메뉴 건너뛰기




Volumn 5, Issue 7, 2014, Pages 542-551

Transthyretin-derived peptides as β-amyloid inhibitors

Author keywords

aggregation; Alzheimer's; amyloid; beta amyloid; intrinsically disordered; peptide based drugs; transthyretin

Indexed keywords

AMYLOID BETA PROTEIN; EFH PEPTIDE; G12 PEPTIDE; GL16 PEPTIDE; GLA PEPTIDE; GSC PEPTIDE; PEPTIDE; PEPTIDOMIMETIC AGENT; PREALBUMIN; THIOFLAVINE; TRANSTHYRETIN DERIVED PEPTIDE; UNCLASSIFIED DRUG; AMYLOID BETA PROTEIN[1-40]; NEUROPROTECTIVE AGENT; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN;

EID: 84904414101     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn500014u     Document Type: Article
Times cited : (38)

References (59)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J. and Selkoe, D. J. (2002) Medicine-The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics Science 297, 353-356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 63849197629 scopus 로고    scopus 로고
    • Amyloid beta-protein assembly and Alzheimer Disease
    • Roychaudhuri, R., Yang, M., Hoshi, M. M., and Teplow, D. B. (2009) Amyloid beta-protein assembly and Alzheimer Disease J. Biol. Chem. 284, 4749-4753
    • (2009) J. Biol. Chem. , vol.284 , pp. 4749-4753
    • Roychaudhuri, R.1    Yang, M.2    Hoshi, M.M.3    Teplow, D.B.4
  • 3
    • 80052266213 scopus 로고    scopus 로고
    • The amyloid cascade hypothesis for Alzheimer's disease: An appraisal for the development of therapeutics
    • Karran, E., Mercken, M., and De Strooper, B. (2011) The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics Nat. Rev. Drug Discovery 10, 698-U1600
    • (2011) Nat. Rev. Drug Discovery , vol.10
    • Karran, E.1    Mercken, M.2    De Strooper, B.3
  • 4
    • 64349107868 scopus 로고    scopus 로고
    • Small molecule inhibitors of Abeta aggregation and neurotoxicity
    • Hawkes, C. A., Ng, V., and McLaurin, J. (2009) Small molecule inhibitors of Abeta aggregation and neurotoxicity Drug Dev. Res. 70, 111-124
    • (2009) Drug Dev. Res. , vol.70 , pp. 111-124
    • Hawkes, C.A.1    Ng, V.2    McLaurin, J.3
  • 8
    • 81455136028 scopus 로고    scopus 로고
    • A safe, blodd-brain barriar permeable triphenylmethane dye inhibits amyloid-beta neurotoxicity by generating nontoxic aggregates
    • Wong, H. E., Qi, W., Choi, H. M., Fernandez, E., and Kwon, I. (2011) A safe, blodd-brain barriar permeable triphenylmethane dye inhibits amyloid-beta neurotoxicity by generating nontoxic aggregates ACS Chem. Neurosci 2, 645-657
    • (2011) ACS Chem. Neurosci , vol.2 , pp. 645-657
    • Wong, H.E.1    Qi, W.2    Choi, H.M.3    Fernandez, E.4    Kwon, I.5
  • 9
    • 0034674785 scopus 로고    scopus 로고
    • Inositol stereoisomers stabilize an oligomeric aggregate of alzheimer amyloid β peptide and inhibit Aβ-induced toxicity
    • DOI 10.1074/jbc.M906994199
    • McLaurin, J., Golomb, R., Jurewicz, A., Antel, J. P., and Fraser, P. E. (2000) Inositol stereoisomers stabilize an oligomeric aggregate of Alzheimer amyloid beta peptide and inhibit A beta-induced toxicity J. Biol. Chem. 275, 18495-18502 (Pubitemid 30414810)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.24 , pp. 18495-18502
    • McLaurin, J.1    Golomb, R.2    Jurewicz, A.3    Antel, J.P.4    Fraser, P.E.5
  • 12
    • 54849425126 scopus 로고    scopus 로고
    • Discovering and improving novel peptide therapeutics
    • McGregor, D. P. (2008) Discovering and improving novel peptide therapeutics Curr. Opin. Pharmacol. 8, 616-619
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 616-619
    • McGregor, D.P.1
  • 13
    • 84863987464 scopus 로고    scopus 로고
    • Inhibition of amyloid formation
