APLP1: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
m (Bot: HTTP→HTTPS)
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Amyloid-like protein 1''', also known as '''APLP1''', is a [[protein]] that in humans is encoded by the ''APLP1'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APLP1 amyloid beta (A4) precursor-like protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=333| accessdate = }}</ref><ref name="pmid8432545">{{cite journal |vauthors=Wasco W, Brook JD, Tanzi RE | title = The amyloid precursor-like protein (APLP) gene maps to the long arm of human chromosome 19 | journal = Genomics | volume = 15 | issue = 1 | pages = 237–9 |date=January 1993 | pmid = 8432545 | doi = 10.1006/geno.1993.1047 }}</ref> APLP1 along with [[APLP2]] are important modulators of [[glucose]] and [[insulin]] [[homeostasis]].<ref name="pmid18393365"/>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Amyloid beta (A4) precursor-like protein 1
| HGNCid = 597
| Symbol = APLP1
| AltSymbols =; APLP
| OMIM = 104775
| ECnumber = 
| Homologene = 68447
| MGIid = 88046
| GeneAtlas_image1 = PBB_GE_APLP1_209462_at_tn.png
| Function = {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005905 |text = coated pit}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006378 |text = mRNA polyadenylation}} {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008219 |text = cell death}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0030198 |text = extracellular matrix organization and biogenesis}} {{GNF_GO|id=GO:0030900 |text = forebrain development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 333
    | Hs_Ensembl = ENSG00000105290
    | Hs_RefseqProtein = NP_001019978
    | Hs_RefseqmRNA = NM_001024807
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 41051241
    | Hs_GenLoc_end = 41062539
    | Hs_Uniprot = P51693
    | Mm_EntrezGene = 11803
    | Mm_Ensembl = ENSMUSG00000006651
    | Mm_RefseqmRNA = XM_994141
    | Mm_RefseqProtein = XP_999235
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 30143740
    | Mm_GenLoc_end = 30154321
    | Mm_Uniprot = Q3TCA7
  }}
}}
'''Amyloid beta (A4) precursor-like protein 1''', also known as '''APLP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APLP1 amyloid beta (A4) precursor-like protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=333| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a member of the highly conserved [[amyloid precursor protein]] gene family. The encoded protein is a membrane-associated glycoprotein that is cleaved by [[secretase]]s in a manner similar to amyloid beta A4 precursor protein cleavage. This cleavage liberates an intracellular cytoplasmic fragment that may act as a transcriptional activator. The encoded protein may also play a role in synaptic maturation during cortical development. [[Alternative splicing|Alternatively spliced]] transcript variants encoding different isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: APLP1 amyloid beta (A4) precursor-like protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=333| accessdate = }}</ref>
{{PBB_Summary
 
