| Type |
Details |
Score |
| Publication |
| First Author: |
Noh H |
| Year: |
2014 |
| Journal: |
Neuroscience |
| Title: |
Age-dependent effects of valproic acid in Alzheimer's disease (AD) mice are associated with nerve growth factor (NGF) regulation. |
| Volume: |
266 |
|
| Pages: |
255-65 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wang E |
| Year: |
2017 |
| Journal: |
J Alzheimers Dis |
| Title: |
Amylin Treatment Reduces Neuroinflammation and Ameliorates Abnormal Patterns of Gene Expression in the Cerebral Cortex of an Alzheimer's Disease Mouse Model. |
| Volume: |
56 |
| Issue: |
1 |
| Pages: |
47-61 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Han X |
| Year: |
2022 |
| Journal: |
EBioMedicine |
| Title: |
KIBRA regulates amyloid β metabolism by controlling extracellular vesicles secretion. |
| Volume: |
78 |
|
| Pages: |
103980 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jawhar S |
| Year: |
2012 |
| Journal: |
Neurobiol Aging |
| Title: |
Motor deficits, neuron loss, and reduced anxiety coinciding with axonal degeneration and intraneuronal Aβ aggregation in the 5XFAD mouse model of Alzheimer's disease. |
| Volume: |
33 |
| Issue: |
1 |
| Pages: |
196.e29-40 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chen C |
| Year: |
2018 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
The prodrug of 7,8-dihydroxyflavone development and therapeutic efficacy for treating Alzheimer's disease. |
| Volume: |
115 |
| Issue: |
3 |
| Pages: |
578-583 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Butler CA |
| Year: |
2024 |
| Journal: |
Alzheimers Dement |
| Title: |
The Abca7(V1613M) variant reduces Aβ generation, plaque load, and neuronal damage. |
| Volume: |
20 |
| Issue: |
7 |
| Pages: |
4914-4934 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Akber U |
| Year: |
2021 |
| Journal: |
J Neurosci |
| Title: |
Cereblon Regulates the Proteotoxicity of Tau by Tuning the Chaperone Activity of DNAJA1. |
| Volume: |
41 |
| Issue: |
24 |
| Pages: |
5138-5156 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Maron R |
| Year: |
2023 |
| Journal: |
Int J Mol Sci |
| Title: |
Amyloid Precursor Protein and Tau Peptides Linked Together Ameliorate Loss of Cognition in an Alzheimer's Disease Animal Model. |
| Volume: |
24 |
| Issue: |
15 |
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Song Y |
| Year: |
2019 |
| Journal: |
EBioMedicine |
| Title: |
A novel mechanism of synaptic and cognitive impairments mediated via microRNA-30b in Alzheimer's disease. |
| Volume: |
39 |
|
| Pages: |
409-421 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhao N |
| Year: |
2021 |
| Journal: |
Neuropharmacology |
| Title: |
Low molecular weight chondroitin sulfate ameliorates pathological changes in 5XFAD mice by improving various functions in the brain. |
| Volume: |
199 |
|
| Pages: |
108796 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Suzuki K |
| Year: |
2014 |
| Journal: |
J Neuroimaging |
| Title: |
Ligand-based molecular MRI: O-17 JJVCPE amyloid imaging in transgenic mice. |
| Volume: |
24 |
| Issue: |
6 |
| Pages: |
595-598 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Yao Y |
| Year: |
2020 |
| Journal: |
Alzheimers Dement |
| Title: |
Correction of microtubule defects within Aβ plaque-associated dystrophic axons results in lowered Aβ release and plaque deposition. |
| Volume: |
16 |
| Issue: |
10 |
| Pages: |
1345-1357 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ohno M |
| Year: |
2009 |
| Journal: |
Neurobiol Learn Mem |
| Title: |
Failures to reconsolidate memory in a mouse model of Alzheimer's disease. |
| Volume: |
92 |
| Issue: |
3 |
| Pages: |
455-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Maruyama T |
| Year: |
2018 |
| Journal: |
Heliyon |
| Title: |
SENP1 and SENP2 regulate SUMOylation of amyloid precursor protein. |
| Volume: |
4 |
| Issue: |
4 |
| Pages: |
e00601 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Han KM |
| Year: |
2020 |
| Journal: |
Cells |
| Title: |
Regorafenib Regulates AD Pathology, Neuroinflammation, and Dendritic Spinogenesis in Cells and a Mouse Model of AD. |
| Volume: |
9 |
| Issue: |
7 |
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Farid MM |
| Year: |
2020 |
| Journal: |
Sci Rep |
| Title: |
Trigonelline recovers memory function in Alzheimer's disease model mice: evidence of brain penetration and target molecule. |
| Volume: |
10 |
| Issue: |
1 |
| Pages: |
16424 |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(Thy1-APPSwe,Prnp-PSEN2*N141I)152HLaoz/? |
| Background: |
C57BL/6-Tg(Thy1-APPSwe,Prnp-PSEN2*N141I)152HLaoz |
| Zygosity: |
ot |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(Thy1-PSEN1*M146V,-APP*Swe)10Arte/? |
| Background: |
involves: C57BL/6 * CBA |
| Zygosity: |
ot |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(Thy1-APP)28Lpr/? |
| Background: |
B6.Cg-Tg(Thy1-APP)28Lpr |
| Zygosity: |
ot |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion 40, Bruce Lamb |
| Allele Type: |
Transgenic |
| Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Msr1/Msr1 Tg(APPV717F)109Ili/? |
| Background: |
involves: 129X1/SvJ * C57BL/6 * DBA/2 * ICR |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(APPSwLon)96Btla/? |
| Background: |
involves: 129S4/SvJae |
| Zygosity: |
ot |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(APPSwLon)96Btla/Tg(APPSwLon)96Btla |
| Background: |
involves: 129S4/SvJae |
| Zygosity: |
hm |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Apoe/Apoe Clu/Clu Tg(APPV717F)109Ili/Tg(APPV717F)109Ili |
| Background: |
involves: 129P2/OlaHsd * 129S2/SvPas |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Apoe/Apoe Tg(APPV717F)109Ili/Tg(APPV717F)109Ili |
