메뉴 건너뛰기




Volumn 6, Issue 1-3, 2015, Pages 19-29

Investigation of the Potential of Hemp, Pea, Rice and Soy Protein Hydrolysates as a Source of Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Peptides

Author keywords

Bioactive peptides; Dipeptidyl peptidase IV inhibition; Hemp; Pea; Rice; Simulated gastrointestinal digestion; Soy

Indexed keywords


EID: 84950294662     PISSN: 18691978     EISSN: 18691986     Source Type: Journal    
DOI: 10.1007/s13228-015-0039-2     Document Type: Article
Times cited : (71)

References (42)
  • 1
    • 33745128793 scopus 로고    scopus 로고
    • Enhancing the action of incretin hormones: a new whey forward?
    • COI: 1:CAS:528:DC%2BD2
    • Drucker DJ (2006) Enhancing the action of incretin hormones: a new whey forward? Endocrinology 147:3171–3172
    • (2006) Endocrinology , vol.147 , pp. 3171-3172
    • Drucker, D.J.1
  • 2
    • 33744814340 scopus 로고    scopus 로고
    • Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV
    • COI: 1:CAS:528:DC%2BD2
    • Bjelke JR, Christensen J, Nielsen PF, Branner S, Kanstrup AB, Wagtmann N, Rasmussen HB (2006) Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV. Biochem J 396:391–399
    • (2006) Biochem J , vol.396 , pp. 391-399
    • Bjelke, J.R.1    Christensen, J.2    Nielsen, P.F.3    Branner, S.4    Kanstrup, A.B.5    Wagtmann, N.6    Rasmussen, H.B.7
  • 3
    • 84897390441 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV and its inhibitors: therapeutics for type 2 diabetes and what else?
    • COI: 1:CAS:528:DC%2B
    • Juillerat-Jeanneret L (2014) Dipeptidyl peptidase IV and its inhibitors: therapeutics for type 2 diabetes and what else? J Med Chem 57:2197–2212
    • (2014) J Med Chem , vol.57 , pp. 2197-2212
    • Juillerat-Jeanneret, L.1
  • 4
    • 84884178268 scopus 로고    scopus 로고
    • Linagliptin: a thorough characterization beyond its clinical efficacy
    • Sortino MA, Sinagra T, Canonico PL (2013) Linagliptin: a thorough characterization beyond its clinical efficacy. Front Endocrinol 4:(Article 16) 11–19
    • (2013) Front Endocrinol , vol.4 , Issue.Article 16 , pp. 11-19
    • Sortino, M.A.1    Sinagra, T.2    Canonico, P.L.3
  • 5
    • 84891428257 scopus 로고    scopus 로고
    • Overview of food products and dietary constituents with antidiabetic properties and their putative mechanisms of action: a natural approach to complement pharmacotherapy in the management of diabetes
    • COI: 1:CAS:528:DC%2B
    • Lacroix IME, Li-Chan ECY (2014) Overview of food products and dietary constituents with antidiabetic properties and their putative mechanisms of action: a natural approach to complement pharmacotherapy in the management of diabetes. Mol Nutr Food Res 58:61–78
    • (2014) Mol Nutr Food Res , vol.58 , pp. 61-78
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 6
    • 84860318855 scopus 로고    scopus 로고
    • Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach
    • COI: 1:CAS:528:DC%2BC3
    • Lacroix IME, Li-Chan ECY (2012) Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach. J Funct Foods 4:403–422
    • (2012) J Funct Foods , vol.4 , pp. 403-422
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 7
    • 84903131059 scopus 로고    scopus 로고
    • An in silico model to predict the potential of dietary proteins as sources of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides
    • COI: 1:CAS:528:DC%2B
    • Nongonierma AB, FitzGerald RJ (2014) An in silico model to predict the potential of dietary proteins as sources of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides. Food Chem 165:489–498
    • (2014) Food Chem , vol.165 , pp. 489-498
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 8
    • 84887112623 scopus 로고    scopus 로고
    • In silico analysis of the large and small subunits of cereal RuBisCO as precursors of cryptic bioactive peptides
    • COI: 1:CAS:528:DC%2B
    • Udenigwe CC, Gong M, Wu S (2013) In silico analysis of the large and small subunits of cereal RuBisCO as precursors of cryptic bioactive peptides. Process Biochem 48:1794–1799
    • (2013) Process Biochem , vol.48 , pp. 1794-1799
    • Udenigwe, C.C.1    Gong, M.2    Wu, S.3
  • 9
    • 84861332110 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates
    • COI: 1:CAS:528:DC%2BC3
    • Lacroix IME, Li-Chan ECY (2012) Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates. Int Dairy J 25:97–102
    • (2012) Int Dairy J , vol.25 , pp. 97-102
    • Lacroix, I.M.E.1    Li-Chan, E.C.Y.2
  • 10
