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Volumn 8, Issue 5, 2012, Pages 1685-1692

Self-assembling glucagon-like peptide 1-mimetic peptide amphiphiles for enhanced activity and proliferation of insulin-secreting cells

Author keywords

Biomimetic material; Cell activation; Cell signaling; Diabetes; Self assembly

Indexed keywords

AMPHIPHILES; BIOMIMETIC MATERIALS; BIOMIMETICS; CELL DEATH; CELL SIGNALING; INSULIN; NANOFIBERS; PEPTIDES; PHYSIOLOGY;

EID: 84859104555     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2012.01.036     Document Type: Article
Times cited : (34)

References (60)
  • 1
    • 78751662679 scopus 로고    scopus 로고
    • Type 1 diabetes: Etiology, immunology, and therapeutic strategies
    • T.L. Van Belle, K.T. Coppieters, and M.G. Von Herrath Type 1 diabetes: etiology, immunology, and therapeutic strategies Physiol Rev 91 2011 79 118
    • (2011) Physiol Rev , vol.91 , pp. 79-118
    • Van Belle, T.L.1    Coppieters, K.T.2    Von Herrath, M.G.3
  • 2
    • 84858150901 scopus 로고    scopus 로고
    • Bethesda, MD: US Department of Health and Human Services, National Institutes of Health
    • Diseases NIoDaDaK. National diabetes statistics, 2007 fact sheet. Bethesda, MD: US Department of Health and Human Services, National Institutes of Health; 2008.
    • (2008) Diseases NIoDaDaK. National Diabetes Statistics, 2007 Fact Sheet
  • 3
    • 0037093012 scopus 로고    scopus 로고
    • Effect of intensive therapy on the microvascular complications of type 1 diabetes mellitus
    • Group WTftDCaCTEoDIaCR
    • Group WTftDCaCTEoDIaCR Effect of intensive therapy on the microvascular complications of type 1 diabetes mellitus JAMA 287 2002 2563 2569
    • (2002) JAMA , vol.287 , pp. 2563-2569
  • 4
    • 70349645780 scopus 로고    scopus 로고
    • Society IoD. Current advances and travails in islet transplantation
    • D.M. Harlan, N.S. Kenyon, O. Korsgren, and B.O. Roep Society IoD. Current advances and travails in islet transplantation Diabetes 58 2009 2175 2184
    • (2009) Diabetes , vol.58 , pp. 2175-2184
    • Harlan, D.M.1    Kenyon, N.S.2    Korsgren, O.3    Roep, B.O.4
  • 6
    • 33845717517 scopus 로고    scopus 로고
    • Overcoming the challenges now limiting islet transplantation: A sequential, integrated approach
    • A. Pileggi, L. Cobianchi, L. Inverardi, and C. Ricordi Overcoming the challenges now limiting islet transplantation: a sequential, integrated approach Ann N Y Acad Sci 1079 2006 383 398
    • (2006) Ann N y Acad Sci , vol.1079 , pp. 383-398
    • Pileggi, A.1    Cobianchi, L.2    Inverardi, L.3    Ricordi, C.4
  • 7
    • 33747038451 scopus 로고    scopus 로고
    • Interventional strategies to prevent beta-cell apoptosis in islet transplantation
    • J.A. Emamaullee, and A.M.J. Shapiro Interventional strategies to prevent beta-cell apoptosis in islet transplantation Diabetes 55 2006 1907 1914
    • (2006) Diabetes , vol.55 , pp. 1907-1914
    • Emamaullee, J.A.1    Shapiro, A.M.J.2
  • 9
    • 34249941467 scopus 로고    scopus 로고
    • Vascular endothelial growth factor as a survival factor for human islets: Effect of immunosuppressive drugs
    • S.E. Cross, S.K. Richards, A. Clark, A.V. Benest, D.O. Bates, and P.W. Mathieson Vascular endothelial growth factor as a survival factor for human islets: effect of immunosuppressive drugs Diabetologia 50 2007 1423 1432
    • (2007) Diabetologia , vol.50 , pp. 1423-1432
    • Cross, S.E.1    Richards, S.K.2    Clark, A.3    Benest, A.V.4    Bates, D.O.5    Mathieson, P.W.6