| Background: |
involves: 129P2/OlaHsd |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Psen1/Psen1 Tg(APP)8.9Btla/? |
| Background: |
involves: 129S2/SvPas * C57BL/6J |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Um JH |
| Year: |
2024 |
| Journal: |
Theranostics |
| Title: |
Selective induction of Rab9-dependent alternative mitophagy using a synthetic derivative of isoquinoline alleviates mitochondrial dysfunction and cognitive deficits in Alzheimer's disease models. |
| Volume: |
14 |
| Issue: |
1 |
| Pages: |
56-74 |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion A12, Eileen McGowan |
| Allele Type: |
Transgenic |
| Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(Ckm-APPSw)A6Lfa/? |
| Background: |
involves: C57BL/6 * SJL |
| Zygosity: |
ot |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Atp7b/Atp7b Tg(PRNP-APPSweInd)8Dwst/? |
| Background: |
involves: C3H/HeJ * C57BL/6 |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Apoe/Apoe Tg(APPSWE)2576Kha/? |
| Background: |
involves: 129P2/OlaHsd * C57BL/6 * SJL |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gallwitz L |
| Year: |
2022 |
| Journal: |
Neurobiol Dis |
| Title: |
Cathepsin D: Analysis of its potential role as an amyloid beta degrading protease. |
| Volume: |
175 |
|
| Pages: |
105919 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wu Y |
| Year: |
2020 |
| Journal: |
FASEB J |
| Title: |
BHBA treatment improves cognitive function by targeting pleiotropic mechanisms in transgenic mouse model of Alzheimer's disease. |
| Volume: |
34 |
| Issue: |
1 |
| Pages: |
1412-1429 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wang Y |
| Year: |
2017 |
| Journal: |
Mol Neurodegener |
| Title: |
Gad67 haploinsufficiency reduces amyloid pathology and rescues olfactory memory deficits in a mouse model of Alzheimer's disease. |
| Volume: |
12 |
| Issue: |
1 |
| Pages: |
73 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wang MD |
| Year: |
2023 |
| Journal: |
Acta Pharmacol Sin |
| Title: |
Salvianolic acid B ameliorates retinal deficits in an early-stage Alzheimer's disease mouse model through downregulating BACE1 and Aβ generation. |
| Volume: |
44 |
| Issue: |
11 |
| Pages: |
2151-2168 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chen C |
| Year: |
2022 |
| Journal: |
Transl Psychiatry |
| Title: |
Early impairment of cortical circuit plasticity and connectivity in the 5XFAD Alzheimer's disease mouse model. |
| Volume: |
12 |
| Issue: |
1 |
| Pages: |
371 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zeng Y |
| Year: |
2015 |
| Journal: |
J Neurochem |
| Title: |
Tripchlorolide improves cognitive deficits by reducing amyloid β and upregulating synapse-related proteins in a transgenic model of Alzheimer's Disease. |
| Volume: |
133 |
| Issue: |
1 |
| Pages: |
38-52 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Py NA |
| Year: |
2014 |
| Journal: |
Front Aging Neurosci |
| Title: |
Differential spatio-temporal regulation of MMPs in the 5xFAD mouse model of Alzheimer's disease: evidence for a pro-amyloidogenic role of MT1-MMP. |
| Volume: |
6 |
|
| Pages: |
247 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Seipold L |
| Year: |
2018 |
| Journal: |
Cell Mol Life Sci |
| Title: |
In vivo regulation of the A disintegrin and metalloproteinase 10 (ADAM10) by the tetraspanin 15. |
| Volume: |
75 |
| Issue: |
17 |
| Pages: |
3251-3267 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Oakley H |
| Year: |
2006 |
| Journal: |
J Neurosci |
| Title: |
Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation. |
| Volume: |
26 |
| Issue: |
40 |
| Pages: |
10129-40 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [, , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with Down's syndrome carry an extra copy of chromosome 21, which contains the APP gene, and almost invariably develop amyloid plaques and Alzheimer's symptoms.APP is important for the neurogenesis and neuronal regeneration, either through the intact protein, or through its many breakdown products [, ]. APP consists of a large N-terminal extracellular region containing heparin-binding and copper-binding sites, Kunitz domain, E2 domain, a short hydrophobic transmembrane domain, and a short C-terminal intracellular domain. The N-terminal region is similar in structure to cysteine-rich growth factors and appears to function as a cell surface receptor, contributing to neurite growth, neuronal adhesion, axonogenesis and cell mobility []. APP acts as a kinesin I membrane receptor to mediate the axonal transport of beta-secretase and presenilin 1. The N-terminal domain can regulate neurite outgrowth through its binding to heparin and collagen I and IV, which are components of the extracellular matrix. APP is also coupled to apoptosis-inducing pathways, and is involved in copper homeostasis/oxidative stress through copper ion reduction, where copper-metallated APP induces neuronal death [, ]. The C-terminal intracellular domain appears to be involved in transcription regulation through protein-protein interactions. APP can promote transcription activation through binding to APBB1/Tip60, and may bind to the adaptor protein FE65 to transactivate a wide variety of different promoters.APP can be processed by different sets of enzymes:In the non-amyloidogenic (non-plaque-forming) pathway, APP is cleaved by alpha-secretase to yield a soluble N-terminal sAPP-alpha (neuroprotective) and a membrane-bound CTF-alpha. CTF-alpha is broken-down by presenilin-containing gamma-secretase to yield soluble p3 and membrane-bound AICD (nuclear signalling). In the amyloidogenic pathway (plaque-forming), APP is broken down by beta-secretase to yield soluble sAPP-beta and membrane-bound CTF-beta. CTF-beta is broken down by gamma-secretase to yield soluble amyloid-beta and membrane-bound AICD. Amyloid-beta is required for neuronal function, but can aggregate to form amyloid plaques that seem to disrupt brain cells by clogging points of cell-cell contact.This entry represents the family of amyloidogenic glycoproteins, such as amyloid-beta precursor protein (APP, or A4) and amyloid beta precursor like protein 1/2 (APLP1/2). APP is an integral, glycosylated membrane protein. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cortes-Canteli M |