    • Hard, T. and Lendel, C. (2012) Inhibition of amyloid formation J. Mol. Biol. 421, 441-465
    • (2012) J. Mol. Biol. , vol.421 , pp. 441-465
    • Hard, T.1    Lendel, C.2
  • 14
    • 33749522024 scopus 로고    scopus 로고
    • Peptide-Based Inhibitors of Amyloid Assembly
    • DOI 10.1016/S0076-6879(06)13015-3, PII S0076687906130153, Amyloid, Prions, and Other Protein Aggregates, Part C
    • Sciarretta, K. L., Gordon, D. J., and Meredith, S. C. (2006) Peptide-based inhibitors of amyloid assembly Methods Enzymol. 413, 273-312 (Pubitemid 44528696)
    • (2006) Methods in Enzymology , vol.413 , pp. 273-312
    • Sciarretta, K.L.1    Gordon, D.J.2    Meredith, S.C.3
  • 15
    • 57349107392 scopus 로고    scopus 로고
    • Peptide and protein mimetics inhibiting amyloid beta-peptide aggregation
    • Takahashi, T. and Mihara, H. (2008) Peptide and protein mimetics inhibiting amyloid beta-peptide aggregation Acc. Chem. Res. 41, 1309-1318
    • (2008) Acc. Chem. Res. , vol.41 , pp. 1309-1318
    • Takahashi, T.1    Mihara, H.2
  • 17
    • 0029910347 scopus 로고    scopus 로고
    • A strategy for designing inhibitors of β-amyloid toxicity
    • DOI 10.1074/jbc.271.47.29525
    • Ghanta, J., Shen, C. L., Kiessling, L. L., and Murphy, R. M. (1996) A strategy for designing inhibitors of beta-amyloid toxicity J. Biol. Chem. 271, 29525-29528 (Pubitemid 26389569)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.47 , pp. 29525-29528
    • Ghanta, J.1    Shen, C.-L.2    Kiessling, L.L.3    Murphy, R.M.4
  • 18
    • 77950937554 scopus 로고    scopus 로고
    • Development of a proteolytically stable retro-inverso peptide inhibitor of beta-amyloid oligomerization as a potential novel treatment for Alzheimer's Disease
    • Taylor, M., Moore, S., Mayes, J., Parkin, E., Beeg, M., Canovi, M., Gobbi, M., Mann, D. M. A., and Allsop, D. (2010) Development of a proteolytically stable retro-inverso peptide inhibitor of beta-amyloid oligomerization as a potential novel treatment for Alzheimer's Disease Biochemistry 49, 3261-3272
    • (2010) Biochemistry , vol.49 , pp. 3261-3272
    • Taylor, M.1    Moore, S.2    Mayes, J.3    Parkin, E.4    Beeg, M.5    Canovi, M.6    Gobbi, M.7    Mann, D.M.A.8    Allsop, D.9
  • 19
    • 0031873102 scopus 로고    scopus 로고
    • β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • DOI 10.1038/nm0798-822
    • Soto, C., Sigurdsson, E. M., Morelli, L., Kumar, R. A., Castano, E. M., and Frangione, B. (1998) Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy Nat. Med. 4, 822-826 (Pubitemid 28331024)
    • (1998) Nature Medicine , vol.4 , Issue.7 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 20
    • 34547533771 scopus 로고    scopus 로고
    • Embedding the amyloid β-peptide sequence in green fluorescent protein inhibits Aβ oligomerization
    • DOI 10.1002/cbic.200700108
    • Takahashi, T., Ohta, K., and Mihara, H. (2007) Embedding the amyloid beta-pepticle sequence in green fluorescent protein inhibits A beta oligomerization ChemBioChem 8, 985-988 (Pubitemid 47183614)
    • (2007) ChemBioChem , vol.8 , Issue.9 , pp. 985-988
    • Takahashi, T.1    Ohta, K.2    Mihara, H.3
  • 22
    • 84873127460 scopus 로고    scopus 로고
    • A novel retro-inverso peptide inhibitor reduces amyloid deposition, oxidation and inflammation and stimulates neurogenesis in the APPswe/PS1 Delta E9 mouse model of Alzheimer's Disease
    • Parthsarathy, V., McClean, P. L., Holscher, C., Taylor, M., Tinker, C., Jones, G., Kolosov, O., Salvati, E., Gregori, M., Masserini, M., and Allsop, D. (2013) A novel retro-inverso peptide inhibitor reduces amyloid deposition, oxidation and inflammation and stimulates neurogenesis in the APPswe/PS1 Delta E9 mouse model of Alzheimer's Disease PLoS One 8, e54769
