메뉴 건너뛰기




Volumn 2, Issue 9, 2007, Pages 1273-1282

Humanin: A potential peptide for neuroprotective therapy against Alzheimer's disease

Author keywords

Alzheimer's disease; Amyloid ; Amyloid precursor protein; cDNA library; Cell death; Humanin; Neuroprotection; Presenilin; Screening

Indexed keywords

AMYLOID BETA PROTEIN; COMPLEMENTARY DNA; HUMANIN; PRION PROTEIN;

EID: 34848874443     PISSN: 17460441     EISSN: None     Source Type: Journal    
DOI: 10.1517/17460441.2.9.1273     Document Type: Article
Times cited : (6)

References (62)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • SELKOE
    • SELKOE: Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. (2001) 81:741-766.
    • (2001) Physiol. Rev , vol.81 , pp. 741-766
  • 3
    • 0037010285 scopus 로고    scopus 로고
    • Alzheimer's disease: β-amyloid protein and tau
    • MORISHIMA-KAWASHIMA M, IHARA Y: Alzheimer's disease: β-amyloid protein and tau. J. Neurosci. Res. (2002) 70:392-401.
    • (2002) J. Neurosci. Res , vol.70 , pp. 392-401
    • MORISHIMA-KAWASHIMA, M.1    IHARA, Y.2
  • 4
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics
    • SELKOE DJ, SCHENK D: Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics. Annu. Rev. Pharmacol. Toxicol. (2003) 43:545-584.
    • (2003) Annu. Rev. Pharmacol. Toxicol , vol.43 , pp. 545-584
    • SELKOE, D.J.1    SCHENK, D.2
  • 5
    • 0028986916 scopus 로고
    • β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • BUSCIGLIO J, LORENZO A, YEH J, YANKNER B: β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron (1995) 14:879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • BUSCIGLIO, J.1    LORENZO, A.2    YEH, J.3    YANKNER, B.4
  • 6
    • 2942604376 scopus 로고    scopus 로고
    • The γ-secretase complex: Machinery for intramembrane proteolysis
    • IWATSUBO T: The γ-secretase complex: machinery for intramembrane proteolysis. Curr. Opin. Neurobiol. (2004) 14:379-383.
    • (2004) Curr. Opin. Neurobiol , vol.14 , pp. 379-383
    • IWATSUBO, T.1
  • 7
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • WALSH DM, SELKOE DJ: Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron (2004) 30:181-193.
    • (2004) Neuron , vol.30 , pp. 181-193
    • WALSH, D.M.1    SELKOE, D.J.2
  • 8
    • 0036550597 scopus 로고    scopus 로고
    • Significance of intracellular Aβ42 accumulation in Alzheimer's disease
    • TABIRA T, CHUI DH, KURODA S: Significance of intracellular Aβ42 accumulation in Alzheimer's disease. Front. Biosci. (2002) 7:A44-A49.
    • (2002) Front. Biosci , vol.7
    • TABIRA, T.1    CHUI, D.H.2    KURODA, S.3
  • 9
    • 0037013327 scopus 로고    scopus 로고
    • Intracellular amyloid-β1-42, but not extracellular soluble amyloid-β peptides, induces neuronal apoptosis
    • KIENLEN-CAMPARD P, MIOLET S, TASIAUX B, OCTAVE JN: Intracellular amyloid-β1-42, but not extracellular soluble amyloid-β peptides, induces neuronal apoptosis. J. Biol. Chem. (2002) 277:15666-15670.
    • (2002) J. Biol. Chem , vol.277 , pp. 15666-15670
    • KIENLEN-CAMPARD, P.1    MIOLET, S.2    TASIAUX, B.3    OCTAVE, J.N.4
  • 10
    • 28844456475 scopus 로고    scopus 로고
    • The development of anti-amyloid therapy for Alzheimer's disease
    • AISEN PS: The development of anti-amyloid therapy for Alzheimer's disease. CNS Drug (2005) 19:989-996.