| Year: |
2010 |
| Journal: |
Neuron |
| Title: |
Fibrinogen and beta-amyloid association alters thrombosis and fibrinolysis: a possible contributing factor to Alzheimer's disease. |
| Volume: |
66 |
| Issue: |
5 |
| Pages: |
695-709 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wilson EN |
| Year: |
2024 |
| Journal: |
Nat Neurosci |
| Title: |
TREM1 disrupts myeloid bioenergetics and cognitive function in aging and Alzheimer disease mouse models. |
| Volume: |
27 |
| Issue: |
5 |
| Pages: |
873-885 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Illouz T |
| Year: |
2024 |
| Journal: |
Sci Rep |
| Title: |
Unbiased analysis of spatial learning strategies in a modified Barnes maze using convolutional neural networks. |
| Volume: |
14 |
| Issue: |
1 |
| Pages: |
15944 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Savastano A |
| Year: |
2016 |
| Journal: |
J Alzheimers Dis |
| Title: |
N-truncated Aβ2-X starting with position two in sporadic Alzheimer's disease cases and two Alzheimer mouse models. |
| Volume: |
49 |
| Issue: |
1 |
| Pages: |
101-10 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Christensen DZ |
| Year: |
2009 |
| Journal: |
Brain Res |
| Title: |
Formic acid is essential for immunohistochemical detection of aggregated intraneuronal Abeta peptides in mouse models of Alzheimer's disease. |
| Volume: |
1301 |
|
| Pages: |
116-25 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wirths O |
| Year: |
2017 |
| Journal: |
Alzheimers Res Ther |
| Title: |
N-truncated Aβ4-x peptides in sporadic Alzheimer's disease cases and transgenic Alzheimer mouse models. |
| Volume: |
9 |
| Issue: |
1 |
| Pages: |
80 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Li R |
| Year: |
2022 |
| Journal: |
Aging Cell |
| Title: |
Accumulation of systematic TPM1 mediates inflammation and neuronal remodeling by phosphorylating PKA and regulating the FABP5/NF-κB signaling pathway in the retina of aged mice. |
| Volume: |
21 |
| Issue: |
3 |
| Pages: |
e13566 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Araki Y |
| Year: |
2003 |
| Journal: |
J Biol Chem |
| Title: |
Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism. |
| Volume: |
278 |
| Issue: |
49 |
| Pages: |
49448-58 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
357
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
182
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Allele |
| Name: |
deletion, Chr 16, Yann Herault 5 |
| Allele Type: |
Targeted |
| Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion A2, Christian Haass |
| Allele Type: |
Transgenic |
| Attribute String: |
Inserted expressed sequence |
|
•
•
•
•
•
|
| Strain |
| Attribute String: |
coisogenic, mutant strain, endonuclease-mediated mutation |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion 24, GemPharmatech |
| Allele Type: |
Transgenic |
| Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion 10, TaconicArtemis |
| Allele Type: |
Transgenic |
| Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(APPSWE)2576Kha/? |
| Background: |
involves: 129S7/SvEvBrd * C57BL/6 * SJL |
| Zygosity: |
ot |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(APPV717F)109Ili/? |
| Background: |
Not Specified |
| Zygosity: |
ot |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(PRNP-APPSweInd)8Dwst/? |
| Background: |
involves: 129S6/SvEvTac |
| Zygosity: |
ot |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wilcock DM |
| Year: |
2006 |
| Journal: |
J Neurosci |
| Title: |
Deglycosylated anti-amyloid-beta antibodies eliminate cognitive deficits and reduce parenchymal amyloid with minimal vascular consequences in aged amyloid precursor protein transgenic mice. |
| Volume: |
26 |
| Issue: |
20 |
| Pages: |
5340-6 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chapman PF |
| Year: |
1999 |
| Journal: |
Nat Neurosci |
| Title: |
Impaired synaptic plasticity and learning in aged amyloid precursor protein transgenic mice. |
| Volume: |
2 |
| Issue: |
3 |
| Pages: |
271-6 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hu Y |
| Year: |
2013 |
| Journal: |
J Biol Chem |
| Title: |
Role of cystatin C in amyloid precursor protein-induced proliferation of neural stem/progenitor cells. |
| Volume: |
288 |
| Issue: |
26 |
| Pages: |
18853-62 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lin CL |
| Year: |
2009 |
| Journal: |
Neurobiol Aging |
| Title: |
Epigallocatechin gallate (EGCG) suppresses beta-amyloid-induced neurotoxicity through inhibiting c-Abl/FE65 nuclear translocation and GSK3 beta activation. |
| Volume: |
30 |
| Issue: |
1 |
| Pages: |
81-92 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Pousinha PA |
| Year: |
2017 |
| Journal: |
Elife |
| Title: |
Physiological and pathophysiological control of synaptic GluN2B-NMDA receptors by the C-terminal domain of amyloid precursor protein. |
| Volume: |
6 |
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhang SQ |
| Year: |
2013 |