    • (2013) PLoS One , vol.8 , pp. 54769
    • Parthsarathy, V.1    McClean, P.L.2    Holscher, C.3    Taylor, M.4    Tinker, C.5    Jones, G.6    Kolosov, O.7    Salvati, E.8    Gregori, M.9    Masserini, M.10    Allsop, D.11
  • 23
    • 33748495574 scopus 로고    scopus 로고
    • Phage display affords peptides that modulate β-amyloid aggregation
    • DOI 10.1021/ja0619861
    • Orner, B. P., Liu, L., Murphy, R. M., and Kiessling, L. L. (2006) Phage display affords peptides that modulate beta-amyloid aggregation J. Am. Chem. Soc. 128, 11882-11889 (Pubitemid 44360224)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.36 , pp. 11882-11889
    • Orner, B.P.1    Liu, L.2    Murphy, R.M.3    Kiessling, L.L.4
  • 25
    • 84880199906 scopus 로고    scopus 로고
    • Combining intracellular selection with protein-fragment complementation to derive Abeta interacting peptides
    • Acerra, N., Kad, N. M., and Mason, J. M. (2013) Combining intracellular selection with protein-fragment complementation to derive Abeta interacting peptides Protein Eng., Des. Sel. 26, 463-470
    • (2013) Protein Eng., Des. Sel. , vol.26 , pp. 463-470
    • Acerra, N.1    Kad, N.M.2    Mason, J.M.3
  • 27
    • 0036759157 scopus 로고    scopus 로고
    • Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways
    • Stein, T. D. and Johnson, J. A. (2002) Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways J. Neurosci. 22, 7380-7388 (Pubitemid 35386337)
    • (2002) Journal of Neuroscience , vol.22 , Issue.17 , pp. 7380-7388
    • Stein, T.D.1    Johnson, J.A.2
  • 28
    • 4444255624 scopus 로고    scopus 로고
    • Sw mice resulting in tau phosphorylation and loss of hippocampal neurons: Support for the amyloid hypothesis
    • DOI 10.1523/JNEUROSCI.2211-04.2004
    • Stein, T. D., Anders, N. J., DeCarli, C., Chan, S. L., Mattson, M. P., and Johnson, J. A. (2004) Neutralization of transthyretin reverses the neuroprotective effects of secreted amyloid precursor protein (APP) in APP(Sw) mice resulting in tau phosphorylation and loss of hippocampal neurons: Support for the amyloid hypothesis J. Neurosci. 24, 7707-7717 (Pubitemid 39186826)
    • (2004) Journal of Neuroscience , vol.24 , Issue.35 , pp. 7707-7717
    • Stein, T.D.1    Anders, N.J.2    DeCarli, C.3    Chan, S.L.4    Mattson, M.P.5    Johnson, J.A.6
  • 30
    • 29144498005 scopus 로고    scopus 로고
    • Transthyretin inhibition of amyloid beta aggregation and toxicity
    • DOI 10.1016/j.clinbiochem.2005.08.007, PII S0009912005002341
    • Giunta, S., Valli, M. B., Galeazzi, R., Fattoretti, P., Corder, E. H., and Galeazzi, L. (2005) Transthyretin inhibition of amylold beta aggregation and toxicity Clin. Biochem. 38, 1112-1119 (Pubitemid 41797752)
    • (2005) Clinical Biochemistry , vol.38 , Issue.12 , pp. 1112-1119
    • Giunta, S.1    Valli, M.B.2    Galeazzi, R.3    Fattoretti, P.4    Corder, E.H.5    Galeazzi, L.6
  • 31
    • 40149086952 scopus 로고    scopus 로고
    • Transthyretin binding to ABeta peptide - Impact on ABeta fibrillogenesis and toxicity
    • Costa, R., Goncalves, A., Saralva, M. J., and Cardoso, I. (2008) Transthyretin binding to ABeta peptide-Impact on ABeta fibrillogenesis and toxicity FEBS Lett. 582, 936-942
    • (2008) FEBS Lett. , vol.582 , pp. 936-942
    • Costa, R.1    Goncalves, A.2    Saralva, M.J.3    Cardoso, I.4
  • 32
    • 80052350163 scopus 로고    scopus 로고
    • Neuronal production of transthyretin in human and murine Alzheimer's Disease: Is it protective?