| section_title =
APLP1 and [[APLP2]] double [[knockout mouse|knockout mice]] display [[hypoglycemia]] and [[hyperinsulinemia]] indicating that these two proteins are important modulators of glucose and insulin homeostasis.<ref name="pmid18393365">{{cite journal |vauthors=Needham BE, Wlodek ME, Ciccotosto GD, Fam BC, Masters CL, Proietto J, Andrikopoulos S, Cappai R | title = Identification of the Alzheimer's disease amyloid precursor protein (APP) and its homologue APLP2 as essential modulators of glucose and insulin homeostasis and growth | journal = J. Pathol. | volume = 215 | issue = 2 | pages = 155–63 |date=June 2008 | pmid = 18393365 | doi = 10.1002/path.2343 | url =  }}</ref>
| summary_text = This gene encodes a member of the highly conserved amyloid precursor protein gene family. The encoded protein is a membrane-associated glycoprotein that is cleaved by secretases in a manner similar to amyloid beta A4 precursor protein cleavage. This cleavage liberates an intracellular cytoplasmic fragment that may act as a transcriptional activator. The encoded protein may also play a role in synaptic maturation during cortical development. Alternatively spliced transcript variants encoding different isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: APLP1 amyloid beta (A4) precursor-like protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=333| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|APLP1}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  |vauthors=Bayer TA, Cappai R, Masters CL |title=It all sticks together--the APP-related family of proteins and Alzheimer's disease. |journal=Mol. Psychiatry |volume=4 |issue= 6 |pages= 524–8 |year= 2000 |pmid= 10578233 |doi=10.1038/sj.mp.4000552 |display-authors=etal}}
| citations =
*{{cite journal  |vauthors=Kim TW, Wu K, Xu JL |title=Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density. |journal=Brain Res. Mol. Brain Res. |volume=32 |issue= 1 |pages= 36–44 |year= 1996 |pmid= 7494461 |doi=10.1016/0169-328X(95)00328-P |display-authors=etal}}
*{{cite journal  | author=Bayer TA, Cappai R, Masters CL, ''et al.'' |title=It all sticks together--the APP-related family of proteins and Alzheimer's disease. |journal=Mol. Psychiatry |volume=4 |issue= 6 |pages= 524-8 |year= 2000 |pmid= 10578233 |doi=  }}
*{{cite journal  |vauthors=Bush AI, Pettingell WH, de Paradis M |title=The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily. |journal=J. Biol. Chem. |volume=269 |issue= 43 |pages= 26618–21 |year= 1994 |pmid= 7929392 |doi=  |display-authors=etal}}
*{{cite journal  | author=Kim TW, Wu K, Xu JL, ''et al.'' |title=Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density. |journal=Brain Res. Mol. Brain Res. |volume=32 |issue= 1 |pages= 36-44 |year= 1996 |pmid= 7494461 |doi=  }}
*{{cite journal  |vauthors=Wasco W, Brook JD, Tanzi RE |title=The amyloid precursor-like protein (APLP) gene maps to the long arm of human chromosome 19. |journal=Genomics |volume=15 |issue= 1 |pages= 237–9 |year= 1993 |pmid= 8432545 |doi= 10.1006/geno.1993.1047 }}
*{{cite journal  | author=Bush AI, Pettingell WH, de Paradis M, ''et al.'' |title=The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily. |journal=J. Biol. Chem. |volume=269 |issue= 43 |pages= 26618-21 |year= 1994 |pmid= 7929392 |doi=  }}
*{{cite journal  |vauthors=Bressler SL, Gray MD, Sopher BL |title=cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein. |journal=Hum. Mol. Genet. |volume=5 |issue= 10 |pages= 1589–98 |year= 1997 |pmid= 8894693 |doi=10.1093/hmg/5.10.1589 |display-authors=etal}}
*{{cite journal  | author=Wasco W, Brook JD, Tanzi RE |title=The amyloid precursor-like protein (APLP) gene maps to the long arm of human chromosome 19. |journal=Genomics |volume=15 |issue= 1 |pages= 237-9 |year= 1993 |pmid= 8432545 |doi= 10.1006/geno.1993.1047 }}
*{{cite journal  |vauthors=Paliga K, Peraus G, Kreger S |title=Human amyloid precursor-like protein 1--cDNA cloning, ectopic expression in COS-7 cells and identification of soluble forms in the cerebrospinal fluid. |journal=Eur. J. Biochem. |volume=250 |issue= 2 |pages= 354–63 |year= 1998 |pmid= 9428684 |doi=10.1111/j.1432-1033.1997.0354a.x |display-authors=etal}}
*{{cite journal  | author=Bressler SL, Gray MD, Sopher BL, ''et al.'' |title=cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein. |journal=Hum. Mol. Genet. |volume=5 |issue= 10 |pages= 1589-98 |year= 1997 |pmid= 8894693 |doi=  }}
*{{cite journal  |vauthors=Lenkkeri U, Kestilä M, Lamerdin J |title=Structure of the human amyloid-precursor-like protein gene APLP1 at 19q13.1. |journal=Hum. Genet. |volume=102 |issue= 2 |pages= 192–6 |year= 1998 |pmid= 9521588 |doi=10.1007/s004390050676 |display-authors=etal}}
*{{cite journal  | author=Paliga K, Peraus G, Kreger S, ''et al.'' |title=Human amyloid precursor-like protein 1--cDNA cloning, ectopic expression in COS-7 cells and identification of soluble forms in the cerebrospinal fluid. |journal=Eur. J. Biochem. |volume=250 |issue= 2 |pages= 354-63 |year= 1998 |pmid= 9428684 |doi=  }}
*{{cite journal  |vauthors=McNamara MJ, Ruff CT, Wasco W |title=Immunohistochemical and in situ analysis of amyloid precursor-like protein-1 and amyloid precursor-like protein-2 expression in Alzheimer disease and aged control brains. |journal=Brain Res. |volume=804 |issue= 1 |pages= 45–51 |year= 1998 |pmid= 9729270 |doi=10.1016/S0006-8993(98)00653-2  |display-authors=etal}}