    • (2005) CNS Drug , vol.19 , pp. 989-996
    • AISEN, P.S.1
  • 11
    • 0037010299 scopus 로고    scopus 로고
    • Death and survival of neuronal cells exposed to Alzheimer's insults
    • NIIKURA T, HASHIMOTO Y, TAJIMA H, NISHIMOTO I: Death and survival of neuronal cells exposed to Alzheimer's insults. J. Neurosci. Res. (2002) 70:380-391.
    • (2002) J. Neurosci. Res , vol.70 , pp. 380-391
    • NIIKURA, T.1    HASHIMOTO, Y.2    TAJIMA, H.3    NISHIMOTO, I.4
  • 12
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • SELKOE DJ: Alzheimer's disease is a synaptic failure. Science (2002) 298:789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • SELKOE, D.J.1
  • 13
    • 15844386159 scopus 로고    scopus 로고
    • G-protein-mediated neuronal DNA fragmentation by familial Alzheimer's disease-associated V642 mutants of APP
    • YAMATSUJI T, OKAMOTO T, TAKEDA S et al.: G-protein-mediated neuronal DNA fragmentation by familial Alzheimer's disease-associated V642 mutants of APP. Science (1996) 272:1349-1352.
    • (1996) Science , vol.272 , pp. 1349-1352
    • YAMATSUJI, T.1    OKAMOTO, T.2    TAKEDA, S.3
  • 14
    • 0034596257 scopus 로고    scopus 로고
    • NIIKURAT, MURAYAMA N, HASHIMOTO Y et al.: V6421 APP-inducible neuronal cells: a model system for investigating Alzheimer's disorders. Biochem Biophys. Res. Commun. (2000) 274:445-454.
    • NIIKURAT, MURAYAMA N, HASHIMOTO Y et al.: V6421 APP-inducible neuronal cells: a model system for investigating Alzheimer's disorders. Biochem Biophys. Res. Commun. (2000) 274:445-454.
  • 16
    • 0034602331 scopus 로고    scopus 로고
    • Multiple mechanisms underlie neurotoxicity by different types of Alzheimer's disease mutations of amyloid precursor protein
    • HASHIMOTO Y, NIIKURA T, ITO Y, NISHIMOTO I: Multiple mechanisms underlie neurotoxicity by different types of Alzheimer's disease mutations of amyloid precursor protein. J. Biol. Chem. (2000) 275:34541-34551.
    • (2000) J. Biol. Chem , vol.275 , pp. 34541-34551
    • HASHIMOTO, Y.1    NIIKURA, T.2    ITO, Y.3    NISHIMOTO, I.4
  • 17
    • 0030042249 scopus 로고    scopus 로고
    • Expression of V642 APP mutant causes cellular apoptosis as Alzheimer trait-linked phenotype
    • YAMATSUJI T, OKAMOTO T, TAKEDA S, MURAYAMA Y, YANAKA N, NISHIMOTO I: Expression of V642 APP mutant causes cellular apoptosis as Alzheimer trait-linked phenotype. EMBO J (1996) 15:498-509.
    • (1996) EMBO J , vol.15 , pp. 498-509
    • YAMATSUJI, T.1    OKAMOTO, T.2    TAKEDA, S.3    MURAYAMA, Y.4    YANAKA, N.5    NISHIMOTO, I.6
  • 18
    • 0035869351 scopus 로고    scopus 로고
    • Insulin-like growth factor I (IGF-I) protects cells from apoptosis by Alzheimer's V6421 mutant APP through IGF-I receptor in an IGF-binding protein-sensitive manner
    • NIIKURA T, HASHIMOTO Y, OKAMOTO T et al.: Insulin-like growth factor I (IGF-I) protects cells from apoptosis by Alzheimer's V6421 mutant APP through IGF-I receptor in an IGF-binding protein-sensitive manner. J. Neurosci. (2001) 21:1902-1910.