    • Li, X. Y., Masliah, E., Reixach, N., and Buxbaum, J. N. (2011) Neuronal production of transthyretin in human and murine Alzheimer's Disease: Is it protective? J. Neurosci. 31, 12483-12490
    • (2011) J. Neurosci. , vol.31 , pp. 12483-12490
    • Li, X.Y.1    Masliah, E.2    Reixach, N.3    Buxbaum, J.N.4
  • 33
    • 84877049480 scopus 로고    scopus 로고
    • Transthyretin as both a sensor and a scavenger of beta-amyloid oligomers
    • Yang, D. T., Joshi, G., Cho, P. Y., Johnson, J. A., and Murphy, R. M. (2013) Transthyretin as both a sensor and a scavenger of beta-amyloid oligomers Biochemistry 52, 2849-2861
    • (2013) Biochemistry , vol.52 , pp. 2849-2861
    • Yang, D.T.1    Joshi, G.2    Cho, P.Y.3    Johnson, J.A.4    Murphy, R.M.5
  • 34
    • 77957042274 scopus 로고    scopus 로고
    • Characterization of the interaction of beta-amyloid with transthyretin monomers and tetramers
    • Du, J. L. and Murphy, R. M. (2010) Characterization of the interaction of beta-amyloid with transthyretin monomers and tetramers Biochemistry 49, 8276-8289
    • (2010) Biochemistry , vol.49 , pp. 8276-8289
    • Du, J.L.1    Murphy, R.M.2
  • 35
    • 84863986886 scopus 로고    scopus 로고
    • Oligomeric intermediates in amyloid formation: Structure determination and mechanisms of toxicity
    • Fandrich, M. (2012) Oligomeric intermediates in amyloid formation: Structure determination and mechanisms of toxicity J. Mol. Biol. 421, 427-440
    • (2012) J. Mol. Biol. , vol.421 , pp. 427-440
    • Fandrich, M.1
  • 36
    • 84862994625 scopus 로고    scopus 로고
    • Identification of beta-amyloid-binding sites on transthyretin
    • Du, J. L., Cho, P. Y., Yang, D. T., and Murphy, R. M. (2012) Identification of beta-amyloid-binding sites on transthyretin Protein Eng., Des. Sel. 25, 337-345
    • (2012) Protein Eng., Des. Sel. , vol.25 , pp. 337-345
    • Du, J.L.1    Cho, P.Y.2    Yang, D.T.3    Murphy, R.M.4
  • 38
    • 34548400699 scopus 로고    scopus 로고
    • Detecting the inter-peptide arrangement and maturation process of transthyretin (105-115) amyloid fibril using a FRET pair with short Förster distance
    • DOI 10.1016/j.bbrc.2007.08.059, PII S0006291X0701741X
    • Deng, W., Cao, A. N., and Lai, L. H. (2007) Detecting the inter-peptide arrangement and maturation process of transthyretin (105-115) amyloid fibril using a FRET pair with short Forster distance Biochem. Biophys. Res. Commun. 362, 689-694 (Pubitemid 47368147)
    • (2007) Biochemical and Biophysical Research Communications , vol.362 , Issue.3 , pp. 689-694
    • Deng, W.1    Cao, A.2    Lai, L.3
  • 39
    • 0028172158 scopus 로고
    • H-1-NMR analysis of fibril-forming peptide-fragments of transthyretin
    • Jarvis, J. A., Kirkpatrick, A., and Craik, D. J. (1994) H-1-NMR analysis of fibril-forming peptide-fragments of transthyretin Int. J. Pept. Prot. Res. 44, 388-398
    • (1994) Int. J. Pept. Prot. Res. , vol.44 , pp. 388-398
    • Jarvis, J.A.1    Kirkpatrick, A.2    Craik, D.J.3
  • 40
    • 0025801516 scopus 로고
    • Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro
    • Gustavsson, A., Engstrom, U., and Westermark, P. (1991) Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro Biochem. Biophys. Res. Commun. 175, 1159-1164
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 1159-1164
    • Gustavsson, A.1    Engstrom, U.2    Westermark, P.3
  • 41
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • DOI 10.1038/nbt1012
    • Fernandez-Escamilla, A. M., Rousseau, F., Schymkowitz, J., and Serrano, L. (2004) Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins Nat. Biotechnol. 22, 1302-1306 (Pubitemid 39336784)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 42
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 45
    • 65749099472 scopus 로고    scopus 로고