| Journal: |
J Neurosci Res |
| Title: |
Baicalein reduces β-amyloid and promotes nonamyloidogenic amyloid precursor protein processing in an Alzheimer's disease transgenic mouse model. |
| Volume: |
91 |
| Issue: |
9 |
| Pages: |
1239-46 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Middei S |
| Year: |
2008 |
| Journal: |
Neurobiol Learn Mem |
| Title: |
Region-specific changes in the microanatomy of single dendritic spines over time might account for selective memory alterations in ageing hAPPsweTg2576 mice, a mouse model for Alzheimer disease. |
| Volume: |
90 |
| Issue: |
2 |
| Pages: |
467-71 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Rocher AB |
| Year: |
2008 |
| Journal: |
Neurobiol Dis |
| Title: |
Significant structural but not physiological changes in cortical neurons of 12-month-old Tg2576 mice. |
| Volume: |
32 |
| Issue: |
2 |
| Pages: |
309-18 |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(APP695)3Dbo/? Tg(Eno2-PTGS2)32Pasi/? Tg(PSEN1)5Dbo/? |
| Background: |
involves: C3H/HeJ * C57BL/6J |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
654
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
707
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
695
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
655
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
695
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Pilat D |
| Year: |
2024 |
| Journal: |
Biomolecules |
| Title: |
Suppression of MT5-MMP Reveals Early Modulation of Alzheimer's Pathogenic Events in Primary Neuronal Cultures of 5xFAD Mice. |
| Volume: |
14 |
| Issue: |
12 |
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ephrame SJ |
| Year: |
2023 |
| Journal: |
Front Aging Neurosci |
| Title: |
O-GlcNAcylation regulates extracellular signal-regulated kinase (ERK) activation in Alzheimer's disease. |
| Volume: |
15 |
|
| Pages: |
1155630 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lee JH |
| Year: |
2022 |
| Journal: |
Nat Neurosci |
| Title: |
Faulty autolysosome acidification in Alzheimer's disease mouse models induces autophagic build-up of Aβ in neurons, yielding senile plaques. |
| Volume: |
25 |
| Issue: |
6 |
| Pages: |
688-701 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhang Z |
| Year: |
2015 |
| Journal: |
Nat Commun |
| Title: |
Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer's disease. |
| Volume: |
6 |
|
| Pages: |
8762 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [, , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with Down's syndrome carry an extra copy of chromosome 21, which contains the APP gene, and almost invariably develop amyloid plaques and Alzheimer's symptoms.APP is important for the neurogenesis and neuronal regeneration, either through the intact protein, or through its many breakdown products [, ]. APP consists of a large N-terminal extracellular region containing heparin-binding and copper-binding sites, Kunitz domain, E2 domain, a short hydrophobic transmembrane domain, and a short C-terminal intracellular domain. The N-terminal region is similar in structure to cysteine-rich growth factors and appears to function as a cell surface receptor, contributing to neurite growth, neuronal adhesion, axonogenesis and cell mobility []. APP acts as a kinesin I membrane receptor to mediate the axonal transport of beta-secretase and presenilin 1. The N-terminal domain can regulate neurite outgrowth through its binding to heparin and collagen I and IV, which are components of the extracellular matrix. APP is also coupled to apoptosis-inducing pathways, and is involved in copper homeostasis/oxidative stress through copper ion reduction, where copper-metallated APP induces neuronal death [, ]. The C-terminal intracellular domain appears to be involved in transcription regulation through protein-protein interactions. APP can promote transcription activation through binding to APBB1/Tip60, and may bind to the adaptor protein FE65 to transactivate a wide variety of different promoters.APP can be processed by different sets of enzymes:In the non-amyloidogenic (non-plaque-forming) pathway, APP is cleaved by alpha-secretase to yield a soluble N-terminal sAPP-alpha (neuroprotective) and a membrane-bound CTF-alpha. CTF-alpha is broken-down by presenilin-containing gamma-secretase to yield soluble p3 and membrane-bound AICD (nuclear signalling). In the amyloidogenic pathway (plaque-forming), APP is broken down by beta-secretase to yield soluble sAPP-beta and membrane-bound CTF-beta. CTF-beta is broken down by gamma-secretase to yield soluble amyloid-beta and membrane-bound AICD. Amyloid-beta is required for neuronal function, but can aggregate to form amyloid plaques that seem to disrupt brain cells by clogging points of cell-cell contact.This superfamily represents a heparin-binding domain found at the N-terminal of the extracellular domain, which is itself found at the N-terminal of amyloidogenic glycoproteins such as amyloid-beta precursor protein (APP, or A4). The core of the heparin-binding domain has an unusual disulphide-rich fold, consisting of a beta-x-α-β-loop-beta topology []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [, , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with Down's syndrome carry an extra copy of chromosome 21, which contains the APP gene, and almost invariably develop amyloid plaques and Alzheimer's symptoms.APP is important for the neurogenesis and neuronal regeneration, either through the intact protein, or through its many breakdown products [, ]. APP consists of a large N-terminal extracellular region containing heparin-binding and copper-binding sites, Kunitz