메뉴 건너뛰기




Volumn 442, Issue 3, 2012, Pages 583-593

Human-protein-derived peptides for intracellular delivery of biomolecules

Author keywords

Cell penetrating peptide; Small interfering RNA (siRNA); Therapeutic biomolecule; Transfection

Indexed keywords

CELL PENETRATING PEPTIDE; NEURTURIN; PROTEOME; SMALL INTERFERING RNA;

EID: 84857869669     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111973     Document Type: Article
Times cited : (13)

References (54)
  • 1
    • 0000822995 scopus 로고
    • On the importance of being ionized
    • Davis, B. D. (1958) On the importance of being ionized. Arch. Biochem. Biophys. 78, 497-509
    • (1958) Arch. Biochem. Biophys. , vol.78 , pp. 497-509
    • Davis, B.D.1
  • 2
    • 0019377789 scopus 로고
    • Transfer of proteins across membranes
    • Kreil, G. (1981) Transfer of proteins across membranes. Annu. Rev. Biochem. 50, 317-348
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 317-348
    • Kreil, G.1
  • 3
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook, A., Bono, F., Jinek, M. and Conti, E. (2007) Structural biology of nucleocytoplasmic transport. Annu. Rev. Biochem. 76, 647-671
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 5
    • 74049153868 scopus 로고    scopus 로고
    • Lentiviral delivery of RNAi effectors against HIV-1
    • Liu, Y. P. and Berkhout, B. (2009) Lentiviral delivery of RNAi effectors against HIV-1. Curr. Top. Med. Chem. 9, 1130-1143
    • (2009) Curr. Top. Med. Chem. , vol.9 , pp. 1130-1143
    • Liu, Y.P.1    Berkhout, B.2
  • 6
    • 67349242729 scopus 로고    scopus 로고
    • Delivery of RNA interference therapeutics using polycation-based nanoparticles
    • Howard, K. A. (2009) Delivery of RNA interference therapeutics using polycation-based nanoparticles. Adv. Drug Delivery Rev. 61, 710-720
    • (2009) Adv. Drug Delivery Rev. , vol.61 , pp. 710-720
    • Howard, K.A.1
  • 7
    • 70349456654 scopus 로고    scopus 로고
    • Recent advances in the use of cell-penetrating peptides for medical and biological applications
    • Fonseca, S. B., Pereira, M. P. and Kelley, S. O. (2009) Recent advances in the use of cell-penetrating peptides for medical and biological applications. Adv. Drug Delivery Rev. 61, 953-964
    • (2009) Adv. Drug Delivery Rev. , vol.61 , pp. 953-964
    • Fonseca, S.B.1    Pereira, M.P.2    Kelley, S.O.3
  • 8
    • 33748433244 scopus 로고    scopus 로고
    • Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery
    • Mäe, M. and Langel, Ü. (2006) Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery. Curr. Opin. Pharmacol. 6, 509-514
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 509-514
    • Mäe, M.1    Langel, Ü.2
  • 9
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • DOI 10.1016/0092-8674(88)90263-2
    • Frankel, A. D. and Pabo, C. O. (1988) Cellular uptake of the tat protein from human immunodeficiency virus. Cell 55, 1189-1193 (Pubitemid 19020071)
    • (1988) Cell , vol.55 , Issue.6 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 10
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • DOI 10.1074/jbc.272.25.16010
    • Vives, E., Brodin, P. and Lebleu, B. (1997) A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272, 16010-16017 (Pubitemid 27265584)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 11
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki, S., Suzuki, T., Ohashi, W., Yagami, T., Tanaka, S., Ueda, K. and Sugiura, Y. (2001) Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276, 5836-5840
    • (2001) J. Biol. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 13
    • 0035883853 scopus 로고    scopus 로고
    • Peptide-mediated RNA delivery: A novel approach for enhanced transfection of primary and post-mitotic cells