  • 10
    • 34047181107 scopus 로고    scopus 로고
    • Factors influencing the loss of beta-cell mass in islet transplantation
    • J.A. Emamaullee, and A.M.J. Shapiro Factors influencing the loss of beta-cell mass in islet transplantation Cell Transplant 16 2007 1 8
    • (2007) Cell Transplant , vol.16 , pp. 1-8
    • Emamaullee, J.A.1    Shapiro, A.M.J.2
  • 11
  • 12
    • 33646735392 scopus 로고    scopus 로고
    • Biological and biomaterial approaches for improved islet transplantation
    • A.S. Narang, and R.I. Mahato Biological and biomaterial approaches for improved islet transplantation Pharmacol Rev 58 2006 194 243
    • (2006) Pharmacol Rev , vol.58 , pp. 194-243
    • Narang, A.S.1    Mahato, R.I.2
  • 13
    • 0036177857 scopus 로고    scopus 로고
    • Cytoprotection of pancreatic islets before and early after transplantation using gene therapy
    • J.L. Contreras, G. Bilbao, C.A. Smyth, D.E. Eckhoff, X.L. Jiang, and S. Jenkins Cytoprotection of pancreatic islets before and early after transplantation using gene therapy Kidney Int 61 2002 S79 S84
    • (2002) Kidney Int , vol.61
    • Contreras, J.L.1    Bilbao, G.2    Smyth, C.A.3    Eckhoff, D.E.4    Jiang, X.L.5    Jenkins, S.6
  • 14
    • 48649106230 scopus 로고    scopus 로고
    • Extracellular matrix protein-coated scaffolds promote the reversal of diabetes after extrahepatic islet transplantation
    • D.M. Salvay, C.B. Rives, X. Zhang, F. Chen, D.B. Kaufman, and W.L. Lowe Extracellular matrix protein-coated scaffolds promote the reversal of diabetes after extrahepatic islet transplantation Transplantation 85 2008 1456 1464
    • (2008) Transplantation , vol.85 , pp. 1456-1464
    • Salvay, D.M.1    Rives, C.B.2    Zhang, X.3    Chen, F.4    Kaufman, D.B.5    Lowe, W.L.6
  • 15
    • 77953651808 scopus 로고    scopus 로고
    • Self-assembling nanostructures to deliver angiogenic factors to pancreatic islets
    • L.W. Chow, L.-J. Wang, D.B. Kaufman, and S.I. Stupp Self-assembling nanostructures to deliver angiogenic factors to pancreatic islets Biomaterials 31 2010 6154 6161
    • (2010) Biomaterials , vol.31 , pp. 6154-6161
    • Chow, L.W.1    Wang, L.-J.2    Kaufman, D.B.3    Stupp, S.I.4
  • 16
    • 33750469720 scopus 로고    scopus 로고
    • Isolated pancreatic islets in three-dimensional matrices are responsive to stimulators and inhibitors of angiogenesis
    • A. Kidszun, D. Schneider, D. Erb, G. Hertl, V. Schmidt, and M. Eckhard Isolated pancreatic islets in three-dimensional matrices are responsive to stimulators and inhibitors of angiogenesis Cell Transplant 15 2006 489 497
    • (2006) Cell Transplant , vol.15 , pp. 489-497
    • Kidszun, A.1    Schneider, D.2    Erb, D.3    Hertl, G.4    Schmidt, V.5    Eckhard, M.6
  • 17
    • 70350726217 scopus 로고    scopus 로고
    • Anti-inflammatory peptide-functionalized hydrogels for insulin-secreting cell encapsulation
    • J. Su, B.-H. Hu, W.L. Lowe, D.B. Kaufman, and P.B. Messersmith Anti-inflammatory peptide-functionalized hydrogels for insulin-secreting cell encapsulation Biomaterials 31 2010 308 314
    • (2010) Biomaterials , vol.31 , pp. 308-314
    • Su, J.1    Hu, B.-H.2    Lowe, W.L.3    Kaufman, D.B.4    Messersmith, P.B.5
  • 18
    • 33847617011 scopus 로고    scopus 로고
    • Mechanisms of action of glucagon-like peptide 1 in the pancreas
    • M.E. Doyle, and J.M. Egan Mechanisms of action of glucagon-like peptide 1 in the pancreas Pharmacol Ther 113 2007 546 593