    • (2001) J. Neurosci , vol.21 , pp. 1902-1910
    • NIIKURA, T.1    HASHIMOTO, Y.2    OKAMOTO, T.3
  • 19
    • 0036488129 scopus 로고    scopus 로고
    • Neurotoxic mechanisms triggered by Alzheimer's disease-linked mutant M146L presenilin 1: Involvement of NO synthase via a novel pertussis toxin target
    • HASHIMOTO Y, ITO Y, ARAKAWA E et al.: Neurotoxic mechanisms triggered by Alzheimer's disease-linked mutant M146L presenilin 1: involvement of NO synthase via a novel pertussis toxin target. J. Neurochem. (2002) 80:426-437.
    • (2002) J. Neurochem , vol.80 , pp. 426-437
    • HASHIMOTO, Y.1    ITO, Y.2    ARAKAWA, E.3
  • 21
    • 0842312970 scopus 로고    scopus 로고
    • Amino- and carboxyl-terminal mutants of presenilin 1 cause neuronal cell death through distinct toxic mechanisms: Study of 27 different presenilin 1 mutants
    • HASHIMOTO Y, TSUKAMOTO E, NIIKURA T et al.: Amino- and carboxyl-terminal mutants of presenilin 1 cause neuronal cell death through distinct toxic mechanisms: study of 27 different presenilin 1 mutants. J. Neurosci. Res. (2004) 75:417-428.
    • (2004) J. Neurosci. Res , vol.75 , pp. 417-428
    • HASHIMOTO, Y.1    TSUKAMOTO, E.2    NIIKURA, T.3
  • 22
    • 3442889339 scopus 로고    scopus 로고
    • Cytotoxic mechanisms by M239V presenilin 2, a little-analyzed Alzheimer's disease-causative mutant
    • ABE Y, HASHIMOTO Y, TOMITA Y et al.: Cytotoxic mechanisms by M239V presenilin 2, a little-analyzed Alzheimer's disease-causative mutant. J. Neurosci. Res. (2004) 77:583-595.
    • (2004) J. Neurosci. Res , vol.77 , pp. 583-595
    • ABE, Y.1    HASHIMOTO, Y.2    TOMITA, Y.3
  • 23
    • 10544224542 scopus 로고    scopus 로고
    • Participation of presenilin 2 in apoptosis: Enhanced basal activity conferred by an Alzheimer mutation
    • WOLOZIN B, IWASAKI K, VITO P et al.: Participation of presenilin 2 in apoptosis: enhanced basal activity conferred by an Alzheimer mutation. Science (1996) 274:1710-1713.
    • (1996) Science , vol.274 , pp. 1710-1713
    • WOLOZIN, B.1    IWASAKI, K.2    VITO, P.3
  • 25
  • 26
    • 0032895651 scopus 로고    scopus 로고
    • Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation
    • CHUI DH, TANAHASHI H, OZAWA K et al.: Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation. Nat. Med. (1999) 5:560-564.
    • (1999) Nat. Med , vol.5 , pp. 560-564
    • CHUI, D.H.1    TANAHASHI, H.2    OZAWA, K.3
  • 27
    • 0033153450 scopus 로고    scopus 로고
    • Superoxide mediates the cell-death-enhancing action of presenilin-1 mutations
    • GUO Q, FU W, HOLTSBERG FW, STEINER SM, MATTSON MP: Superoxide mediates the cell-death-enhancing action of presenilin-1 mutations. J. Neurosci. Res. (1999) 56:457-470.
    • (1999) J. Neurosci. Res , vol.56 , pp. 457-470
    • GUO, Q.1    FU, W.2    HOLTSBERG, F.W.3    STEINER, S.M.4    MATTSON, M.P.5
  • 29
    • 34848885554 scopus 로고    scopus 로고
    • Neuronal cell death in Alzheimer's disease and its potential therapy with neuroprotective factors
    • Welsh EM Ed, Nova Science Publishers, New York
    • NIIKURA T, NISHIMOTO I: Neuronal cell death in Alzheimer's disease and its potential therapy with neuroprotective factors. In: Frontiers in Alzheimer's Disease Research. Welsh EM (Ed.), Nova Science Publishers, New York (2006):55-96.
    • (2006) Frontiers in Alzheimer's Disease Research , pp. 55-96
    • NIIKURA, T.1    NISHIMOTO, I.2
  • 30
    • 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, DADAMIO L: Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3. Science (1996) 271:521-525.