    • Bettinger, T., Carlisle, R. C., Read, M. L., Ogris, M. and Seymour, L. W. (2001) Peptide-mediated RNA delivery: a novel approach for enhanced transfection of primary and post-mitotic cells. Nucleic Acids Res. 29, 3882-3891 (Pubitemid 32910528)
    • (2001) Nucleic Acids Research , vol.29 , Issue.18 , pp. 3882-3891
    • Bettinger, T.1    Carlisle, R.C.2    Read, M.L.3    Ogris, M.4    Seymour, L.W.5
  • 15
    • 0032508926 scopus 로고    scopus 로고
    • Cellular uptake of an α-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically
    • DOI 10.1016/S0005-2736(98)00161-8, PII S0005273698001618
    • Oehlke, J., Scheller, A., Wiesner, B., Krause, E., Beyermann, M., Klauschenz, E., Melzig, M. and Bienert, M. (1998) Cellular uptake of an α-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically. Biochim. Biophys. Acta 1414, 127-139 (Pubitemid 28511045)
    • (1998) Biochimica et Biophysica Acta - Biomembranes , vol.1414 , Issue.1-2 , pp. 127-139
    • Oehlke, J.1    Scheller, A.2    Wiesner, B.3    Krause, E.4    Beyermann, M.5    Klauschenz, E.6    Melzig, M.7    Bienert, M.8
  • 16
    • 0037063996 scopus 로고    scopus 로고
    • Nuclear targeting of macromolecular polyanions by an HIV-Tat derived peptide: Role for cell-surface proteoglycans
    • DOI 10.1074/jbc.M205395200
    • Sandgren, S., Cheng, F. and Belting, M. (2002) Nuclear targeting of macromolecular polyanions by an HIV-Tat derived peptide. Role for cell-surface proteoglycans. J. Biol. Chem. 277, 38877-38883 (Pubitemid 35157770)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38877-38883
    • Sandgren, S.1    Cheng, F.2    Belting, M.3
  • 17
    • 1842529513 scopus 로고    scopus 로고
    • A Stepwise Dissection of the Intracellular Fate of Cationic Cell-penetrating Peptides
    • DOI 10.1074/jbc.M311461200
    • Fischer, R., Kohler, K., Fotin-Mleczek, M. and Brock, R. (2004) A stepwise dissection of the intracellular fate of cationic cell-penetrating peptides. J. Biol. Chem. 279, 12625-12635 (Pubitemid 38445834)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12625-12635
    • Fischer, R.1    Kohler, K.2    Fotin-Mleczek, M.3    Brock, R.4
  • 18
    • 13844272403 scopus 로고    scopus 로고
    • Adaptive translocation: The role of hydrogen bonding and membrane potential in the uptake of guanidinium-rich transporters into cells
    • DOI 10.1016/j.addr.2004.10.003, PII S0169409X04002650
    • Rothbard, J. B., Jessop, T. C. and Wender, P. A. (2005) Adaptive translocation: the role of hydrogen bonding and membrane potential in the uptake of guanidinium-rich transporters into cells. Adv. Drug Delivery Rev. 57, 495-504 (Pubitemid 40255557)
    • (2005) Advanced Drug Delivery Reviews , vol.57 , Issue.4 SPEC.ISS. , pp. 495-504
    • Rothbard, J.B.1    Jessop, T.C.2    Wender, P.A.3
  • 20
    • 57149110011 scopus 로고    scopus 로고
    • CNS delivery via adsorptive transcytosis
    • Herve, F., Ghinea, N. and Scherrmann, J. M. (2008) CNS delivery via adsorptive transcytosis. AAPS J. 10, 455-472
    • (2008) AAPS J. , vol.10 , pp. 455-472
    • Herve, F.1    Ghinea, N.2    Scherrmann, J.M.3
  • 21
    • 3843092828 scopus 로고    scopus 로고
    • Chances and pitfalls of cell penetrating peptides for cellular drug delivery
    • DOI 10.1016/j.ejpb.2004.02.018, PII S0939641104000906
    • Trehin, R. and Merkle, H. P. (2004) Chances and pitfalls of cell penetrating peptides for cellular drug delivery. Eur. J. Pharm. Biopharm. 58, 209-223 (Pubitemid 39037230)
    • (2004) European Journal of Pharmaceutics and Biopharmaceutics , vol.58 , Issue.2 , pp. 209-223
    • Trehin, R.1    Merkle, H.P.2
  • 22
    • 2942715203 scopus 로고    scopus 로고
    • Primary amphipathic cell-penetrating peptides: Structural requirements and interactions with model membranes