    • (2007) Pharmacol Ther , vol.113 , pp. 546-593
    • Doyle, M.E.1    Egan, J.M.2
  • 19
    • 0037312818 scopus 로고    scopus 로고
    • Glucagon-like peptides: Regulators of cell proliferation, differentiation, and apoptosis
    • D.J. Drucker Glucagon-like peptides: regulators of cell proliferation, differentiation, and apoptosis Mol Endocrinol 17 2003 161 171
    • (2003) Mol Endocrinol , vol.17 , pp. 161-171
    • Drucker, D.J.1
  • 20
    • 0037181507 scopus 로고    scopus 로고
    • NMR studies of the aggregation of glucagon-like peptide-1: Formation of a symmetric helical dimer
    • X. Chang, D. Keller, S.I. O'Donoghue, and J.J. Led NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer FEBS Lett 515 2002 165 170
    • (2002) FEBS Lett , vol.515 , pp. 165-170
    • Chang, X.1    Keller, D.2    O'Donoghue, S.I.3    Led, J.J.4
  • 22
    • 73649107900 scopus 로고    scopus 로고
    • Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor
    • C. Underwood, P. Garibay, L. Knudsen, S. Hastrup, G. Peters, and R. Rudolph Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor J Biol Chem 285 1 2010 723 730
    • (2010) J Biol Chem , vol.285 , Issue.1 , pp. 723-730
    • Underwood, C.1    Garibay, P.2    Knudsen, L.3    Hastrup, S.4    Peters, G.5    Rudolph, R.6
  • 23
    • 33751504607 scopus 로고    scopus 로고
    • Caveolin-1 regulates cellular trafficking and function of the glucagon-like Peptide 1 receptor
    • C.A. Syme, L. Zhang, and A. Bisello Caveolin-1 regulates cellular trafficking and function of the glucagon-like Peptide 1 receptor Mol Endocrinol 20 2006 3400 3411
    • (2006) Mol Endocrinol , vol.20 , pp. 3400-3411
    • Syme, C.A.1    Zhang, L.2    Bisello, A.3
  • 25
    • 11144319307 scopus 로고    scopus 로고
    • Synthesis, bioactivity and specificity of glucagon-like peptide-1 (7-37)/polymer conjugate to isolated rat islets
    • S. Kim, S. Wan Kim, and Y.H. Bae Synthesis, bioactivity and specificity of glucagon-like peptide-1 (7-37)/polymer conjugate to isolated rat islets Biomaterials 26 2005 3597 3606
    • (2005) Biomaterials , vol.26 , pp. 3597-3606
    • Kim, S.1    Wan Kim, S.2    Bae, Y.H.3
  • 26
    • 77954518307 scopus 로고    scopus 로고
    • Encapsulation of pancreatic islets within nano-thin functional polyethylene glycol coatings for enhanced insulin secretion
    • S. Kizilel, A. Scavone, X. Liu, J.M. Nothias, D. Ostrega, and P. Witkowski Encapsulation of pancreatic islets within nano-thin functional polyethylene glycol coatings for enhanced insulin secretion Tissue Eng Part A 16 2010 2217 2228
    • (2010) Tissue Eng Part A , vol.16 , pp. 2217-2228
    • Kizilel, S.1    Scavone, A.2    Liu, X.3    Nothias, J.M.4    Ostrega, D.5    Witkowski, P.6
  • 27
    • 70349190405 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 functionalized PEG hydrogels promote survival and function of encapsulated pancreatic beta-cells
    • C. Lin, and K. Anseth Glucagon-like peptide-1 functionalized PEG hydrogels promote survival and function of encapsulated pancreatic beta-cells Biomacromolecules 10 9 2009 2460 2467
    • (2009) Biomacromolecules , vol.10 , Issue.9 , pp. 2460-2467
    • Lin, C.1    Anseth, K.2
  • 28
    • 0031603860 scopus 로고    scopus 로고
    • Protein-like molecular architecture: Biomaterial applications for inducing cellular receptor binding and signal transduction