    • The importance of being tyrosine: Lessons in molecular recognition from minimalist synthetic binding proteins
    • Koide, S. and Sidhu, S. S. (2009) The importance of being tyrosine: Lessons in molecular recognition from minimalist synthetic binding proteins ACS Chem. Biol. 4, 325-334
    • (2009) ACS Chem. Biol. , vol.4 , pp. 325-334
    • Koide, S.1    Sidhu, S.S.2
  • 48
    • 84869811189 scopus 로고    scopus 로고
    • Dye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (Abeta) self-assembly
    • Jameson, L. P., Smith, N. W., and Dzyuba, S. V. (2012) Dye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (Abeta) self-assembly ACS Chem. Neurosci. 3, 807-819
    • (2012) ACS Chem. Neurosci. , vol.3 , pp. 807-819
    • Jameson, L.P.1    Smith, N.W.2    Dzyuba, S.V.3
  • 49
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe, C. G. (2008) Structural classification of toxic amyloid oligomers J. Biol. Chem. 283, 29639-29643
    • (2008) J. Biol. Chem. , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 50
    • 77952320068 scopus 로고    scopus 로고
    • Molecular mechanism of Thioflavin-T binding to amyloid fibrils
    • Biancalana, M. and Koide, S. (2010) Molecular mechanism of Thioflavin-T binding to amyloid fibrils Biochim. Biophys. Acta, Proteins Proteomics 1804, 1405-1412
    • (2010) Biochim. Biophys. Acta, Proteins Proteomics , vol.1804 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2
  • 51
    • 0035949432 scopus 로고    scopus 로고
    • An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured
    • DOI 10.1021/bi011194d
    • Jiang, X., Smith, C. S., Petrassi, H. M., Hammarstrom, P., White, J. T., Sacchettini, J. C., and Kelly, J. W. (2001) An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured Biochemistry 40, 11442-11452 (Pubitemid 32911287)
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11442-11452
    • Jiang, X.1    Smith, C.S.2    Petrassi, H.M.3    Hammarstrom, P.4    White, J.T.5    Sacchettini, J.C.6    Kelly, J.W.7
  • 52
    • 79953133327 scopus 로고    scopus 로고
    • Abeta 42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta 42 species
    • Jan, A., Adolfsson, O., Allaman, I., Buccarello, A. L., Magistretti, P. J., Pfeifer, A., Muhs, A., and Lashuel, H. A. (2011) Abeta 42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta 42 species J. Biol. Chem. 286, 8585-8596
    • (2011) J. Biol. Chem. , vol.286 , pp. 8585-8596
    • Jan, A.1    Adolfsson, O.2    Allaman, I.3    Buccarello, A.L.4    Magistretti, P.J.5    Pfeifer, A.6    Muhs, A.7    Lashuel, H.A.8
  • 57
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state
    • Pallitto, M. M. and Murphy, R. M. (2001) A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state Biophys. J. 81, 1805-1822 (Pubitemid 32783616)
    • (2001) Biophysical Journal , vol.81 , Issue.3 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 58
    • 0032994428 scopus 로고    scopus 로고
    • Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
    • DOI 10.1073/pnas.96.11.6020
    • Fancy, D. A. and Kodadek, T. (1999) Chemistry for the analysis of protein-protein interactions: Rapid and efficient cross-linking triggered by long wavelength light Proc. Natl. Acad. Sci. U.S.A. 96, 6020-6024 (Pubitemid 29256612)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.11 , pp. 6020-6024
    • Fancy, D.A.1    Kodadek, T.2
  • 59
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid beta-protein oligomerization - Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • Bitan, G., Lomakin, A., and Teplow, D. B. (2001) Amyloid beta-protein oligomerization-Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins J. Biol. Chem. 276, 35176-35184
    • (2001) J. Biol. Chem. , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.