    • DOI 10.1021/bi049298m
    • Deshayes, S., Plenat, T., drian-Herrada, G., Divita, G., Le Grimellec, C. and Heitz, F. (2004) Primary amphipathic cell-penetrating peptides: structural requirements and interactions with model membranes. Biochemistry 43, 7698-7706 (Pubitemid 38787677)
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7698-7706
    • Deshayes, S.1    Plenat, T.2    Aldrian-Herrada, G.3    Divita, G.4    Le, G.C.5    Heitz, F.6
  • 24
    • 33746863376 scopus 로고    scopus 로고
    • Cholesteryl Oligoarginine Delivering Vascular Endothelial Growth Factor siRNA Effectively Inhibits Tumor Growth in Colon Adenocarcinoma
    • DOI 10.1016/j.ymthe.2006.03.022, PII S1525001606001420
    • Kim, W. J., Christensen, L. V., Jo, S., Yockman, J. W., Jeong, J. H., Kim, Y. H. and Kim, S. W. (2006) Cholesteryl oligoarginine delivering vascular endothelial growth factor siRNA effectively inhibits tumor growth in colon adenocarcinoma. Mol. Ther. 14, 343-350 (Pubitemid 44184964)
    • (2006) Molecular Therapy , vol.14 , Issue.3 , pp. 343-350
    • Kim, W.J.1    Christensen, L.V.2    Jo, S.3    Yockman, J.W.4    Jeong, J.H.5    Kim, Y.-H.6    Kim, S.W.7
  • 26
    • 0029006149 scopus 로고
    • Inhibition of nuclear translocation of transcription factor NF-κB by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence
    • Lin, Y. Z., Yao, S. Y., Veach, R. A., Torgerson, T. R. and Hawiger, J. (1995) Inhibition of nuclear translocation of transcription factor NF-κB by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence. J. Biol. Chem. 270, 14255-14258
    • (1995) J. Biol. Chem. , vol.270 , pp. 14255-14258
    • Lin, Y.Z.1    Yao, S.Y.2    Veach, R.A.3    Torgerson, T.R.4    Hawiger, J.5
  • 27
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • DOI 10.1038/35078107
    • Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K. and Tuschl, T. (2001) Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498 (Pubitemid 32494397)
    • (2001) Nature , vol.411 , Issue.6836 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 28
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in caenorhabditis elegans
    • DOI 10.1038/35888
    • Fire, A., Xu, S., Montgomery, M. K., Kostas, S. A., Driver, S. E. and Mello, C. C. (1998) Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 391, 806-811 (Pubitemid 28099681)
    • (1998) Nature , vol.391 , Issue.6669 , pp. 806-811
    • Fire, A.1    Xu, S.2    Montgomery, M.K.3    Kostas, S.A.4    Driver, S.E.5    Mello, C.C.6
  • 30
    • 39149093340 scopus 로고    scopus 로고
    • Enhancing the cellular uptake of siRNA duplexes following noncovalent packaging with protein transduction domain peptides
    • Meade, B. R. and Dowdy, S. F. (2008) Enhancing the cellular uptake of siRNA duplexes following noncovalent packaging with protein transduction domain peptides. Adv. Drug Delivery Rev. 60, 530-536
    • (2008) Adv. Drug Delivery Rev. , vol.60 , pp. 530-536
    • Meade, B.R.1    Dowdy, S.F.2
  • 32
    • 0029417238 scopus 로고
    • Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo
    • Blangy, A., Lane, H. A., d'Herin, P., Harper, M., Kress, M. and Nigg, E. A. (1995) Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo. Cell 83, 1159-1169
    • (1995) Cell , vol.83 , pp. 1159-1169
    • Blangy, A.1    Lane, H.A.2    D'Herin, P.3    Harper, M.4    Kress, M.5    Nigg, E.A.6
  • 34
    • 67650366798 scopus 로고    scopus 로고
    • Inhibition of ovarian cancer growth by a tumor-targeting peptide that binds eukaryotic translation initiation factor 4E
    • Ko, S. Y., Guo, H., Barengo, N. and Naora, H. (2009) Inhibition of ovarian cancer growth by a tumor-targeting peptide that binds eukaryotic translation initiation factor 4E. Clin. Cancer Res. 15, 4336-4347
