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Volumn 4, Issue 10, 1998, Pages 1177-1181

Calsenilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; PRESENILIN 1;

EID: 0031721511     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/2673     Document Type: Article
Times cited : (309)

References (22)
  • 1
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington, R, et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375, 754-760 (1995).
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1
  • 2
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease locus
    • Levy-Lahad, E. et al. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 269, 973-977 (1995).
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1
  • 3
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev, E.I. et al. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 376, 775-778 (1995).
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1
  • 4
    • 0029671219 scopus 로고    scopus 로고
    • Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3
    • Vito, P., Lacana, E. & D'Adamio, L. Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3. Science 271, 521-525 (1996).
    • (1996) Science , vol.271 , pp. 521-525
    • Vito, P.1    Lacana, E.2    D'Adamio, L.3
  • 5
    • 0029856850 scopus 로고    scopus 로고
    • Requirement of the familial Alzheimer's disease gene PS2 for apoptosis. Opposing effect of ALG-3
    • Vito, P. et al. Requirement of the familial Alzheimer's disease gene PS2 for apoptosis. Opposing effect of ALG-3. J. Biol. Chem. 271, 31025-31028 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 31025-31028
    • Vito, P.1
  • 6
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy, J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20, 154-159 (1997).
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 7
    • 0031982670 scopus 로고    scopus 로고
    • Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease
    • Mattson, M.P., Guo, Q., Furukawa, K. & Pedersen, W.A. Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease. J. Neurochem. 70, 1-14 (1998).
    • (1998) J. Neurochem. , vol.70 , pp. 1-14
    • Mattson, M.P.1    Guo, Q.2    Furukawa, K.3    Pedersen, W.A.4
  • 8
    • 12444276104 scopus 로고
    • Prediction of the coding sequences of unidentified human genes. II. the coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1
    • Nomura, N. et al. Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1, 223-229 (1994).
    • (1994) DNA Res. , vol.1 , pp. 223-229
    • Nomura, N.1
  • 9
    • 0030890399 scopus 로고    scopus 로고
    • Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells
    • Kim, T.W. et al. Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells. J. Biol. Chem. 272, 11006-11010 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 11006-11010
    • Kim, T.W.1
  • 10
    • 0025825054 scopus 로고
    • Recoverin: A calcium sensitive activator of retinal rod guanylate cyclase
    • Dizhoor, A.M. et al. Recoverin: a calcium sensitive activator of retinal rod guanylate cyclase. Science 251, 915-918 (1991).
    • (1991) Science , vol.251 , pp. 915-918
    • Dizhoor, A.M.1
  • 11
    • 0027064497 scopus 로고
    • Molecular cloning of hippocalcin, a novel calcium-binding protein of the recoverin family exclusively expressed in hippocampus
    • Kobayashi, M., Takamatsu, K., Saitoh, S., Miura, M. & Noguchi, T. Molecular cloning of hippocalcin, a novel calcium-binding protein of the recoverin family exclusively expressed in hippocampus. Biochem. Biophys. Res. Commun. 189, 511-517 (1992).
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 511-517
    • Kobayashi, M.1    Takamatsu, K.2    Saitoh, S.3    Miura, M.4    Noguchi, T.5
  • 12
    • 0028933014 scopus 로고
    • Identification of neuronal calcium sensor (NCS-1) possibly involved in the regulation of receptor phosphorylation
    • Nef, S., Fiumelli, H., de Castro, E., Raes, M.B. & Nef, P. Identification of neuronal calcium sensor (NCS-1) possibly involved in the regulation of receptor phosphorylation. J. Recept. Signal Transduct. Res. 15, 365-378 (1995).
    • (1995) J. Recept. Signal Transduct. Res. , vol.15 , pp. 365-378
    • Nef, S.1    Fiumelli, H.2    De Castro, E.3    Raes, M.B.4    Nef, P.5
  • 13