    • (1996) Science , vol.271 , pp. 521-525
    • VITO, P.1    LACANA, E.2    DADAMIO, L.3
  • 31
    • 0031080175 scopus 로고    scopus 로고
    • Functional cloning of genes involved in T-cell receptor-induced programmed cell death
    • D'ADAMIO L, LACANA E, VITO P: Functional cloning of genes involved in T-cell receptor-induced programmed cell death. Semin. Immunol. (1997) 9:17-23.
    • (1997) Semin. Immunol , vol.9 , pp. 17-23
    • D'ADAMIO, L.1    LACANA, E.2    VITO, P.3
  • 33
  • 34
    • 0037809240 scopus 로고    scopus 로고
    • The C-terminal fragment of presenilin 2 triggers p53-mediated staurosporine-induced apoptosis, a function independent of the presenilinase-derived N-terminal counterpart
    • ALVES DA COSTA C, MATTSON MP, ANCOLIO K, CHECLER F: The C-terminal fragment of presenilin 2 triggers p53-mediated staurosporine-induced apoptosis, a function independent of the presenilinase-derived N-terminal counterpart. J. Biol. Chem. (2003) 278:12064-12069.
    • (2003) J. Biol. Chem , vol.278 , pp. 12064-12069
    • ALVES DA COSTA, C.1    MATTSON, M.P.2    ANCOLIO, K.3    CHECLER, F.4
  • 35
    • 31544445520 scopus 로고    scopus 로고
    • Inhibition of cyclooxygenase as potential novel therapeutic strategy in N141I presenilin-2 familial Alzheimer's disease
    • QIN W, PENG Y, KSIEZAK-REDING H et al.: Inhibition of cyclooxygenase as potential novel therapeutic strategy in N141I presenilin-2 familial Alzheimer's disease. Mol. Psychiatry (2006) 11:172-181
    • (2006) Mol. Psychiatry , vol.11 , pp. 172-181
    • QIN, W.1    PENG, Y.2    KSIEZAK-REDING, H.3
  • 36
    • 4243333514 scopus 로고    scopus 로고
    • A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer's disease genes and Aβ
    • HASHIMOTO Y, NIIKURA T, TAJIMA H et al.: A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer's disease genes and Aβ. Proc. Natl. Acad. Sci. USA (2001) 98:6336-6341.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6336-6341
    • HASHIMOTO, Y.1    NIIKURA, T.2    TAJIMA, H.3
  • 37
    • 1942533393 scopus 로고    scopus 로고
    • The Gtx homeodomain transcription factor exerts neuroprotection using its homeodomain
    • HASHIMOTO Y, TSUJI O, KANEKURA K et al.: The Gtx homeodomain transcription factor exerts neuroprotection using its homeodomain. J. Biol. Chem. (2004) 279:16767-16777.
    • (2004) J. Biol. Chem , vol.279 , pp. 16767-16777
    • HASHIMOTO, Y.1    TSUJI, O.2    KANEKURA, K.3
  • 38
    • 0013056674 scopus 로고    scopus 로고
    • Identification of essential amino acids in Humanin, a neuroprotective factor against Alzheimer's disease relevant insults
    • YAMAGISHI Y, HASHIMOTO Y, NIIKURA T, NISHIMOTO I: Identification of essential amino acids in Humanin, a neuroprotective factor against Alzheimer's disease relevant insults. Peptides (2003) 24:585-595.
    • (2003) Peptides , vol.24 , pp. 585-595
    • YAMAGISHI, Y.1    HASHIMOTO, Y.2    NIIKURA, T.3    NISHIMOTO, I.4
  • 39
    • 0034805623 scopus 로고    scopus 로고
    • Mechanisms of neuroprotection by a novel rescue factor Humanin from Swedish mutant amyloid precursor protein
    • HASHIMOTO Y, ITO Y, NIIKURA T et al.: Mechanisms of neuroprotection by a novel rescue factor Humanin from Swedish mutant amyloid precursor protein. Biochem. Biophys. Res. Commun. (2001) 283:460-468.