    • (2009) Clin. Cancer Res. , vol.15 , pp. 4336-4347
    • Ko, S.Y.1    Guo, H.2    Barengo, N.3    Naora, H.4
  • 35
    • 0343167422 scopus 로고    scopus 로고
    • Rapid induction of apoptosis mediated by peptides that bind initiation factor eIF4E
    • DOI 10.1016/S0960-9822(00)00567-4
    • Herbert, T. P., Fahraeus, R., Prescott, A., Lane, D. P. and Proud, C. G. (2000) Rapid induction of apoptosis mediated by peptides that bind initiation factor eIF4E. Curr. Biol. 10, 793-796 (Pubitemid 30466944)
    • (2000) Current Biology , vol.10 , Issue.13 , pp. 793-796
    • Herbert, T.P.1    Fahraeus, R.2    Prescott, A.3    Lane, D.P.4    Proud, C.G.5
  • 36
    • 0033198763 scopus 로고    scopus 로고
    • Chain length of cationic α-helical peptide sufficient for gene delivery into cells
    • DOI 10.1021/bc990012d
    • Niidome, T., Takaji, K., Urakawa, M., Ohmori, N., Wada, A., Hirayama, T. and Aoyagi, H. (1999) Chain length of cationic alpha-helical peptide sufficient for gene delivery into cells. Bioconjugate Chem. 10, 773-780 (Pubitemid 29456363)
    • (1999) Bioconjugate Chemistry , vol.10 , Issue.5 , pp. 773-780
    • Niidome, T.1    Takaji, K.2    Urakawa, M.3    Ohmori, N.4    Wada, A.5    Hirayama, T.6    Aoyagi, H.7
  • 38
    • 0030989670 scopus 로고    scopus 로고
    • X-ray structure of glial cell-derived neurotrophic factor at 1.9 Å resolution and implications for receptor binding
    • DOI 10.1038/nsb0697-435
    • Eigenbrot, C. and Gerber, N. (1997) X-ray structure of glial cell-derived neurotrophic factor at 1.9 Å resolution and implications for receptor binding. Nat. Struct. Biol. 4, 435-438 (Pubitemid 27263594)
    • (1997) Nature Structural Biology , vol.4 , Issue.6 , pp. 435-438
    • Eigenbrot, C.1    Gerber, N.2
  • 39
    • 33744789162 scopus 로고    scopus 로고
    • Structure of Artemin Complexed with Its Receptor GFRα3: Convergent Recognition of Glial Cell Line-Derived Neurotrophic Factors
    • DOI 10.1016/j.str.2006.05.010, PII S0969212606002279
    • Wang, X., Baloh, R. H., Milbrandt, J. and Garcia, K. C. (2006) Structure of artemin complexed with its receptor GFRα3: convergent recognition of glial cell line-derived neurotrophic factors. Structure 14, 1083-1092 (Pubitemid 43831668)
    • (2006) Structure , vol.14 , Issue.6 , pp. 1083-1092
    • Wang, X.1    Baloh, R.H.2    Milbrandt, J.3    Garcia, K.C.4
  • 40
    • 0032444658 scopus 로고    scopus 로고
    • Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins
    • Buck, M. (1998) Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys. 31, 297-355
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 297-355
    • Buck, M.1
  • 42
    • 34250835903 scopus 로고    scopus 로고
    • A comprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • DOI 10.1111/j.1600-0854.2007.00572.x
    • Duchardt, F., Fotin-Mleczek, M., Schwarz, H., Fischer, R. and Brock, R. (2007) A comprehensive model for the cellular uptake of cationic cell-penetrating peptides. Traffic 8, 848-866 (Pubitemid 46971632)
    • (2007) Traffic , vol.8 , Issue.7 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer, R.4    Brock, R.5
  • 43
    • 74049160383 scopus 로고    scopus 로고
    • Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction
    • Gump, J. M., June, R. K. and Dowdy, S. F. (2010) Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction. J. Biol. Chem. 285, 1500-1507
    • (2010) J. Biol. Chem. , vol.285 , pp. 1500-1507
    • Gump, J.M.1    June, R.K.2    Dowdy, S.F.3
  • 46
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D. J. and Thornton, J. M. (1988) Helix geometry in proteins. J. Mol. Biol. 201, 601-619
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 47
    • 0442276416 scopus 로고    scopus 로고
