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Volumn 18, Issue 36, 2011, Pages 5554-5563

Advances in characterization of neuroprotective peptide, humanin

Author keywords

Aggregation; Disordered structure; Humanin; Liposome; Neuroprotection; sheet

Indexed keywords

HUMANIN; LIPOSOME; NEUROPROTECTIVE AGENT; ZINC;

EID: 84055189716     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/092986711798347261     Document Type: Article
Times cited : (12)

References (69)
  • 1
    • 33750082374 scopus 로고    scopus 로고
    • Early diagnostics and therapeutics for Alzheimer's disease - How early can we get there?
    • DOI 10.1586/14737175.6.9.1293
    • Monien, B.H.; Apostolova, L.G.; Bitan, G. Early diagnostics and therapeutics for Alzheimer's disease-how early can we get there? Expert Rev Neurother, 2006, 6(9), 1293-1306. (Pubitemid 44580952)
    • (2006) Expert Review of Neurotherapeutics , vol.6 , Issue.9 , pp. 1293-1306
    • Monien, B.H.1    Apostolova, L.G.2    Bitan, G.3
  • 2
    • 0011162190 scopus 로고
    • Selective loss of central cholinergic neurons in Alzheimer's disease
    • Davies, P.; Maloney, A.J. Selective loss of central cholinergic neurons in Alzheimer's disease. Lancet, 1976, 2(8000), 1403. (Pubitemid 8004505)
    • (1976) Lancet , vol.2 , Issue.8000 , pp. 1403
    • Davies, P.1    Maloney, A.J.F.2
  • 4
    • 0025339542 scopus 로고
    • Selective inhibition of human acetylcholinesterase by galanthamine in vitro and in vivo
    • DOI 10.1016/0024-3205(90)90429-U
    • Thomsen, T.; Kewitz, H. Selective inhibition of human acetylcholinesterase by galanthamine in vitro and in vivo. Life Sci, 1990, 46(21), 1553-1558. (Pubitemid 20177958)
    • (1990) Life Sciences , vol.46 , Issue.21 , pp. 1553-1558
    • Thomsen, T.1    Kewitz, H.2
  • 5
    • 0000545124 scopus 로고    scopus 로고
    • Structure-activity relationship of acetylcholinesterase inhibitors: Donepezil hydrochloride for treatment of Alzheimer's disease
    • Sugimoto, H. Structure-activity relationship of acetylcholinesterase inhibitors: donepezil hydrochloride for treatment of Alzheimer's disease. Pure Appl. Chem., 1999, 71, 2031-2037.
    • (1999) Pure Appl. Chem. , vol.71 , pp. 2031-2037
    • Sugimoto, H.1
  • 6
    • 56249113825 scopus 로고    scopus 로고
    • Amyloid-based therapeutics: Findings translated into novel treatments
    • Aisen, P.S. Amyloid-based therapeutics: findings translated into novel treatments. CNS Spectr, 2008, 13(10 Suppl 16), 36-38.
    • (2008) CNS Spectr , vol.13 , Issue.10 SUPPL. 16 , pp. 36-38
    • Aisen, P.S.1
  • 7
    • 79960343359 scopus 로고    scopus 로고
    • Amyloid: Little proteins, big clues
    • Schnabel, J. Amyloid: little proteins, big clues. Nature, 2011, 475(7355), S12-14.
    • (2011) Nature , vol.475 , Issue.7355
    • Schnabel, J.1
  • 8
    • 79952442060 scopus 로고    scopus 로고
    • Neuroprotective therapeutics for Alzheimer's disease: Progress and prospects
    • Palmer, A.M. Neuroprotective therapeutics for Alzheimer's disease: progress and prospects. Trends Pharmacol Sci, 2011, 32(3), 141-147.