domain, E2 domain, a short hydrophobic transmembrane domain, and a short C-terminal intracellular domain. The N-terminal region is similar in structure to cysteine-rich growth factors and appears to function as a cell surface receptor, contributing to neurite growth, neuronal adhesion, axonogenesis and cell mobility []. APP acts as a kinesin I membrane receptor to mediate the axonal transport of beta-secretase and presenilin 1. The N-terminal domain can regulate neurite outgrowth through its binding to heparin and collagen I and IV, which are components of the extracellular matrix. APP is also coupled to apoptosis-inducing pathways, and is involved in copper homeostasis/oxidative stress through copper ion reduction, where copper-metallated APP induces neuronal death [, ]. The C-terminal intracellular domain appears to be involved in transcription regulation through protein-protein interactions. APP can promote transcription activation through binding to APBB1/Tip60, and may bind to the adaptor protein FE65 to transactivate a wide variety of different promoters.APP can be processed by different sets of enzymes:In the non-amyloidogenic (non-plaque-forming) pathway, APP is cleaved by alpha-secretase to yield a soluble N-terminal sAPP-alpha (neuroprotective) and a membrane-bound CTF-alpha. CTF-alpha is broken-down by presenilin-containing gamma-secretase to yield soluble p3 and membrane-bound AICD (nuclear signalling). In the amyloidogenic pathway (plaque-forming), APP is broken down by beta-secretase to yield soluble sAPP-beta and membrane-bound CTF-beta. CTF-beta is broken down by gamma-secretase to yield soluble amyloid-beta and membrane-bound AICD. Amyloid-beta is required for neuronal function, but can aggregate to form amyloid plaques that seem to disrupt brain cells by clogging points of cell-cell contact.This superfamily represents a copper-binding domain found within the extracellular domain, which is at the N-terminal of amyloidogenic glycoproteins such as amyloid-beta precursor protein (APP, or A4). The copper-binding domain has a dodecin-like fold consisting of a 2-layer alpha/beta topology []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Conserved_site |
| Description: |
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [, , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with Down's syndrome carry an extra copy of chromosome 21, which contains the APP gene, and almost invariably develop amyloid plaques and Alzheimer's symptoms.APP is important for the neurogenesis and neuronal regeneration, either through the intact protein, or through its many breakdown products [, ]. APP consists of a large N-terminal extracellular region containing heparin-binding and copper-binding sites, Kunitz domain, E2 domain, a short hydrophobic transmembrane domain, and a short C-terminal intracellular domain. The N-terminal region is similar in structure to cysteine-rich growth factors and appears to function as a cell surface receptor, contributing to neurite growth, neuronal adhesion, axonogenesis and cell mobility []. APP acts as a kinesin I membrane receptor to mediate the axonal transportof beta-secretase and presenilin 1. The N-terminal domain can regulate neurite outgrowth through its binding to heparin and collagen I and IV, which are components of the extracellular matrix. APP is also coupled to apoptosis-inducing pathways, and is involved in copper homeostasis/oxidative stress through copper ion reduction, where copper-metallated APP induces neuronal death [, ]. The C-terminal intracellular domain appears to be involved in transcription regulation through protein-protein interactions. APP can promote transcription activation through binding to APBB1/Tip60, and may bind to the adaptor protein FE65 to transactivate a wide variety of different promoters.APP can be processed by different sets of enzymes:In the non-amyloidogenic (non-plaque-forming) pathway, APP is cleaved by alpha-secretase to yield a soluble N-terminal sAPP-alpha (neuroprotective) and a membrane-bound CTF-alpha. CTF-alpha is broken-down by presenilin-containing gamma-secretase to yield soluble p3 and membrane-bound AICD (nuclear signalling). In the amyloidogenic pathway (plaque-forming), APP is broken down by beta-secretase to yield soluble sAPP-beta and membrane-bound CTF-beta. CTF-beta is broken down by gamma-secretase to yield soluble amyloid-beta and membrane-bound AICD. Amyloid-beta is required for neuronal function, but can aggregate to form amyloid plaques that seem to disrupt brain cells by clogging points of cell-cell contact.This entry represents a conserved octapeptide located in the CuBD domain. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Conserved_site |
| Description: |
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [, , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with Down's syndrome carry an extra copy of chromosome 21, which contains the APP gene, and almost invariably develop amyloid plaques and Alzheimer's symptoms.APP is important for the neurogenesis and neuronal regeneration, either through the intact protein, or through its many breakdown products [, ]. APP consists of a large N-terminal extracellular region containing heparin-binding and copper-binding sites, Kunitz domain, E2 domain, a short hydrophobic transmembrane domain, and a short C-terminal intracellular domain. The N-terminal region is similar in structure to cysteine-rich growth factors and appears to function as a cell surface receptor, contributing to neurite growth, neuronal adhesion, axonogenesis and cell mobility []. APP acts as a kinesin I membrane receptor to mediate the axonal