*{{cite journal  | author=Lenkkeri U, Kestilä M, Lamerdin J, ''et al.'' |title=Structure of the human amyloid-precursor-like protein gene APLP1 at 19q13.1. |journal=Hum. Genet. |volume=102 |issue= 2 |pages= 192-6 |year= 1998 |pmid= 9521588 |doi=  }}
*{{cite journal  |vauthors=Tomita S, Ozaki T, Taru H |title=Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein. |journal=J. Biol. Chem. |volume=274 |issue= 4 |pages= 2243–54 |year= 1999 |pmid= 9890987 |doi=10.1074/jbc.274.4.2243  |display-authors=etal}}
*{{cite journal  | author=McNamara MJ, Ruff CT, Wasco W, ''et al.'' |title=Immunohistochemical and in situ analysis of amyloid precursor-like protein-1 and amyloid precursor-like protein-2 expression in Alzheimer disease and aged control brains. |journal=Brain Res. |volume=804 |issue= 1 |pages= 45-51 |year= 1998 |pmid= 9729270 |doi= }}
*{{cite journal  |vauthors=Homayouni R, Rice DS, Sheldon M, Curran T |title=Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. |journal=J. Neurosci. |volume=19 |issue= 17 |pages= 7507–15 |year= 1999 |pmid= 10460257 |doi=  }}
*{{cite journal  | author=Tomita S, Ozaki T, Taru H, ''et al.'' |title=Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein. |journal=J. Biol. Chem. |volume=274 |issue= 4 |pages= 2243-54 |year= 1999 |pmid= 9890987 |doi= }}
*{{cite journal  |vauthors=Simons A, Ruppert T, Schmidt C |title=Evidence for a copper-binding superfamily of the amyloid precursor protein. |journal=Biochemistry |volume=41 |issue= 30 |pages= 9310–20 |year= 2002 |pmid= 12135352 |doi=10.1021/bi0258647 |display-authors=etal}}
*{{cite journal  | author=Homayouni R, Rice DS, Sheldon M, Curran T |title=Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. |journal=J. Neurosci. |volume=19 |issue= 17 |pages= 7507-15 |year= 1999 |pmid= 10460257 |doi=  }}
*{{cite journal  |vauthors=Scheinfeld MH, Ghersi E, Laky K |title=Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-secretase regulates transcription. |journal=J. Biol. Chem. |volume=277 |issue= 46 |pages= 44195–201 |year= 2003 |pmid= 12228233 |doi= 10.1074/jbc.M208110200 |display-authors=etal}}
*{{cite journal  | author=Simons A, Ruppert T, Schmidt C, ''et al.'' |title=Evidence for a copper-binding superfamily of the amyloid precursor protein. |journal=Biochemistry |volume=41 |issue= 30 |pages= 9310-20 |year= 2002 |pmid= 12135352 |doi=  }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Scheinfeld MH, Ghersi E, Laky K, ''et al.'' |title=Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-secretase regulates transcription. |journal=J. Biol. Chem. |volume=277 |issue= 46 |pages= 44195-201 |year= 2003 |pmid= 12228233 |doi= 10.1074/jbc.M208110200 }}
*{{cite journal  |vauthors=Walsh DM, Fadeeva JV, LaVoie MJ |title=gamma-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins. |journal=Biochemistry |volume=42 |issue= 22 |pages= 6664–73 |year= 2003 |pmid= 12779321 |doi= 10.1021/bi027375c |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Yamakami M, Yoshimori T, Yokosawa H |title=Tom1, a VHS domain-containing protein, interacts with tollip, ubiquitin, and clathrin. |journal=J. Biol. Chem. |volume=278 |issue= 52 |pages= 52865–72 |year= 2004 |pmid= 14563850 |doi= 10.1074/jbc.M306740200 }}
*{{cite journal  | author=Walsh DM, Fadeeva JV, LaVoie MJ, ''et al.'' |title=gamma-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins. |journal=Biochemistry |volume=42 |issue= 22 |pages= 6664-73 |year= 2003 |pmid= 12779321 |doi= 10.1021/bi027375c }}
*{{cite journal  |vauthors=Adlerz L, Beckman M, Holback S |title=Accumulation of the amyloid precursor-like protein APLP2 and reduction of APLP1 in retinoic acid-differentiated human neuroblastoma cells upon curcumin-induced neurite retraction. |journal=Brain Res. Mol. Brain Res. |volume=119 |issue= 1 |pages= 62–72 |year= 2004 |pmid= 14597230 |doi=10.1016/j.molbrainres.2003.08.014 |display-authors=etal}}
*{{cite journal  | author=Yamakami M, Yoshimori T, Yokosawa H |title=Tom1, a VHS domain-containing protein, interacts with tollip, ubiquitin, and clathrin. |journal=J. Biol. Chem. |volume=278 |issue= 52 |pages= 52865-72 |year= 2004 |pmid= 14563850 |doi= 10.1074/jbc.M306740200 }}
*{{cite journal  |vauthors=Li Q, Südhof TC |title=Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1. |journal=J. Biol. Chem. |volume=279 |issue= 11 |pages= 10542–50 |year= 2004 |pmid= 14699153 |doi= 10.1074/jbc.M310001200 }}
*{{cite journal  | author=Adlerz L, Beckman M, Holback S, ''et al.'' |title=Accumulation of the amyloid precursor-like protein APLP2 and reduction of APLP1 in retinoic acid-differentiated human neuroblastoma cells upon curcumin-induced neurite retraction. |journal=Brain Res. Mol. Brain Res. |volume=119 |issue= 1 |pages= 62-72 |year= 2004 |pmid= 14597230 |doi=  }}
*{{cite journal  |vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Li Q, Südhof TC |title=Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1. |journal=J. Biol. Chem. |volume=279 |issue= 11 |pages= 10542-50 |year= 2004 |pmid= 14699153 |doi= 10.1074/jbc.M310001200 }}
*{{cite journal  |vauthors=Eggert S, Paliga K, Soba P |title=The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation. |journal=J. Biol. Chem. |volume=279 |issue= 18 |pages= 18146–56 |year= 2004 |pmid= 14970212 |doi= 10.1074/jbc.M311601200 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Eggert S, Paliga K, Soba P, ''et al.'' |title=The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation. |journal=J. Biol. Chem. |volume=279 |issue= 18 |pages= 18146-56 |year= 2004 |pmid= 14970212 |doi= 10.1074/jbc.M311601200 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{gene-19-stub}}
{{WikiDoc Sources}}