    • G.B. Fields, J.L. Lauer, Y. Dori, P. Forns, Y.C. Yu, and M. Tirrell Protein-like molecular architecture: biomaterial applications for inducing cellular receptor binding and signal transduction Biopolymers 47 1998 143 151
    • (1998) Biopolymers , vol.47 , pp. 143-151
    • Fields, G.B.1    Lauer, J.L.2    Dori, Y.3    Forns, P.4    Yu, Y.C.5    Tirrell, M.6
  • 29
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • J.D. Hartgerink, E. Beniash, and S.I. Stupp Self-assembly and mineralization of peptide-amphiphile nanofibers Science 294 2001 1684 1688
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 30
    • 0037117498 scopus 로고    scopus 로고
    • Peptide-amphiphile nanofibers: A versatile scaffold for the preparation of self-assembling materials
    • J.D. Hartgerink, E. Beniash, and S.I. Stupp Peptide-amphiphile nanofibers: a versatile scaffold for the preparation of self-assembling materials Proc Natl Acad Sci USA 99 2002 5133 5138
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5133-5138
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 31
    • 58149101861 scopus 로고    scopus 로고
    • Molecular self-assembly into one-dimensional nanostructures
    • L.C. Palmer, and S.I. Stupp Molecular self-assembly into one-dimensional nanostructures Acc Chem Res 41 2008 1674 1684
    • (2008) Acc Chem Res , vol.41 , pp. 1674-1684
    • Palmer, L.C.1    Stupp, S.I.2
  • 33
    • 33744946043 scopus 로고    scopus 로고
    • Self-assembly of peptide-amphiphile nanofibers: The roles of hydrogen bonding and amphiphilic packing
    • S.E. Paramonov, H.-W. Jun, and J.D. Hartgerink Self-assembly of peptide-amphiphile nanofibers: the roles of hydrogen bonding and amphiphilic packing J Am Chem Soc 128 2006 7291 7298
    • (2006) J Am Chem Soc , vol.128 , pp. 7291-7298
    • Paramonov, S.E.1    Jun, H.-W.2    Hartgerink, J.D.3
  • 34
    • 19944414362 scopus 로고    scopus 로고
    • Probing the interior of peptide amphiphile supramolecular aggregates
    • J.D. Tovar, R.C. Claussen, and S.I. Stupp Probing the interior of peptide amphiphile supramolecular aggregates J Am Chem Soc 127 2005 7337 7345
    • (2005) J Am Chem Soc , vol.127 , pp. 7337-7345
    • Tovar, J.D.1    Claussen, R.C.2    Stupp, S.I.3
  • 35
    • 40549086613 scopus 로고    scopus 로고
    • Molecular simulation study of peptide amphiphile self-assembly
    • Y.S. Velichko, S.I. Stupp, and M.O. de la Cruz Molecular simulation study of peptide amphiphile self-assembly J Phys Chem B 112 2008 2326 2334
    • (2008) J Phys Chem B , vol.112 , pp. 2326-2334
    • Velichko, Y.S.1    Stupp, S.I.2    De La Cruz, M.O.3
  • 36
    • 33644885444 scopus 로고    scopus 로고
    • Intermolecular forces in the self-assembly of peptide amphiphile nanofibers
    • J.C. Stendahl, M.S. Rao, M.O. Guler, and S.I. Stupp Intermolecular forces in the self-assembly of peptide amphiphile nanofibers Adv Funct Mater 16 2006 499 508
    • (2006) Adv Funct Mater , vol.16 , pp. 499-508
    • Stendahl, J.C.1    Rao, M.S.2    Guler, M.O.3    Stupp, S.I.4
  • 38
    • 0037841389 scopus 로고    scopus 로고
    • Characterization of peptide-amphiphiles possessing cellular activation sequences
    • N.B. Malkar, J.L. Lauer-Fields, D. Juska, and G.B. Fields Characterization of peptide-amphiphiles possessing cellular activation sequences Biomacromolecules 4 2003 518 528
    • (2003) Biomacromolecules , vol.4 , pp. 518-528
    • Malkar, N.B.1    Lauer-Fields, J.L.2    Juska, D.3    Fields, G.B.4
  • 40
    • 44349108852 scopus 로고    scopus 로고
    • Peptide amphiphile nanostructure-heparin interactions and their relationship to bioactivity