    • (2011) Trends Pharmacol Sci , vol.32 , Issue.3 , pp. 141-147
    • Palmer, A.M.1
  • 11
    • 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.; Sudo, H.; Hata, M.; Arakawa, E.; Abe, Y.; Kita, Y.; Nishimoto, I. Detailed characterization of neuroprotection by a rescue factor humanin against various Alzheimer's disease-relevant insults. J Neurosci, 2001, 21(23), 9235-9245. (Pubitemid 33096867)
    • (2001) Journal of Neuroscience , vol.21 , Issue.23 , pp. 9235-9245
    • Hashimoto, Y.1    Niikura, T.2    Ito, Y.3    Sudo, H.4    Hata, M.5    Arakawa, E.6    Abe, Y.7    Kita, Y.8    Nishimoto, I.9
  • 12
    • 0035678839 scopus 로고    scopus 로고
    • 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(8), 1597-1599. (Pubitemid 34038091)
    • (2001) British Journal of Pharmacology , vol.134 , Issue.8 , pp. 1597-1599
    • Mamiya, T.1    Ukai, M.2
  • 13
    • 0037035593 scopus 로고    scopus 로고
    • Humanin inhibits cell death of serum-deprived PC12h cells
    • Kariya, S.; Takahashi, N.; Ooba, N.; Kawahara, M.; Nakayama, H.; Ueno, S. Humanin inhibits cell death of serum-deprived PC12h cells. Neuroreport, 2002, 13(6), 903-907. (Pubitemid 34492924)
    • (2002) NeuroReport , vol.13 , Issue.6 , pp. 903-907
    • Kariya, S.1    Takahashi, N.2    Ooba, N.3    Kawahara, M.4    Nakayama, H.5    Ueno, S.6
  • 14
    • 34848874443 scopus 로고    scopus 로고
    • Humanin: A potential peptide for neuroprotective therapy against Alzheimer's disease
    • DOI 10.1517/17460441.2.9.1273
    • Niikura, T. Humanin, a potential peptide for neuroprotective therapy against Alzheimer's disease. Expert Opinion on Drug Discovery, 2007, 2, 1273-1282. (Pubitemid 47496484)
    • (2007) Expert Opinion on Drug Discovery , vol.2 , Issue.9 , pp. 1273-1282
    • Niikura, T.1
  • 16
    • 0038485614 scopus 로고    scopus 로고
    • Humanin peptide suppresses apoptosis by interfering with Bax activation
    • DOI 10.1038/nature01627
    • Guo, B.; Zhai, D.; Cabezas, E.; Welsh, K.; Nouraini, S.; Satterthwait, A.C.; Reed, J.C. Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature, 2003, 423(6938), 456-461. (Pubitemid 36626999)
    • (2003) Nature , vol.423 , Issue.6938 , pp. 456-461
    • Guo, B.1    Zhai, D.2    Cabezas, E.3    Welsh, K.4    Nouraini, S.5    Satterthwait, A.C.6    Reed, J.C.7
  • 18
    • 0037262465 scopus 로고    scopus 로고
    • Humanin rescues human cerebrovascular smooth muscle cells from Aβ-induced toxicity
    • DOI 10.1046/j.1471-4159.2003.01524.x
    • Jung, S.S.; Van Nostrand, W.E. Humanin rescues human cerebrovascular smooth muscle cells from Abeta-induced toxicity. J Neurochem, 2003, 84(2), 266-272. (Pubitemid 36182268)
    • (2003) Journal of Neurochemistry , vol.84 , Issue.2 , pp. 266-272
    • Jung, S.S.1    Van Nostrand, W.E.2
  • 19
    • 18344390443 scopus 로고    scopus 로고
    • Humanin detected in skeletal muscles of MELAS patients: A possible new therapeutic agent
    • DOI 10.1007/s00401-004-0965-5
    • Kariya, S.; Hirano, M.; Furiya, Y.; Sugie, K.; Ueno, S. Humanin detected in skeletal muscles of MELAS patients: a possible new therapeutic agent. Acta Neuropathol, 2005, 109(4), 367-372. (Pubitemid 40637308)
    • (2005) Acta Neuropathologica , vol.109 , Issue.4 , pp. 367-372
    • Kariya, S.1    Hirano, M.2    Furiya, Y.3    Sugie, K.4    Ueno, S.5
  • 21
    • 48949104380 scopus 로고    scopus 로고
    • Neuroprotective effect of humanin on cerebral ischemia/reperfusion injury is mediated by a PI3K/Akt pathway
    • Xu, X.; Chua, C.C.; Gao, J.; Chua, K.W.; Wang, H.; Hamdy, R.C.; Chua, B.H. Neuroprotective effect of humanin on cerebral ischemia/reperfusion injury is mediated by a PI3K/Akt pathway. Brain Res, 2008, 1227, 12-18.