    • (2001) Biochem. Biophys. Res. Commun , vol.283 , pp. 460-468
    • HASHIMOTO, Y.1    ITO, Y.2    NIIKURA, T.3
  • 40
    • 0035576106 scopus 로고    scopus 로고
    • Detailed characterization of neuroprotection by a rescue factor humanin against various Alzheimer's disease-relevant insults
    • HASHIMOTO Y, NIIKURA T, ITO Y et al.: Detailed characterization of neuroprotection by a rescue factor humanin against various Alzheimer's disease-relevant insults. J. Neurosci. (2001) 21:9235-9245.
    • (2001) J. Neurosci , vol.21 , pp. 9235-9245
    • HASHIMOTO, Y.1    NIIKURA, T.2    ITO, Y.3
  • 41
    • 12444261796 scopus 로고    scopus 로고
    • Two serine residues distinctly regulate the rescue function of Humanin, an inhibiting factor of Alzheimer's disease-related neurotoxicity: Functional potentiation by isomerization and dimerization
    • TERASHITA K, HASHIMOTO Y, NIIKURA T et al.: Two serine residues distinctly regulate the rescue function of Humanin, an inhibiting factor of Alzheimer's disease-related neurotoxicity: functional potentiation by isomerization and dimerization. J. Neurochem. (2003) 85:1521-1538.
    • (2003) J. Neurochem , vol.85 , pp. 1521-1538
    • TERASHITA, K.1    HASHIMOTO, Y.2    NIIKURA, T.3
  • 42
    • 0017169386 scopus 로고
    • Synthesis and some pharmacological properties of deamino [4-threonine,8-D-arginine] vasopressin and deamino [8-D-arginine] vasopressin, highly potent and specific antidiuretic peptides, and [8-D-arginie] vasopressin and deamino-arginine-vasopressin
    • MANNING M, BALASPIRI L, MOEHRING J: Synthesis and some pharmacological properties of deamino [4-threonine,8-D-arginine] vasopressin and deamino [8-D-arginine] vasopressin, highly potent and specific antidiuretic peptides, and [8-D-arginie] vasopressin and deamino-arginine-vasopressin. J. Med. Chem. (1976) 19:842-845.
    • (1976) J. Med. Chem , vol.19 , pp. 842-845
    • MANNING, M.1    BALASPIRI, L.2    MOEHRING, J.3
  • 43
    • 0027477463 scopus 로고
    • Structural alternations in the peptide backbone of β-amyloid core protein may account for its deposition and stability in Alzheimer's disease
    • ROHER AE, LOWENSON JD, CLARKE S et al.: Structural alternations in the peptide backbone of β-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J. Biol. Chem. (1993) 268:3072-3038.
    • (1993) J. Biol. Chem , vol.268 , pp. 3072-3038
    • ROHER, A.E.1    LOWENSON, J.D.2    CLARKE, S.3
  • 44
    • 0033539510 scopus 로고    scopus 로고
    • Serine racemase: A glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission
    • WOLOSKER H, BLACKSHAW S, SNYDER SH: Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission. Proc. Natl. Acad. Sci. USA (1999) 96:13409-13414.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13409-13414
    • WOLOSKER, H.1    BLACKSHAW, S.2    SNYDER, S.H.3
  • 45
    • 13844299455 scopus 로고    scopus 로고
    • Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity
    • BENAKI D, ZIKOS C, EVANGELOU A et al.: Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity. Biochem. Biophys. Res. Commun. (2005) 329:152-160.
    • (2005) Biochem. Biophys. Res. Commun , vol.329 , pp. 152-160
    • BENAKI, D.1    ZIKOS, C.2    EVANGELOU, A.3
  • 46
    • 33748565003 scopus 로고    scopus 로고
    • Solution structure of Ser14Gly-humanin, a potent rescue factor against neuronal cell death in Alzheimer's disease
    • BENAKI D, ZIKOS C, EVANGELOU A et al.: Solution structure of Ser14Gly-humanin, a potent rescue factor against neuronal cell death in Alzheimer's disease. Biochem. Biophys. Res. Commun. (2006) 349:634-642.