    • Structural features of transmembrane helices
    • DOI 10.1016/S0014-5793(04)00061-4
    • Hildebrand, P. W., Preissner, R. and Frommel, C. (2004) Structural features of transmembrane helices. FEBS Lett. 559, 145-151 (Pubitemid 38186719)
    • (2004) FEBS Letters , vol.559 , Issue.1-3 , pp. 145-151
    • Hildebrand, P.W.1    Preissner, R.2    Frommel, C.3
  • 48
    • 58249095956 scopus 로고    scopus 로고
    • The membrane repair response masks membrane disturbances caused by cell-penetrating peptide uptake
    • Palm-Apergi, C., Lorents, A., Padari, K., Pooga, M. and Hallbrink, M. (2009) The membrane repair response masks membrane disturbances caused by cell-penetrating peptide uptake. FASEB J. 23, 214-223
    • (2009) FASEB J. , vol.23 , pp. 214-223
    • Palm-Apergi, C.1    Lorents, A.2    Padari, K.3    Pooga, M.4    Hallbrink, M.5
  • 49
    • 79952197490 scopus 로고    scopus 로고
    • Thermodynamics of lipid interactions with cell-penetrating peptides
    • Sauder, R., Seelig, J. and Ziegler, A. (2011) Thermodynamics of lipid interactions with cell-penetrating peptides. Methods Mol. Biol. 683, 129-155
    • (2011) Methods Mol. Biol. , vol.683 , pp. 129-155
    • Sauder, R.1    Seelig, J.2    Ziegler, A.3
  • 50
    • 33750504883 scopus 로고    scopus 로고
    • Formation of transmembrane ionic channels of primary amphipathic cell-penetrating peptides. Consequences on the mechanism of cell penetration
    • DOI 10.1016/j.bbamem.2006.08.010, PII S0005273606002999
    • Deshayes, S., Plenat, T., Charnet, P., Divita, G., Molle, G. and Heitz, F. (2006) Formation of transmembrane ionic channels of primary amphipathic cell-penetrating peptides. Consequences on the mechanism of cell penetration. Biochim. Biophys. Acta 1758, 1846-1851 (Pubitemid 44666684)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.11 , pp. 1846-1851
    • Deshayes, S.1    Plenat, T.2    Charnet, P.3    Divita, G.4    Molle, G.5    Heitz, F.6
  • 51
    • 0036903815 scopus 로고    scopus 로고
    • Signalling by glial cell line-derived neurotrophic factor (GDNF) requires heparan sulphate glycosaminoglycan
    • DOI 10.1242/jcs.00114
    • Barnett, M. W., Fisher, C. E., Perona-Wright, G. and Davies, J. A. (2002) Signalling by glial cell line-derived neurotrophic factor (GDNF) requires heparan sulphate glycosaminoglycan. J. Cell Sci. 115, 4495-4503 (Pubitemid 36004410)
    • (2002) Journal of Cell Science , vol.115 , Issue.23 , pp. 4495-4503
    • Barnett, M.W.1    Fisher, C.E.2    Perona-Wright, G.3    Davies, J.A.4
  • 52
    • 0037191354 scopus 로고    scopus 로고
    • Heparin facilitates glial cell line-derived neurotrophic factor signal transduction
    • Tanaka, M., Xiao, H. and Kiuchi, K. (2002) Heparin facilitates glial cell line-derived neurotrophic factor signal transduction. NeuroReport 13, 1913-1916 (Pubitemid 35398959)
    • (2002) NeuroReport , vol.13 , Issue.15 , pp. 1913-1916
    • Tanaka, M.1    Xiao, H.2    Kiuchi, K.3
  • 53
    • 38949213664 scopus 로고    scopus 로고
    • Predicting cell-penetrating peptides
    • DOI 10.1016/j.addr.2007.09.003, PII S0169409X07002918
    • Hansen, M., Kilk, K. and Langel, Ü. (2008) Predicting cell-penetrating peptides. Adv. Drug Delivery Rev. 60, 572-579 (Pubitemid 351215574)
    • (2008) Advanced Drug Delivery Reviews , vol.60 , Issue.4-5 , pp. 572-579
    • Hansen, M.1    Kilk, K.2    Langel, U.3
  • 54
    • 0032059367 scopus 로고    scopus 로고
    • Presentation of antigenic peptides by products of the major histocompatibility complex
    • Fairchild, P. J. (1998) Presentation of antigenic peptides by products of the major histocompatibility complex. J. Pept. Sci. 4, 182-194
    • (1998) J. Pept. Sci. , vol.4 , pp. 182-194
    • Fairchild, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.