transport of beta-secretase and presenilin 1. The N-terminal domain can regulate neurite outgrowth through its binding to heparin and collagen I and IV, which are components of the extracellular matrix. APP is also coupled to apoptosis-inducing pathways, and is involved in copper homeostasis/oxidative stress through copper ion reduction, where copper-metallated APP induces neuronal death [, ]. The C-terminal intracellular domain appears to be involved in transcription regulation through protein-protein interactions. APP can promote transcription activation through binding to APBB1/Tip60, and may bind to the adaptor protein FE65 to transactivate a wide variety of different promoters.APP can be processed by different sets of enzymes:In the non-amyloidogenic (non-plaque-forming) pathway, APP is cleaved by alpha-secretase to yield a soluble N-terminal sAPP-alpha (neuroprotective) and a membrane-bound CTF-alpha. CTF-alpha is broken-down by presenilin-containing gamma-secretase to yield soluble p3 and membrane-bound AICD (nuclear signalling). In the amyloidogenic pathway (plaque-forming), APP is broken down by beta-secretase to yield soluble sAPP-beta and membrane-bound CTF-beta. CTF-beta is broken down by gamma-secretase to yield soluble amyloid-beta and membrane-bound AICD. Amyloid-beta is required for neuronal function, but can aggregate to form amyloid plaques that seem to disrupt brain cells by clogging points of cell-cell contact.This entry represents a conserved signature pattern located in the intra-cellular domain and found towards the C-terminal extremity of these proteins. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [, , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with Down's syndrome carry an extra copy of chromosome 21, which contains the APP gene, and almost invariably develop amyloid plaques and Alzheimer's symptoms.APP is important for the neurogenesis and neuronal regeneration, either through the intact protein, or through its many breakdown products [, ]. APP consists of a large N-terminal extracellular region containing heparin-binding and copper-binding sites, Kunitz domain, E2 domain, a short hydrophobic transmembrane domain, and a short C-terminal intracellular domain. The N-terminal region is similar in structure to cysteine-rich growth factors and appears to function as a cell surface receptor, contributing to neurite growth, neuronal adhesion, axonogenesis and cell mobility []. APP acts as a kinesin I membrane receptor to mediate the axonal transport of beta-secretase and presenilin 1. The N-terminal domain can regulate neurite outgrowth through its binding to heparin and collagen I and IV, which are components of the extracellular matrix. APP is also coupled to apoptosis-inducing pathways, and is involved in copper homeostasis/oxidative stress through copper ion reduction, where copper-metallated APP induces neuronal death [, ]. The C-terminal intracellular domain appears to be involved in transcription regulation through protein-protein interactions. APP can promote transcription activation through binding to APBB1/Tip60, and may bind to the adaptor protein FE65 to transactivate a wide variety of different promoters.APP can be processed by different sets of enzymes:In the non-amyloidogenic (non-plaque-forming) pathway, APP is cleaved by alpha-secretase to yield a soluble N-terminal sAPP-alpha (neuroprotective) and a membrane-bound CTF-alpha. CTF-alpha is broken-down by presenilin-containing gamma-secretase to yield soluble p3 and membrane-bound AICD (nuclear signalling). In the amyloidogenic pathway (plaque-forming), APP is broken down by beta-secretase to yield soluble sAPP-beta and membrane-bound CTF-beta. CTF-beta is broken down by gamma-secretase to yield soluble amyloid-beta and membrane-bound AICD. Amyloid-beta is required for neuronal function, but can aggregate to form amyloid plaques that seem to disrupt brain cells by clogging points of cell-cell contact.This entry represents the amyloid-beta peptide (A-beta) superfamily, which originates as a breakdown product from the cleavage of amyloid-beta precursor protein (APP, or A4), an integral, glycosylated membrane brain protein. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [, , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with Down's syndrome carry an extra copy of chromosome 21, which contains the APP gene, and almost invariably develop amyloid plaques and Alzheimer's symptoms.APP is important for the neurogenesis and neuronal regeneration, either through the intact protein, or through its many breakdown products [, ]. APP consists of a large N-terminal extracellular region containing heparin-binding and copper-binding sites, Kunitz domain, E2 domain, a short hydrophobic transmembrane domain, and a short C-terminal intracellular domain. The N-terminal region is similar in structure to cysteine-rich growth factors and appears to function as a cell surface receptor, contributing to neurite growth, neuronal adhesion, axonogenesis and cell mobility []. APP acts as a kinesin I membrane receptor to mediate the axonal transport of beta-secretase and presenilin 1. The N-terminal domain can regulate neurite outgrowth through its binding to heparin and collagen I and IV, which are components of the extracellular matrix. APP is also coupled to apoptosis-inducing pathways, and is involved in copper homeostasis/oxidative stress through copper ion reduction, where copper-metallated APP induces neuronal death [, ]. The C-terminal intracellular domain appears to be involved in transcription regulation through protein-protein interactions. APP can promote transcription activation