    • (2008) Brain Res , vol.1227 , pp. 12-18
    • Xu, X.1    Chua, C.C.2    Gao, J.3    Chua, K.W.4    Wang, H.5    Hamdy, R.C.6    Chua, B.H.7
  • 23
    • 76249131322 scopus 로고    scopus 로고
    • The neurosurvival factor Humanin inhibits beta-cell apoptosis via signal transducer and activator of transcription 3 activation and delays and ameliorates diabetes in nonobese diabetic mice
    • Hoang, P.T.; Park, P.; Cobb, L.J.; Paharkova-Vatchkova, V.; Hakimi, M.; Cohen, P.; Lee, K.W. The neurosurvival factor Humanin inhibits beta-cell apoptosis via signal transducer and activator of transcription 3 activation and delays and ameliorates diabetes in nonobese diabetic mice. Metabolism: clinical and experimental, 2010, 59(3), 343-349.
    • (2010) Metabolism: Clinical and Experimental , vol.59 , Issue.3 , pp. 343-349
    • Hoang, P.T.1    Park, P.2    Cobb, L.J.3    Paharkova-Vatchkova, V.4    Hakimi, M.5    Cohen, P.6    Lee, K.W.7
  • 24
    • 79251577369 scopus 로고    scopus 로고
    • A humanin derivative reduces amyloid beta accumulation and ameliorates memory deficit in triple transgenic mice
    • Niikura, T.; Sidahmed, E.; Hirata-Fukae, C.; Aisen, P.S.; Matsuoka, Y. A humanin derivative reduces amyloid beta accumulation and ameliorates memory deficit in triple transgenic mice. PLoS One, 2011, 6(1), e16259.
    • (2011) PLoS One , vol.6 , Issue.1
    • Niikura, T.1    Sidahmed, E.2    Hirata-Fukae, C.3    Aisen, P.S.4    Matsuoka, Y.5
  • 25
  • 26
    • 33749020532 scopus 로고    scopus 로고
    • Humanin is a novel neuroprotective agent against stroke
    • DOI 10.1161/01.STR.0000242772.94277.1f, PII 0000767020061000000037
    • Xu, X.; Chua, C.C.; Gao, J.; Hamdy, R.C.; Chua, B.H. Humanin is a novel neuroprotective agent against stroke. Stroke, 2006, 37(10), 2613-2619. (Pubitemid 44454687)
    • (2006) Stroke , vol.37 , Issue.10 , pp. 2613-2619
    • Xu, X.1    Chua, C.C.2    Gao, J.3    Hamdy, R.C.4    Chua, B.H.L.5
  • 28
    • 0036673025 scopus 로고    scopus 로고
    • A novel rat gene encoding a Humanin-like peptide endowed with broad neuroprotective activity
    • Caricasole, A.; Bruno, V.; Cappuccio, I.; Melchiorri, D.; Copani, A.; Nicoletti, F. A novel rat gene encoding a Humanin-like peptide endowed with broad neuroprotective activity. FASEB J, 2002, 16(10), 1331-1333.
