 | -
First Author: Tsukuba T
Year: 1998
Journal: J Biol Chem
Title: Role of the COOH-terminal domains of meprin A in folding, secretion, and activity of the metalloendopeptidase.
Volume: 273
Issue: 52
Pages: 35260-7
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Publication
7670368 | -
First Author: Bond JS
Year: 1995
Journal: Protein Sci
Title: The astacin family of metalloendopeptidases.
Volume: 4
Issue: 7
Pages: 1247-61
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Publication
17428795 | J:122772
First Author: Litterst C
Year: 2007
Journal: J Biol Chem
Title: Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor.
Volume: 282
Issue: 22
Pages: 16155-63
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Publication
15215246 | J:93344
First Author: Budagian V
Year: 2004
Journal: J Biol Chem
Title: Natural soluble interleukin-15Ralpha is generated by cleavage that involves the tumor necrosis factor-alpha-converting enzyme (TACE/ADAM17).
Volume: 279
Issue: 39
Pages: 40368-75
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