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • Kim, T.-W., Pettingell, W.H., Jung, Y.-K., Kovacs, D.M. & Tanzi, R.E. Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. Science 277, 373-376 (1997).
    • (1997) Science , vol.277 , pp. 373-376
    • Kim, T.-W.1    Pettingell, W.H.2    Jung, Y.-K.3    Kovacs, D.M.4    Tanzi, R.E.5
  • 14
    • 0030873546 scopus 로고    scopus 로고
    • Presenilins are processed by caspase-type proteases
    • Loetscher, H. et al. Presenilins are processed by caspase-type proteases. J. Biol. Chem. 272, 20655-20659 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 20655-20659
    • Loetscher, H.1
  • 15
    • 0030904751 scopus 로고    scopus 로고
    • Presenilin 1 interaction in the brain with a novel member of the Armadillo family
    • Zhou, J. et al. Presenilin 1 interaction in the brain with a novel member of the Armadillo family. Neuroreport 8, 2085-2090 (1997).
    • (1997) Neuroreport , vol.8 , pp. 2085-2090
    • Zhou, J.1
  • 16
    • 17344372115 scopus 로고    scopus 로고
    • Interaction of presenilins with the filamin family of actin-binding proteins
    • Zhang, W., Han, S.W., McKeel, D.W., Goate, A. & Wu, J.Y. Interaction of presenilins with the filamin family of actin-binding proteins. J. Neurosci. 18, 914-922 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 914-922
    • Zhang, W.1    Han, S.W.2    McKeel, D.W.3    Goate, A.4    Wu, J.Y.5
  • 17
    • 0032057279 scopus 로고    scopus 로고
    • The presenilin 2 loop domain interacts with the μ-calpain C-terminal region
    • Shinozaki, K. et al. The presenilin 2 loop domain interacts with the μ-calpain C-terminal region. Int. J. Mol. Med. 1, 797-799 (1998).
    • (1998) Int. J. Mol. Med. , vol.1 , pp. 797-799
    • Shinozaki, K.1
  • 18
    • 0032539814 scopus 로고    scopus 로고
    • Calbindin D28k blocks the proapoptotic actions of mutant presenilin 1: Reduced oxidative stress and preserved mitochondrial function
    • Guo, Q., Christakos, S., Robinson, N. & Mattson, M.P. Calbindin D28k blocks the proapoptotic actions of mutant presenilin 1: Reduced oxidative stress and preserved mitochondrial function. Proc. Natl. Acad. Sci. USA 95, 3227-3232 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3227-3232
    • Guo, Q.1    Christakos, S.2    Robinson, N.3    Mattson, M.P.4
  • 19
    • 0028207004 scopus 로고
    • Calcium regulates processing of the Alzheimer amyloid protein precursor in a protein kinase C-independent manner
    • Buxbaum, J.D., Ruefli, A.A., Parker, C.A., Cypess, A.M. & Greengard, P. Calcium regulates processing of the Alzheimer amyloid protein precursor in a protein kinase C-independent manner. Proc. Natl. Acad. Sci. USA 91, 4489-4493 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4489-4493
    • Buxbaum, J.D.1    Ruefli, A.A.2    Parker, C.A.3    Cypess, A.M.4    Greengard, P.5
  • 20
    • 0028204224 scopus 로고
    • Calcium ionophore increases amyloid beta peptide production by cultured cells
    • Querfurth, H.W. & Selkoe, D.J. Calcium ionophore increases amyloid beta peptide production by cultured cells. Biochemistry 33, 4550-4561 (1994).
    • (1994) Biochemistry , vol.33 , pp. 4550-4561
    • Querfurth, H.W.1    Selkoe, D.J.2
  • 21
    • 0030667426 scopus 로고    scopus 로고
    • Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors
    • Thinakaran, G. et al. Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors. J. Biol. Chem. 272, 28415-28422 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28415-28422
    • Thinakaran, G.1
  • 22
    • 0345055313 scopus 로고    scopus 로고
    • Increased sensitivity to mitochondrial toxin-induced apoptosis in neural cells expressing mutant presenilin-1 is linked to perturbed calcium homeostasis and enhanced oxyradical production
    • Keller, J.N., Guo, Q., Holtsberg, F.W., Bruce-Keller, A.J. & Mattson, M.P. Increased sensitivity to mitochondrial toxin-induced apoptosis in neural cells expressing mutant presenilin-1 is linked to perturbed calcium homeostasis and enhanced oxyradical production. J. Neurosci. 18, 4439-4450 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 4439-4450
    • Keller, J.N.1    Guo, Q.2    Holtsberg, F.W.3    Bruce-Keller, A.J.4    Mattson, M.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.