    • (2002) FASEB J , vol.16 , Issue.10 , pp. 1331-1333
    • Caricasole, A.1    Bruno, V.2    Cappuccio, I.3    Melchiorri, D.4    Copani, A.5    Nicoletti, F.6
  • 29
    • 0037166058 scopus 로고    scopus 로고
    • Evidence for in vivo production of Humanin peptide, a neuroprotective factor against Alzheimer's disease-related insults
    • DOI 10.1016/S0304-3940(02)00199-4, PII S0304394002001994
    • Tajima, H.; Niikura, T.; Hashimoto, Y.; Ito, Y.; Kita, Y.; Terashita, K.; Yamazaki, K.; Koto, A.; Aiso, S.; Nishimoto, I. Evidence for in vivo production of Humanin peptide, a neuroprotective factor against Alzheimer's disease-related insults. Neurosci Lett, 2002, 324(3), 227-231. (Pubitemid 34493875)
    • (2002) Neuroscience Letters , vol.324 , Issue.3 , pp. 227-231
    • Tajima, H.1    Niikura, T.2    Hashimoto, Y.3    Ito, Y.4    Kita, Y.5    Terashita, K.6    Yamazaki, K.7    Koto, A.8    Aiso, S.9    Nishimoto, I.10
  • 30
    • 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
    • DOI 10.1002/jcp.20672
    • Colon, E.; Strand, M.L.; Carlsson-Skwirut, C.; Wahlgren, A.; Svechnikov, K.V.; Cohen, P.; Soder, O. 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(2), 373-385. (Pubitemid 43993428)
    • (2006) Journal of Cellular Physiology , vol.208 , Issue.2 , pp. 373-385
    • Colon, E.1    Strand, M.-L.2    Carlsson-Skwirut, C.3    Wahlgren, A.4    Svechnikov, K.V.5    Cohen, P.6    Soder, O.7
  • 33
    • 26444463390 scopus 로고    scopus 로고
    • Involvement of tyrosine kinases and STAT3 in Humanin-mediated neuroprotection
    • DOI 10.1016/j.lfs.2005.03.031, PII S0024320505005734
    • 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(24), 3092-3104. (Pubitemid 41423745)
    • (2005) Life Sciences , vol.77 , Issue.24 , pp. 3092-3104
    • Hashimoto, Y.1    Suzuki, H.2    Aiso, S.3    Niikura, T.4    Nishimoto, I.5    Matsuoka, M.6
  • 35
    • 2442705358 scopus 로고    scopus 로고
    • Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor
    • Ying, G.; Iribarren, P.; Zhou, Y.; Gong, W.; Zhang, N.; Yu, Z.X.; Le, Y.; Cui, Y.; Wang, J.M. Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor. J Immunol, 2004, 172(11), 7078-7085. (Pubitemid 38669150)
    • (2004) Journal of Immunology , vol.172 , Issue.11 , pp. 7078-7085
    • Ying, G.1    Iribarren, P.2    Zhou, Y.3    Gong, W.4    Zhang, N.5    Yu, Z.-X.6    Le, Y.7    Cui, Y.8    Wang, J.M.9
  • 36
    • 67449124590 scopus 로고    scopus 로고
    • Humanin inhibits neuronal cell death by interacting with a cytokine receptor complex or complexes involving CNTF receptor alpha/WSX-1/gp130
    • Hashimoto, Y.; Kurita, M.; Aiso, S.; Nishimoto, I.; Matsuoka, M. Humanin inhibits neuronal cell death by interacting with a cytokine receptor complex or complexes involving CNTF receptor alpha/WSX-1/gp130. Mol Biol Cell, 2009, 20(12), 2864-2873.
    • (2009) Mol Biol Cell , vol.20 , Issue.12 , pp. 2864-2873
    • Hashimoto, Y.1    Kurita, M.2    Aiso, S.3    Nishimoto, I.4    Matsuoka, M.5
  • 37
    • 24644445576 scopus 로고    scopus 로고
    • Humanin delays apoptosis in K562 cells by downregulation of P38 MAP kinase
    • DOI 10.1007/s10495-005-1191-x
    • Wang, D.; Li, H.; Yuan, H.; Zheng, M.; Bai, C.; Chen, L.; Pei, X. Humanin delays apoptosis in K562 cells by downregulation of P38 MAP kinase. Apoptosis, 2005, 10(5), 963-971. (Pubitemid 41285576)
    • (2005) Apoptosis , vol.10 , Issue.5 , pp. 963-971
    • Wang, D.1    Li, H.2    Yuan, H.3    Zheng, M.4    Bai, C.5    Chen, L.6    Pei, X.7
  • 38
    • 18144399957 scopus 로고    scopus 로고
    • Humanin binds and nullifies bid activity by blocking its activation of Bax and Bak
    • DOI 10.1074/jbc.M411902200