    • K. Rajangam, M.S. Arnold, M.A. Rocco, and S.I. Stupp Peptide amphiphile nanostructure-heparin interactions and their relationship to bioactivity Biomaterials 29 2008 3298 3305
    • (2008) Biomaterials , vol.29 , pp. 3298-3305
    • Rajangam, K.1    Arnold, M.S.2    Rocco, M.A.3    Stupp, S.I.4
  • 43
    • 13644268564 scopus 로고    scopus 로고
    • Coassembly of amphiphiles with opposite peptide polarities into nanofibers
    • H.A. Behanna, J.J.J.M. Donners, A.C. Gordon, and S.I. Stupp Coassembly of amphiphiles with opposite peptide polarities into nanofibers J Am Chem Soc 127 2005 1193 1200
    • (2005) J Am Chem Soc , vol.127 , pp. 1193-1200
    • Behanna, H.A.1    Donners, J.J.J.M.2    Gordon, A.C.3    Stupp, S.I.4
  • 44
    • 33846235173 scopus 로고    scopus 로고
    • Modulation of fluorescence through coassembly of molecules in organic nanostructures
    • H.A. Behanna, K. Rajangam, and S.I. Stupp Modulation of fluorescence through coassembly of molecules in organic nanostructures J Am Chem Soc 129 2007 321 327
    • (2007) J Am Chem Soc , vol.129 , pp. 321-327
    • Behanna, H.A.1    Rajangam, K.2    Stupp, S.I.3
  • 45
    • 0038789021 scopus 로고    scopus 로고
    • Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction
    • K.L. Niece, J.D. Hartgerink, J.J.J.M. Donners, and S.I. Stupp Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction J Am Chem Soc 125 2003 7146 7147
    • (2003) J Am Chem Soc , vol.125 , pp. 7146-7147
    • Niece, K.L.1    Hartgerink, J.D.2    Donners, J.J.J.M.3    Stupp, S.I.4
  • 46
    • 1442281238 scopus 로고    scopus 로고
    • Selective differentiation of neural progenitor cells by high-epitope density nanofibers
    • G.A. Silva, C. Czeisler, K.L. Niece, E. Beniash, D.A. Harrington, and J.A. Kessler Selective differentiation of neural progenitor cells by high-epitope density nanofibers Science 303 2004 1352 1355
    • (2004) Science , vol.303 , pp. 1352-1355
    • Silva, G.A.1    Czeisler, C.2    Niece, K.L.3    Beniash, E.4    Harrington, D.A.5    Kessler, J.A.6
  • 50
    • 52049092122 scopus 로고    scopus 로고
    • Growth factor delivery from self-assembling nanofibers to facilitate islet transplantation
    • J.C. Stendahl, L.-J. Wang, L.W. Chow, D.B. Kaufman, and S.I. Stupp Growth factor delivery from self-assembling nanofibers to facilitate islet transplantation Transplantation 86 2008 478 481
    • (2008) Transplantation , vol.86 , pp. 478-481
    • Stendahl, J.C.1    Wang, L.-J.2    Chow, L.W.3    Kaufman, D.B.4    Stupp, S.I.5
  • 51
    • 56949086428 scopus 로고    scopus 로고
    • Incretin-based therapies in type 2 diabetes: A review of clinical results
    • E. Bosi, P. Lucotti, E. Setola, L. Monti, and P.M. Piatti Incretin-based therapies in type 2 diabetes: a review of clinical results Diabetes Res Clin Pract 82 Suppl 2 2008 S102 S107
    • (2008) Diabetes Res Clin Pract , vol.82 , Issue.SUPPL. 2
    • Bosi, E.1    Lucotti, P.2    Setola, E.3    Monti, L.4    Piatti, P.M.5
  • 52
    • 0141461415 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 receptor is involved in learning and neuroprotection
    • M.J. During, L. Cao, D.S. Zuzga, J.S. Francis, H.L. Fitzsimons, and X. Jiao Glucagon-like peptide-1 receptor is involved in learning and neuroprotection Nat Med 9 2003 1173 1179
    • (2003) Nat Med , vol.9 , pp. 1173-1179
    • During, M.J.1    Cao, L.2    Zuzga, D.S.3    Francis, J.S.4    Fitzsimons, H.L.5    Jiao, X.6
  • 53