Latest revision as of 18:08, 29 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Amyloid-like protein 1, also known as APLP1, is a protein that in humans is encoded by the APLP1 gene.[1][2] APLP1 along with APLP2 are important modulators of glucose and insulin homeostasis.[3]

Function

This gene encodes a member of the highly conserved amyloid precursor protein gene family. The encoded protein is a membrane-associated glycoprotein that is cleaved by secretases in a manner similar to amyloid beta A4 precursor protein cleavage. This cleavage liberates an intracellular cytoplasmic fragment that may act as a transcriptional activator. The encoded protein may also play a role in synaptic maturation during cortical development. Alternatively spliced transcript variants encoding different isoforms have been described.[1]

APLP1 and APLP2 double knockout mice display hypoglycemia and hyperinsulinemia indicating that these two proteins are important modulators of glucose and insulin homeostasis.[3]

References

  1. ↑ 1.0 1.1 "Entrez Gene: APLP1 amyloid beta (A4) precursor-like protein 1".
  2. ↑ Wasco W, Brook JD, Tanzi RE (January 1993). "The amyloid precursor-like protein (APLP) gene maps to the long arm of human chromosome 19". Genomics. 15 (1): 237–9. doi:10.1006/geno.1993.1047. PMID 8432545.
  3. ↑ 3.0 3.1 Needham BE, Wlodek ME, Ciccotosto GD, Fam BC, Masters CL, Proietto J, Andrikopoulos S, Cappai R (June 2008). "Identification of the Alzheimer's disease amyloid precursor protein (APP) and its homologue APLP2 as essential modulators of glucose and insulin homeostasis and growth". J. Pathol. 215 (2): 155–63. doi:10.1002/path.2343. PMID 18393365.