    • Zhai, D.; Luciano, F.; Zhu, X.; Guo, B.; Satterthwait, A.C.; Reed, J.C. Humanin binds and nullifies Bid activity by blocking its activation of Bax and Bak. J Biol Chem, 2005, 280(16), 15815-15824. (Pubitemid 40616702)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 15815-15824
    • Zhai, D.1    Luciano, F.2    Zhu, X.3    Guo, B.4    Satterthwait, A.C.5    Reed, J.C.6
  • 40
    • 0043207393 scopus 로고    scopus 로고
    • 1-40
    • DOI 10.1016/S0196-9781(03)00131-1
    • Zou, P.; Ding, Y.; Sha, Y.; Hu, B.; Nie, S. Humanin peptides block calcium influx of rat hippocampal neurons by altering fibrogenesis of Abeta(1-40). Peptides, 2003, 24(5), 679-685. (Pubitemid 36929997)
    • (2003) Peptides , vol.24 , Issue.5 , pp. 679-685
    • Zou, P.1    Ding, Y.2    Sha, Y.3    Hu, B.4    Nie, S.5
  • 41
    • 33748297432 scopus 로고    scopus 로고
    • Zinc(II) binds to the neuroprotective peptide humanin
    • DOI 10.1016/j.jinorgbio.2006.06.002, PII S0162013406001693
    • Armas, A.; Sonois, V.; Mothes, E.; Mazarguil, H.; Faller, P. Zinc(II) binds to the neuroprotective peptide humanin. J Inorg Biochem, 2006, 100(10), 1672-1678. (Pubitemid 44332529)
    • (2006) Journal of Inorganic Biochemistry , vol.100 , Issue.10 , pp. 1672-1678
    • Armas, A.1    Sonois, V.2    Mothes, E.3    Mazarguil, H.4    Faller, P.5
  • 42
    • 54849164100 scopus 로고    scopus 로고
    • A rescue factor for Alzheimer's diseases: Discovery, activity, structure, and mechanism
    • Arakawa, T.; Kita, Y.; Niikura, T. A rescue factor for Alzheimer's diseases: discovery, activity, structure, and mechanism. Curr Med Chem, 2008, 15(21), 2086-2098.
    • (2008) Curr Med Chem , vol.15 , Issue.21 , pp. 2086-2098
    • Arakawa, T.1    Kita, Y.2    Niikura, T.3
  • 43
    • 33750072017 scopus 로고    scopus 로고
    • The secondary structure analysis of a potent Ser14Gly analog of antiAlzheimer peptide, Humanin, by circular dichroism
    • DOI 10.1002/psc.773
    • 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(10), 639-642. (Pubitemid 44574892)
    • (2006) Journal of Peptide Science , vol.12 , Issue.10 , pp. 639-642
    • Arakawa, T.1    Niikura, T.2    Tajima, H.3    Kita, Y.4
  • 44
    • 63449089439 scopus 로고    scopus 로고
    • Active form of neuroprotective Humanin, HN, and inactive analog, S7A-HN, are monomeric and disordered in aqueous phosphate solution at pH 6.0; No correlation of solution structure with activity
    • Arisaka, F.; Arakawa, T.; Niikura, T.; Kita, Y. Active form of neuroprotective Humanin, HN, and inactive analog, S7A-HN, are monomeric and disordered in aqueous phosphate solution at pH 6.0; No correlation of solution structure with activity. Protein Pept Lett, 2009, 16(2), 132-137.
    • (2009) Protein Pept Lett , vol.16 , Issue.2 , pp. 132-137
    • Arisaka, F.1    Arakawa, T.2    Niikura, T.3    Kita, Y.4
  • 45
    • 45749106275 scopus 로고    scopus 로고
    • The complex structure transition of humanin peptides by sodium dodecylsulfate and trifluoroethanol
    • DOI 10.2174/092986608784567555
    • Kita, Y.; Niikura, T.; Arisaka, F.; Arakawa, T. The complex structure transition of Humanin peptides by sodium dodecylsulfate and trifluoroethanol. Protein Pept Lett, 2008, 15(5), 510-515. (Pubitemid 351872471)
    • (2008) Protein and Peptide Letters , vol.15 , Issue.5 , pp. 510-515
    • Kita, Y.1    Niikura, T.2    Arisaka, F.3    Arakawa, T.4
  • 46
    • 79956073354 scopus 로고    scopus 로고
    • The biological activity of Humanin analogs correlates with structure stabilities in solution
    • Arakawa, T.; Niikura, T.; Kita, Y. The biological activity of Humanin analogs correlates with structure stabilities in solution. Int J Biol Macromol, 2011, 49(1), 93-97.
