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Items: 1 to 20 of 107

1.

FE65 regulates and interacts with the Bloom syndrome protein in dynamic nuclear spheres - potential relevance to Alzheimer's disease.

Schrötter A, Mastalski T, Nensa FM, Neumann M, Loosse C, Pfeiffer K, Magraoui FE, Platta HW, Erdmann R, Theiss C, Uszkoreit J, Eisenacher M, Meyer HE, Marcus K, Müller T.

J Cell Sci. 2013 Jun 1;126(Pt 11):2480-92. doi: 10.1242/jcs.121004.

3.

Expression of the Fe65 adapter protein in adult and developing mouse brain.

Kesavapany S, Banner SJ, Lau KF, Shaw CE, Miller CC, Cooper JD, McLoughlin DM.

Neuroscience. 2002;115(3):951-60.

PMID:
12435432
4.
5.

Alphabeta hinders nuclear targeting of AICD and Fe65 in primary neuronal cultures.

Henriques AG, Vieira SI, da Cruz e Silva EF, da Cruz e Silva OA.

J Mol Neurosci. 2009 Sep;39(1-2):248-55. doi: 10.1007/s12031-009-9192-9.

6.

Phosphorylation of LRP1 regulates the interaction with Fe65.

Klug W, Dietl A, Simon B, Sinning I, Wild K.

FEBS Lett. 2011 Oct 20;585(20):3229-35. doi: 10.1016/j.febslet.2011.09.028.

7.

Amyloid precursor protein binding protein Fe65 is cleaved by caspases during DNA damage-induced apoptosis.

Saeki K, Nose Y, Hirao N, Takasawa R, Tanuma S.

Biol Pharm Bull. 2011;34(2):290-4.

8.

Amyloid beta a4 precursor protein-binding family B member 1 (FE65) interactomics revealed synaptic vesicle glycoprotein 2A (SV2A) and sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) as new binding proteins in the human brain.

Nensa FM, Neumann MH, Schrötter A, Przyborski A, Mastalski T, Susdalzew S, Looβe C, Helling S, El Magraoui F, Erdmann R, Meyer HE, Uszkoreit J, Eisenacher M, Suh J, Guénette SY, Röhner N, Kögel D, Theiss C, Marcus K, Müller T.

Mol Cell Proteomics. 2014 Feb;13(2):475-88. doi: 10.1074/mcp.M113.029280.

9.

Fe65 stimulates proteolytic liberation of the beta-amyloid precursor protein intracellular domain.

Wiley JC, Smith EA, Hudson MP, Ladiges WC, Bothwell M.

J Biol Chem. 2007 Nov 16;282(46):33313-25.

10.
11.

Essential roles for Fe65, Alzheimer amyloid precursor-binding protein, in the cellular response to DNA damage.

Minopoli G, Stante M, Napolitano F, Telese F, Aloia L, De Felice M, Di Lauro R, Pacelli R, Brunetti A, Zambrano N, Russo T.

J Biol Chem. 2007 Jan 12;282(2):831-5.

12.

Regulation of FE65 nuclear translocation and function by amyloid beta-protein precursor in osmotically stressed cells.

Nakaya T, Kawai T, Suzuki T.

J Biol Chem. 2008 Jul 4;283(27):19119-31. doi: 10.1074/jbc.M801827200.

13.

Nuclear spheres modulate the expression of BEST1 and GADD45G.

Loosse C, Pawlas M, Bukhari HS, Maghnouj A, Hahn S, Marcus K, Müller T.

Cell Signal. 2016 Jan;28(1):100-9. doi: 10.1016/j.cellsig.2015.10.019.

PMID:
26521045
14.

Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein, blocks cell cycle progression by down-regulating thymidylate synthase expression.

Bruni P, Minopoli G, Brancaccio T, Napolitano M, Faraonio R, Zambrano N, Hansen U, Russo T.

J Biol Chem. 2002 Sep 20;277(38):35481-8.

15.

Phosphorylation of a tyrosine in the amyloid-beta protein precursor intracellular domain inhibits Fe65 binding and signaling.

Zhou D, Zambrano N, Russo T, D'Adamio L.

J Alzheimers Dis. 2009;16(2):301-7. doi: 10.3233/JAD-2009-0970.

PMID:
19221419
16.

The amyloid precursor protein intracellular domain(AICD) disrupts actin dynamics and mitochondrial bioenergetics.

Ward MW, Concannon CG, Whyte J, Walsh CM, Corley B, Prehn JH.

J Neurochem. 2010 Apr;113(1):275-84.

PMID:
20405578
17.

Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins.

Zambrano N, Buxbaum JD, Minopoli G, Fiore F, De Candia P, De Renzis S, Faraonio R, Sabo S, Cheetham J, Sudol M, Russo T.

J Biol Chem. 1997 Mar 7;272(10):6399-405.

19.

Megalin interacts with APP and the intracellular adapter protein FE65 in neurons.

Alvira-Botero X, Pérez-Gonzalez R, Spuch C, Vargas T, Antequera D, Garzón M, Bermejo-Pareja F, Carro E.

Mol Cell Neurosci. 2010 Nov;45(3):306-15. doi: 10.1016/j.mcn.2010.07.005.

PMID:
20637285
20.

A ternary complex consisting of AICD, FE65, and TIP60 down-regulates Stathmin1.

Müller T, Schrötter A, Loosse C, Pfeiffer K, Theiss C, Kauth M, Meyer HE, Marcus K.

Biochim Biophys Acta. 2013 Jan;1834(1):387-94. doi: 10.1016/j.bbapap.2012.07.017.

PMID:
22902274

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