External links

Further reading

  • Bayer TA, Cappai R, Masters CL, et al. (2000). "It all sticks together--the APP-related family of proteins and Alzheimer's disease". Mol. Psychiatry. 4 (6): 524–8. doi:10.1038/sj.mp.4000552. PMID 10578233.
  • Kim TW, Wu K, Xu JL, et al. (1996). "Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density". Brain Res. Mol. Brain Res. 32 (1): 36–44. doi:10.1016/0169-328X(95)00328-P. PMID 7494461.
  • Bush AI, Pettingell WH, de Paradis M, et al. (1994). "The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily". J. Biol. Chem. 269 (43): 26618–21. PMID 7929392.
  • Wasco W, Brook JD, Tanzi RE (1993). "The amyloid precursor-like protein (APLP) gene maps to the long arm of human chromosome 19". Genomics. 15 (1): 237–9. doi:10.1006/geno.1993.1047. PMID 8432545.
  • Bressler SL, Gray MD, Sopher BL, et al. (1997). "cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein". Hum. Mol. Genet. 5 (10): 1589–98. doi:10.1093/hmg/5.10.1589. PMID 8894693.
  • Paliga K, Peraus G, Kreger S, et al. (1998). "Human amyloid precursor-like protein 1--cDNA cloning, ectopic expression in COS-7 cells and identification of soluble forms in the cerebrospinal fluid". Eur. J. Biochem. 250 (2): 354–63. doi:10.1111/j.1432-1033.1997.0354a.x. PMID 9428684.
  • Lenkkeri U, Kestilä M, Lamerdin J, et al. (1998). "Structure of the human amyloid-precursor-like protein gene APLP1 at 19q13.1". Hum. Genet. 102 (2): 192–6. doi:10.1007/s004390050676. PMID 9521588.
  • McNamara MJ, Ruff CT, Wasco W, et al. (1998). "Immunohistochemical and in situ analysis of amyloid precursor-like protein-1 and amyloid precursor-like protein-2 expression in Alzheimer disease and aged control brains". Brain Res. 804 (1): 45–51. doi:10.1016/S0006-8993(98)00653-2. PMID 9729270.
  • Tomita S, Ozaki T, Taru H, et al. (1999). "Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein". J. Biol. Chem. 274 (4): 2243–54. doi:10.1074/jbc.274.4.2243. PMID 9890987.
  • Homayouni R, Rice DS, Sheldon M, Curran T (1999). "Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1". J. Neurosci. 19 (17): 7507–15. PMID 10460257.
  • Simons A, Ruppert T, Schmidt C, et al. (2002). "Evidence for a copper-binding superfamily of the amyloid precursor protein". Biochemistry. 41 (30): 9310–20. doi:10.1021/bi0258647. PMID 12135352.
  • Scheinfeld MH, Ghersi E, Laky K, et al. (2003). "Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-secretase regulates transcription". J. Biol. Chem. 277 (46): 44195–201. doi:10.1074/jbc.M208110200. PMID 12228233.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Walsh DM, Fadeeva JV, LaVoie MJ, et al. (2003). "gamma-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins". Biochemistry. 42 (22): 6664–73. doi:10.1021/bi027375c. PMID 12779321.
  • Yamakami M, Yoshimori T, Yokosawa H (2004). "Tom1, a VHS domain-containing protein, interacts with tollip, ubiquitin, and clathrin". J. Biol. Chem. 278 (52): 52865–72. doi:10.1074/jbc.M306740200. PMID 14563850.
  • Adlerz L, Beckman M, Holback S, et al. (2004). "Accumulation of the amyloid precursor-like protein APLP2 and reduction of APLP1 in retinoic acid-differentiated human neuroblastoma cells upon curcumin-induced neurite retraction". Brain Res. Mol. Brain Res. 119 (1): 62–72. doi:10.1016/j.molbrainres.2003.08.014. PMID 14597230.
  • Li Q, Südhof TC (2004). "Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1". J. Biol. Chem. 279 (11): 10542–50. doi:10.1074/jbc.M310001200. PMID 14699153.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Eggert S, Paliga K, Soba P, et al. (2004). "The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation". J. Biol. Chem. 279 (18): 18146–56. doi:10.1074/jbc.M311601200. PMID 14970212.
Retrieved from "https://www.wikidoc.org/index.php?title=APLP1&oldid=1418764"