through binding to APBB1/Tip60, and may bind to the adaptor protein FE65 to transactivate a wide variety of different promoters.APP can be processed by different sets of enzymes:In the non-amyloidogenic (non-plaque-forming) pathway, APP is cleaved by alpha-secretase to yield a soluble N-terminal sAPP-alpha (neuroprotective) and a membrane-bound CTF-alpha. CTF-alpha is broken-down by presenilin-containing gamma-secretase to yield soluble p3 and membrane-bound AICD (nuclear signalling). In the amyloidogenic pathway (plaque-forming), APP is broken down by beta-secretase to yield soluble sAPP-beta and membrane-bound CTF-beta. CTF-beta is broken down by gamma-secretase to yield soluble amyloid-beta and membrane-bound AICD. Amyloid-beta is required for neuronal function, but can aggregate to form amyloid plaques that seem to disrupt brain cells by clogging points of cell-cell contact.This entry represents a heparin-binding domain found at the N-terminal of the extracellular domain, which is itself found at the N-terminal of amyloidogenic glycoproteins such as amyloid-beta precursor protein (APP, or A4). The core of the heparin-binding domain has an unusual disulphide-rich fold, consisting of a beta-x-α-β-loop-beta topology []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [, , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with Down's syndrome carry an extra copy of chromosome 21, which contains the APP gene, and almost invariably develop amyloid plaques and Alzheimer's symptoms.APP is important for the neurogenesis and neuronal regeneration, either through the intact protein, or through its many breakdown products [, ]. APP consists of a large N-terminal extracellular region containing heparin-binding and copper-binding sites, Kunitz domain, E2 domain, a short hydrophobic transmembrane domain, and a short C-terminal intracellular domain. The N-terminal region is similar in structure to cysteine-rich growth factors and appears to function as a cell surface receptor, contributing to neurite growth, neuronal adhesion, axonogenesis and cell mobility []. APP acts as a kinesin I membrane receptor to mediate the axonal transport of beta-secretase and presenilin 1. The N-terminal domain can regulate neurite outgrowth through its binding to heparin and collagen I and IV, which are components of the extracellular matrix. APP is also coupled to apoptosis-inducing pathways, and is involved in copper homeostasis/oxidative stress through copper ion reduction, where copper-metallated APP induces neuronal death [, ]. The C-terminal intracellular domain appears to be involved in transcription regulation through protein-protein interactions. APP can promote transcription activation through binding to APBB1/Tip60, and may bind to the adaptor protein FE65 to transactivate a wide variety of different promoters.APP can be processed by different sets of enzymes:In the non-amyloidogenic (non-plaque-forming) pathway, APP is cleaved by alpha-secretase to yield a soluble N-terminal sAPP-alpha (neuroprotective) and a membrane-bound CTF-alpha. CTF-alpha is broken-down by presenilin-containing gamma-secretase to yield soluble p3 and membrane-bound AICD (nuclear signalling). In the amyloidogenic pathway (plaque-forming), APP is broken down by beta-secretase to yield soluble sAPP-beta and membrane-bound CTF-beta. CTF-beta is broken down by gamma-secretase to yield soluble amyloid-beta and membrane-bound AICD. Amyloid-beta is required for neuronal function, but can aggregate to form amyloid plaques that seem to disrupt brain cells by clogging points of cell-cell contact.This entry represents the amyloid-beta peptide (A-beta), which originates as a breakdown product from the cleavage of amyloid-beta precursor protein (APP, or A4), an integral, glycosylated membrane brain protein. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [, , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with Down's syndrome carry an extra copy of chromosome 21, which contains the APP gene, and almost invariably develop amyloid plaques and Alzheimer's symptoms.APP is important for the neurogenesis and neuronal regeneration, either through the intact protein, or through its many breakdown products [, ]. APP consists of a large N-terminal extracellular region containing heparin-binding and copper-binding sites, Kunitz domain, E2domain, a short hydrophobic transmembrane domain, and a short C-terminal intracellular domain. The N-terminal region is similar in structure to cysteine-rich growth factors and appears to function as a cell surface receptor, contributing to neurite growth, neuronal adhesion, axonogenesis and cell mobility []. APP acts as a kinesin I membrane receptor to mediate the axonal transport of beta-secretase and presenilin 1. The N-terminal domain can regulate neurite outgrowth through its binding to heparin and collagen I and IV, which are components of the extracellular matrix. APP is also coupled to apoptosis-inducing pathways, and is involved in copper homeostasis/oxidative stress through copper ion reduction, where copper-metallated APP induces neuronal death [, ]. The C-terminal intracellular domain appears to be involved in transcription regulation through protein-protein interactions. APP can promote transcription activation through binding to APBB1/Tip60, and may bind to the adaptor protein FE65 to transactivate a wide variety of different promoters.APP can be processed by different sets of enzymes:In the non-amyloidogenic (non-plaque-forming) pathway, APP is cleaved by alpha-secretase to yield a soluble N-terminal sAPP-alpha (neuroprotective) and a membrane-bound CTF-alpha. CTF-alpha is