    • (2006) Biochem. Biophys. Res. Commun , vol.349 , pp. 634-642
    • BENAKI, D.1    ZIKOS, C.2    EVANGELOU, A.3
  • 47
    • 33750072017 scopus 로고    scopus 로고
    • The secondary structure analysis of a potent Ser14Gly analog of antiAlzheimer peptide, Humanin, by circular dichroism
    • ARAKAWA T, NIIKURA T, TAJIMA H, KITA Y: The secondary structure analysis of a potent Ser14Gly analog of antiAlzheimer peptide, Humanin, by circular dichroism. J. Pept. Sci. (2006) 12:639-642.
    • (2006) J. Pept. Sci , vol.12 , pp. 639-642
    • ARAKAWA, T.1    NIIKURA, T.2    TAJIMA, H.3    KITA, Y.4
  • 48
    • 26444463390 scopus 로고    scopus 로고
    • Involvement of tyrosine kinases and STAT3 in Humanin-mediated neuroprotection
    • HASHIMOTO Y, SUZUKI H, AISO S, NIIKURA T, NISHIMOTO I, MATSUOKA M: Involvement of tyrosine kinases and STAT3 in Humanin-mediated neuroprotection. Life Sci. (2005) 77:3092-3104.
    • (2005) Life Sci , vol.77 , pp. 3092-3104
    • HASHIMOTO, Y.1    SUZUKI, H.2    AISO, S.3    NIIKURA, T.4    NISHIMOTO, I.5    MATSUOKA, M.6
  • 49
    • 0032742013 scopus 로고    scopus 로고
    • Utilization of two seven-transmembrane, G protein-coupled receptors, formyl peptide receptor-like 1 and formyl peptide receptor, by the synthetic hexapeptide WKYMVm for human phagocyte activation
    • LE Y, GONG Y, LI B et al.: Utilization of two seven-transmembrane, G protein-coupled receptors, formyl peptide receptor-like 1 and formyl peptide receptor, by the synthetic hexapeptide WKYMVm for human phagocyte activation. J. Immunol. (1999) 163:6777-6784.
    • (1999) J. Immunol , vol.163 , pp. 6777-6784
    • LE, Y.1    GONG, Y.2    LI, B.3
  • 50
    • 4744351478 scopus 로고    scopus 로고
    • HARADA M, HABATA Y, HOSOYA M et al.: N-Formylated humanin activates both formyl peptide receptor-like 1 and 2. Biochem. Biophys. Res. Commun. (2004) 324:255-261.
    • HARADA M, HABATA Y, HOSOYA M et al.: N-Formylated humanin activates both formyl peptide receptor-like 1 and 2. Biochem. Biophys. Res. Commun. (2004) 324:255-261.
  • 51
    • 33646893677 scopus 로고    scopus 로고
    • Tubulin is the target binding site for NAP-related peptides: ADNF-9, D-NAP and D-SAL
    • HOLSTER-COCHAV M, DIVINSIG I, GOZES I: Tubulin is the target binding site for NAP-related peptides: ADNF-9, D-NAP and D-SAL. J. Mol. Neurosci. (2006) 28:303-307.
    • (2006) J. Mol. Neurosci , vol.28 , pp. 303-307
    • HOLSTER-COCHAV, M.1    DIVINSIG, I.2    GOZES, I.3
  • 52
    • 20144387217 scopus 로고    scopus 로고
    • A humanin derivative, S14G-HN, prevents amyloid-β-induced memory impairment in mice
    • TAJIMA H, KAWASUMI M, CHIBA T et al.: A humanin derivative, S14G-HN, prevents amyloid-β-induced memory impairment in mice. J. Neurosci. Res. (2005) 79:714-723.
    • (2005) J. Neurosci. Res , vol.79 , pp. 714-723
    • TAJIMA, H.1    KAWASUMI, M.2    CHIBA, T.3
  • 53
    • 0035678839 scopus 로고    scopus 로고
    • Gly(14)]-Humanin improved the learning and memory impairment induced by scopolamine in vivo
    • MAMIYA T, UKAI M: [Gly(14)]-Humanin improved the learning and memory impairment induced by scopolamine in vivo. Br. J. Pharmacol. (2001) 134:1597-1599.