    • (2011) Int J Biol Macromol , vol.49 , Issue.1 , pp. 93-97
    • Arakawa, T.1    Niikura, T.2    Kita, Y.3
  • 47
    • 77549088022 scopus 로고    scopus 로고
    • Structure changes of natively disordered Humanin in the presence of lipid
    • Hirano, A.; Shiraki, K.; Niikura, T.; Arakawa, T.; Kita, Y. Structure changes of natively disordered Humanin in the presence of lipid. Int J Biol Macromol, 2010, 46(3), 375-379.
    • (2010) Int J Biol Macromol , vol.46 , Issue.3 , pp. 375-379
    • Hirano, A.1    Shiraki, K.2    Niikura, T.3    Arakawa, T.4    Kita, Y.5
  • 48
    • 79551682990 scopus 로고    scopus 로고
    • Structure of three Humanin peptides with different activities upon interaction with liposome
    • Hirano, A.; Shiraki, K.; Niikura, T.; Arakawa, T.; Kita, Y. Structure of three Humanin peptides with different activities upon interaction with liposome. Int J Biol Macromol, 2011, 48(2), 360-363.
    • (2011) Int J Biol Macromol , vol.48 , Issue.2 , pp. 360-363
    • Hirano, A.1    Shiraki, K.2    Niikura, T.3    Arakawa, T.4    Kita, Y.5
  • 49
    • 48749126388 scopus 로고    scopus 로고
    • The structure analysis of Humanin analog, AGA-(C8R)HNG17, by circular dichroism and sedimentation equilibrium: Comparison with the parent molecule
    • Arisaka, F.; Niikura, T.; Arakawa, T.; Kita, Y. The structure analysis of Humanin analog, AGA-(C8R)HNG17, by circular dichroism and sedimentation equilibrium: Comparison with the parent molecule. Int J Biol Macromol, 2008, 43(2), 88-93.
    • (2008) Int J Biol Macromol , vol.43 , Issue.2 , pp. 88-93
    • Arisaka, F.1    Niikura, T.2    Arakawa, T.3    Kita, Y.4
  • 50
    • 79551682990 scopus 로고    scopus 로고
    • Structure of three Humanin peptides with different activities upon interaction with liposome
    • Hirano, A.; Shiraki, K.; Niikura, T.; Arakawa, T.; Kita, Y. Structure of three Humanin peptides with different activities upon interaction with liposome. Int J Biol Macromol, 2011, 48(2), 360-363.
    • (2011) Int J Biol Macromol , vol.48 , Issue.2 , pp. 360-363
    • Hirano, A.1    Shiraki, K.2    Niikura, T.3    Arakawa, T.4    Kita, Y.5
  • 53
    • 0029671001 scopus 로고    scopus 로고
    • Structural studies of opioid peptides: A review of recent progress in x-ray diffraction studies
    • Deschamps, J.R.; George, C.; Flippen-Anderson, J.L. Structural studies of opioid peptides: a review of recent progress in x-ray diffraction studies. Biopolymers, 1996, 40(1), 121-139.
    • (1996) Biopolymers , vol.40 , Issue.1 , pp. 121-139
    • Deschamps, J.R.1    George, C.2    Flippen-Anderson, J.L.3
  • 55
    • 0026155119 scopus 로고
    • Peptide-membrane interactions and a new principle in quantitative structure-activity relationships
    • Schwyzer, R. Peptide-membrane interactions and a new principle in quantitative structure-activity relationships. Biopolymers, 1991, 31(6), 785-792.
    • (1991) Biopolymers , vol.31 , Issue.6 , pp. 785-792
    • Schwyzer, R.1
  • 56
    • 0028903022 scopus 로고
    • 100 years lock-and-key concept: Are peptide keys shaped and guided to their receptors by the target cell membrane?
    • Schwyzer, R. 100 years lock-and-key concept: are peptide keys shaped and guided to their receptors by the target cell membrane? Biopolymers, 1995, 37(1), 5-16.
    • (1995) Biopolymers , vol.37 , Issue.1 , pp. 5-16
    • Schwyzer, R.1
  • 57
    • 66649125501 scopus 로고    scopus 로고
    • Humanin structural versatility and interaction with model cerebral cortex membranes
    • Pistolesi, S.; Rossini, L.; Ferro, E.; Basosi, R.; Trabalzini, L.; Pogni, R. Humanin structural versatility and interaction with model cerebral cortex membranes. Biochemistry, 2009, 48(22), 5026-5033.