broken-down by presenilin-containing gamma-secretase to yield soluble p3 and membrane-bound AICD (nuclear signalling). In the amyloidogenic pathway (plaque-forming), APP is broken down by beta-secretase to yield soluble sAPP-beta and membrane-bound CTF-beta. CTF-beta is broken down by gamma-secretase to yield soluble amyloid-beta and membrane-bound AICD. Amyloid-beta is required for neuronal function, but can aggregate to form amyloid plaques that seem to disrupt brain cells by clogging points of cell-cell contact.This entry represents a copper-binding domain found within the extracellular domain, which is at the N-terminal of amyloidogenic glycoproteins such as amyloid-beta precursor protein (APP, or A4). The copper-binding domain has a dodecin-like fold consisting of a 2-layer alpha/beta topology []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Amyloid-beta precursor protein (APP, or A4) is associated with Alzheimer's disease (AD), because one of its breakdown products, amyloid-beta (A-beta), aggregates to form amyloid or senile plaques [, , ]. Mutations in APP or in proteins that process APP have been linked with early-onset, familial AD. Individuals with Down's syndrome carry an extra copy of chromosome 21, which contains the APP gene, and almost invariably develop amyloid plaques and Alzheimer's symptoms.APP is important for the neurogenesis and neuronal regeneration, either through the intact protein, or through its many breakdown products [, ]. APP consists of a large N-terminal extracellular region containing heparin-binding and copper-binding sites, Kunitz domain, E2 domain, a short hydrophobic transmembrane domain, and a short C-terminal intracellular domain. The N-terminal region is similar in structure to cysteine-rich growth factors and appears to function as a cellsurface receptor, contributing to neurite growth, neuronal adhesion, axonogenesis and cell mobility []. APP acts as a kinesin I membrane receptor to mediate the axonal transport of beta-secretase and presenilin 1. The N-terminal domain can regulate neurite outgrowth through its binding to heparin and collagen I and IV, which are components of the extracellular matrix. APP is also coupled to apoptosis-inducing pathways, and is involved in copper homeostasis/oxidative stress through copper ion reduction, where copper-metallated APP induces neuronal death [, ]. The C-terminal intracellular domain appears to be involved in transcription regulation through protein-protein interactions. APP can promote transcription activation through binding to APBB1/Tip60, and may bind to the adaptor protein FE65 to transactivate a wide variety of different promoters.APP can be processed by different sets of enzymes:In the non-amyloidogenic (non-plaque-forming) pathway, APP is cleaved by alpha-secretase to yield a soluble N-terminal sAPP-alpha (neuroprotective) and a membrane-bound CTF-alpha. CTF-alpha is broken-down by presenilin-containing gamma-secretase to yield soluble p3 and membrane-bound AICD (nuclear signalling). In the amyloidogenic pathway (plaque-forming), APP is broken down by beta-secretase to yield soluble sAPP-beta and membrane-bound CTF-beta. CTF-beta is broken down by gamma-secretase to yield soluble amyloid-beta and membrane-bound AICD. Amyloid-beta is required for neuronal function, but can aggregate to form amyloid plaques that seem to disrupt brain cells by clogging points of cell-cell contact.This entry represents an extracellular domain that is usually found at the N-terminal of amyloidogenic glycoproteins such as amyloid-beta precursor protein (APP, or A4). |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion 109, Ivan Lieberburg |
| Allele Type: |
Transgenic |
| Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion 2, Fred Van Leuven |
| Allele Type: |
Transgenic |
| Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion B, Lars Nilsson |
| Allele Type: |
Transgenic |
| Attribute String: |
Inserted expressed sequence |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion f, A Claudio Cuello |
| Allele Type: |
Transgenic |
| Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(Camk2a-tTA)1Mmay/? Tg(tetO-APPSwInd)18Dbo/? |
| Background: |
involves: C3H/HeJ * C57BL/6 * CBA |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(Thy1-APPSwe,Prnp-PSEN2*N141I)152HLaoz/? Tg(Thy1-MAPT)183Gotz/? |
| Background: |
B6.Cg-Tg(Thy1-APPSwe,Prnp-PSEN2*N141I)152HLaoz Tg(Thy1-MAPT)183Gotz |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tlr2/Tlr2 Tg(APP695)3Dbo/? Tg(PSEN1)5Dbo/? |
| Background: |
involves: 129 * C3H/HeJ * C57BL/6 |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Psen1/Psen1 Tg(APPSwe,tauP301L)1Lfa/? |
| Background: |
involves: 129S1/Sv * 129X1/SvJ * C57BL/6 |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| HT Experiment |
| Series Id: |
GSE64398 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
Baseline |
| Source: |
ArrayExpress |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| HT Experiment |
|
| Experiment Type: |
RNA-Seq |
| Study Type: |
WT vs. Mutant |
| Source: |
GEO |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Rangan P |
| Year: |
2022 |
| Journal: |
Cell Rep |
| Title: |
Fasting-mimicking diet cycles reduce neuroinflammation to attenuate cognitive decline in Alzheimer's models. |
| Volume: |
40 |
| Issue: |
13 |
| Pages: |
111417 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wu D |
| Year: |
2021 |
| Journal: |
Clin Transl Med |
| Title: |
Medial septum tau accumulation induces spatial memory deficit via disrupting medial septum-hippocampus cholinergic pathway. |
| Volume: |
11 |
| Issue: |
6 |
| Pages: |
e428 |
|
•
•
•
•
•
|