    • (2001) Br. J. Pharmacol , vol.134 , pp. 1597-1599
    • MAMIYA, T.1    UKAI, M.2
  • 54
    • 6944252056 scopus 로고    scopus 로고
    • Effect of humanin analogues on experimentally induced impairment of spatial memory in rats
    • KREJCOVA G, PATOCKA J, SLANINOVA J: Effect of humanin analogues on experimentally induced impairment of spatial memory in rats. J. Pept. Sci. (2004) 10:636-639.
    • (2004) J. Pept. Sci , vol.10 , pp. 636-639
    • KREJCOVA, G.1    PATOCKA, J.2    SLANINOVA, J.3
  • 55
    • 0242268394 scopus 로고    scopus 로고
    • Interaction between the Alzheimer's survival peptide humanin and insulin-like growth factor-binding protein 3 regulates cell survival and apoptosis
    • IKONEN M, LIU B, HASHIMOTO Y et al.: Interaction between the Alzheimer's survival peptide humanin and insulin-like growth factor-binding protein 3 regulates cell survival and apoptosis. Proc. Natl. Acad. Sci. USA (2003) 100:13042-13047.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13042-13047
    • IKONEN, M.1    LIU, B.2    HASHIMOTO, Y.3
  • 56
    • 0347683451 scopus 로고    scopus 로고
    • Cellular internalization of insulin-like growth factor binding protein-3: Distinct endocytic pathways facilitate reuptake and nuclear localization
    • LEE KW, LIU B, MA L et al.: Cellular internalization of insulin-like growth factor binding protein-3: distinct endocytic pathways facilitate reuptake and nuclear localization. J. Biol. Chem. (2004) 279:469-476.
    • (2004) J. Biol. Chem , vol.279 , pp. 469-476
    • LEE, K.W.1    LIU, B.2    MA, L.3
  • 58
    • 0037262465 scopus 로고    scopus 로고
    • Humanin rescues human cerebrovascular smooth muscle cells from Aβ-induced toxicity
    • JUNG SS, VAN NOSTRAND WE: Humanin rescues human cerebrovascular smooth muscle cells from Aβ-induced toxicity. J. Neurochem. (2003) 84:266-272.
    • (2003) J. Neurochem , vol.84 , pp. 266-272
    • JUNG, S.S.1    VAN NOSTRAND, W.E.2
  • 59
    • 33745626174 scopus 로고    scopus 로고
    • Anti-apoptotic factor humanin is expressed in the testis and prevents cell-death in leydig cells during the first wave of spermatogenesis
    • COLON E, STRAND ML, CARLSSON-SKWIRUT C et al.: Anti-apoptotic factor humanin is expressed in the testis and prevents cell-death in leydig cells during the first wave of spermatogenesis. J. Cell. Physiol. (2006) 208:373-385.
    • (2006) J. Cell. Physiol , vol.208 , pp. 373-385
    • COLON, E.1    STRAND, M.L.2    CARLSSON-SKWIRUT, C.3
  • 60
    • 24644445576 scopus 로고    scopus 로고
    • Humanin delays apoptosis in K562 cells by downregulation of P38 MAP kinase
    • WANG D, LI H, YUAN H et al.: Humanin delays apoptosis in K562 cells by downregulation of P38 MAP kinase. Apoptosis (2005) 10:963-971.
    • (2005) Apoptosis , vol.10 , pp. 963-971
    • WANG, D.1    LI, H.2    YUAN, H.3
  • 61
    • 0038485614 scopus 로고    scopus 로고
    • Humanin peptide suppresses apoptosis by interfering with Bax activation
    • GUO B, ZHAI D, CABEZAS E et al.: Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature (2003) 423:456-461.
    • (2003) Nature , vol.423 , pp. 456-461
    • GUO, B.1    ZHAI, D.2    CABEZAS, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.