    • (2009) Biochemistry , vol.48 , Issue.22 , pp. 5026-5033
    • Pistolesi, S.1    Rossini, L.2    Ferro, E.3    Basosi, R.4    Trabalzini, L.5    Pogni, R.6
  • 58
    • 0013056674 scopus 로고    scopus 로고
    • Identification of essential amino acids in Humanin, a neuroprotective factor against Alzheimer's disease-relevant insults
    • DOI 10.1016/S0196-9781(03)00106-2
    • 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(4), 585-595. (Pubitemid 36829348)
    • (2003) Peptides , vol.24 , Issue.4 , pp. 585-595
    • Yamagishi, Y.1    Hashimoto, Y.2    Niikura, T.3    Nishimoto, I.4
  • 59
    • 2442705358 scopus 로고    scopus 로고
    • Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor
    • Ying, G.; Iribarren, P.; Zhou, Y.; Gong, W.; Zhang, N.; Yu, Z.X.; Le, Y.; Cui, Y.; Wang, J.M. Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor. J immunol, 2004, 172(11), 7078-7085. (Pubitemid 38669150)
    • (2004) Journal of Immunology , vol.172 , Issue.11 , pp. 7078-7085
    • Ying, G.1    Iribarren, P.2    Zhou, Y.3    Gong, W.4    Zhang, N.5    Yu, Z.-X.6    Le, Y.7    Cui, Y.8    Wang, J.M.9
  • 62
    • 2342442848 scopus 로고    scopus 로고
    • The Effect of Cholesterol and Monosialoganglioside (GM1) on the Release and Aggregation of Amyloid β-Peptide from Liposomes Prepared from Brain Membrane-like Lipids
    • DOI 10.1074/jbc.M308622200
    • Tashima, Y.; Oe, R.; Lee, S.; Sugihara, G.; Chambers, E.J.; Takahashi, M.; Yamada, T. The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid beta-peptide from liposomes prepared from brain membrane-like lipids. J Biol Chem, 2004, 279(17), 17587-17595. (Pubitemid 38560523)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17587-17595
    • Tashima, Y.1    Oe, R.2    Lee, S.3    Sugihara, G.4    Chambers, E.J.5    Takahashi, M.6    Yamada, T.7
  • 63
    • 0031968525 scopus 로고    scopus 로고
    • G protein-coupled receptors in gastrointestinal physiology. I. CCK receptors: An exemplary family
    • Wank, S.A. G protein-coupled receptors in gastrointestinal physiology. I. CCK receptors: an exemplary family. Am J Physiol, 1998, 274(4 Pt 1), G607-613.
    • (1998) Am J Physiol , vol.274 , Issue.4 PART 1
    • Wank, S.A.1
  • 64
    • 0034739738 scopus 로고    scopus 로고
    • Neuromedin B
    • DOI 10.1016/S0301-0082(00)00004-6, PII S0301008200000046
    • Ohki-Hamazaki, H. Neuromedin B. Progress in neurobiology, 2000, 62(3), 297-312. (Pubitemid 30326778)
    • (2000) Progress in Neurobiology , vol.62 , Issue.3 , pp. 297-312
    • Ohki-Hamazaki, H.1
  • 65
    • 0030840674 scopus 로고    scopus 로고
    • Y-receptor subtypes-how many more?
    • Blomqvist, A.G.; Herzog, H. Y-receptor subtypes-how many more? Trends Neurosci, 1997, 20(7), 294-298.
    • (1997) Trends Neurosci , vol.20 , Issue.7 , pp. 294-298
    • Blomqvist, A.G.1    Herzog, H.2
  • 66
    • 33745506432 scopus 로고    scopus 로고
    • Recognition of GPCRs by Peptide Ligands and Membrane Compartments theory: Structural Studies of Endogenous Peptide Hormones in Membrane Environment
    • DOI 10.1007/s10540-006-9014-z
    • Sankararamakrishnan, R. Recognition of GPCRs by peptide ligands and membrane compartments theory: structural studies of endogenous peptide hormones in membrane environment. Bioscience reports, 2006, 26(2), 131-158. (Pubitemid 43958797)
    • (2006) Bioscience Reports , vol.26 , Issue.2 , pp. 131-158
    • Sankararamakrishnan, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.