    • 0031690479 scopus 로고    scopus 로고
    • Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for type 2 diabetes
    • J.J. Holst, and C.F. Deacon Inhibition of the activity of dipeptidyl-peptidase IV as a treatment for type 2 diabetes Diabetes 47 1998 1663 1670
    • (1998) Diabetes , vol.47 , pp. 1663-1670
    • Holst, J.J.1    Deacon, C.F.2
  • 54
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • N.J. Greenfield Using circular dichroism spectra to estimate protein secondary structure Nat Protoc 1 2006 2876 2890
    • (2006) Nat Protoc , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 55
    • 0031543338 scopus 로고    scopus 로고
    • A set of constructed type spectra for the practical estimation of peptide secondary structure from circular dichroism
    • J. Reed, and T.A. Reed A set of constructed type spectra for the practical estimation of peptide secondary structure from circular dichroism Anal Biochem 254 1997 36 40
    • (1997) Anal Biochem , vol.254 , pp. 36-40
    • Reed, J.1    Reed, T.A.2
  • 56
    • 0035340019 scopus 로고    scopus 로고
    • Insulinotropic actions of exendin-4 and glucagon-like peptide-1 in vivo and in vitro
    • D.G. Parkes, R. Pittner, C. Jodka, P. Smith, and A. Young Insulinotropic actions of exendin-4 and glucagon-like peptide-1 in vivo and in vitro Metab Clin Exp 50 2001 583 589
    • (2001) Metab Clin Exp , vol.50 , pp. 583-589
    • Parkes, D.G.1    Pittner, R.2    Jodka, C.3    Smith, P.4    Young, A.5
  • 57
    • 58849146524 scopus 로고    scopus 로고
    • The reversal of hyperglycaemia in diabetic mice using PLGA scaffolds seeded with islet-like cells derived from human embryonic stem cells
    • G.H. Mao, G.A. Chen, H.Y. Bai, T.R. Song, and Y.X. Wang The reversal of hyperglycaemia in diabetic mice using PLGA scaffolds seeded with islet-like cells derived from human embryonic stem cells Biomaterials 30 2009 1706 1714
    • (2009) Biomaterials , vol.30 , pp. 1706-1714
    • Mao, G.H.1    Chen, G.A.2    Bai, H.Y.3    Song, T.R.4    Wang, Y.X.5
  • 58
    • 64149118087 scopus 로고    scopus 로고
    • Highly efficient differentiation of human ES cells and iPS cells into mature pancreatic insulin-producing cells
    • D. Zhang, W. Jiang, M. Liu, X. Sui, X. Yin, and S. Chen Highly efficient differentiation of human ES cells and iPS cells into mature pancreatic insulin-producing cells Cell Res 19 2009 429 438
    • (2009) Cell Res , vol.19 , pp. 429-438
    • Zhang, D.1    Jiang, W.2    Liu, M.3    Sui, X.4    Yin, X.5    Chen, S.6
  • 59
    • 0037357951 scopus 로고    scopus 로고
    • GLP-1 receptor agonists are growth and differentiation factors for pancreatic islet beta cells
    • J.M. Egan, A. Bulotta, H. Hui, and R. Perfetti GLP-1 receptor agonists are growth and differentiation factors for pancreatic islet beta cells Diabetes Metab Res Rev 19 2003 115 123
    • (2003) Diabetes Metab Res Rev , vol.19 , pp. 115-123
    • Egan, J.M.1    Bulotta, A.2    Hui, H.3    Perfetti, R.4
  • 60
    • 34247506810 scopus 로고    scopus 로고
    • Nanostructures by self-assembling peptide amphiphile as potential selective drug carriers
    • A. Accardo, D. Tesauro, G. Mangiapia, C. Pedone, and G. Morelli Nanostructures by self-assembling peptide amphiphile as potential selective drug carriers Biopolymers 88 2007 115 121
    • (2007) Biopolymers , vol.88 , pp. 115-121
    • Accardo, A.1    Tesauro, D.2    Mangiapia, G.3    Pedone, C.4    Morelli, G.5


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