    • 84871549211 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk-derived dipeptides and hydrolysates
    • COI: 1:CAS:528:DC%2BC3
    • Nongonierma AB, FitzGerald RJ (2013) Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk-derived dipeptides and hydrolysates. Peptides 39:157–163
    • (2013) Peptides , vol.39 , pp. 157-163
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 11
    • 84878313919 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin
    • COI: 1:CAS:528:DC%2BC3
    • Silveira ST, Martínez-Maqueda D, Recio I, Hernández-Ledesma B (2013) Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin. Food Chem 141:1072–1077
    • (2013) Food Chem , vol.141 , pp. 1072-1077
    • Silveira, S.T.1    Martínez-Maqueda, D.2    Recio, I.3    Hernández-Ledesma, B.4
  • 12
    • 79952799368 scopus 로고    scopus 로고
    • Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors
    • COI: 1:CAS:528:DC%2BC3
    • Tulipano G, Sibilia V, Caroli AM, Cocchi D (2011) Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors. Peptides 32:835–838
    • (2011) Peptides , vol.32 , pp. 835-838
    • Tulipano, G.1    Sibilia, V.2    Caroli, A.M.3    Cocchi, D.4
  • 13
    • 80052897910 scopus 로고    scopus 로고
    • Novel dipeptidyl peptidase-4-inhibiting peptide derived from β-lactoglobulin
    • COI: 1:CAS:528:DC%2B
    • Uchida M, Ohshiba Y, Mogami O (2011) Novel dipeptidyl peptidase-4-inhibiting peptide derived from β-lactoglobulin. J Pharmacol Sci 117:63–66
    • (2011) J Pharmacol Sci , vol.117 , pp. 63-66
    • Uchida, M.1    Ohshiba, Y.2    Mogami, O.3
  • 14
    • 82655173852 scopus 로고    scopus 로고
    • Isolation and identification of casein-derived dipeptidyl-peptidase 4 (DPP-4)-inhibitory peptide LPQNIPPL from gouda-type cheese and its effect on plasma glucose in rats
    • COI: 1:CAS:528:DC%2B
    • Uenishi H, Kabuki T, Seto Y, Serizawa A, Nakajima H (2012) Isolation and identification of casein-derived dipeptidyl-peptidase 4 (DPP-4)-inhibitory peptide LPQNIPPL from gouda-type cheese and its effect on plasma glucose in rats. Int Dairy J 22:24–30
    • (2012) Int Dairy J , vol.22 , pp. 24-30
    • Uenishi, H.1    Kabuki, T.2    Seto, Y.3    Serizawa, A.4    Nakajima, H.5
  • 15
    • 84860295841 scopus 로고    scopus 로고
    • Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran
    • COI: 1:CAS:528:DC%2BC3
    • Hatanaka T et al (2012) Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran. Food Chem 134:797–802
    • (2012) Food Chem , vol.134 , pp. 797-802
    • Hatanaka, T.1
  • 16
    • 84891647698 scopus 로고    scopus 로고
    • In vitro α-glucosidase, angiotensin converting enzyme and dipeptidyl peptidase-IV inhibitory properties of brewers’ spent grain protein hydrolysates
    • COI: 1:CAS:528:DC%2BC2
    • Connolly A, Piggott CO, FitzGerald RJ (2014) In vitro α-glucosidase, angiotensin converting enzyme and dipeptidyl peptidase-IV inhibitory properties of brewers’ spent grain protein hydrolysates. Food Res Int 56:100–107
    • (2014) Food Res Int , vol.56 , pp. 100-107
    • Connolly, A.1    Piggott, C.O.2    FitzGerald, R.J.3
  • 18
    • 84887497662 scopus 로고    scopus 로고
    • In vitro assessment of the cardioprotective, anti-diabetic and antioxidant potential of Palmaria palmata protein hydrolysates
    • COI: 1:CAS:528:DC%2B
    • Harnedy PA, FitzGerald RJ (2013) In vitro assessment of the cardioprotective, anti-diabetic and antioxidant potential of Palmaria palmata protein hydrolysates. J Appl Phycol 25:1793–1803
    • (2013) J Appl Phycol , vol.25 , pp. 1793-1803
    • Harnedy, P.A.1    FitzGerald, R.J.2
  • 19
    • 84859788742 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates
    • COI: 1:CAS:528:DC%2BC3
    • Huang S-L, Jao C-L, Ho K-P, Hsu K-C (2012) Dipeptidyl-peptidase IV inhibitory activity of peptides derived from tuna cooking juice hydrolysates. Peptides 35:114–121
    • (2012) Peptides , vol.35 , pp. 114-121
    • Huang, S.-L.1    Jao, C.-L.2    Ho, K.-P.3    Hsu, K.-C.4
  • 20
    • 84887176534 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory peptides generated in Spanish dry-cured ham
    • COI: 1:CAS:528:DC%2B
    • Gallego M, Aristoy M-C, Toldrá F (2014) Dipeptidyl peptidase IV inhibitory peptides generated in Spanish dry-cured ham. Meat Sci 96:757–761
    • (2014) Meat Sci , vol.96 , pp. 757-761
    • Gallego, M.1    Aristoy, M.-C.2    Toldrá, F.3
  • 21
    • 84856555742 scopus 로고    scopus 로고
    • Peptides derived from Atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors
    • COI: 1:CAS:528:DC%2BC38X
    • Li-Chan ECY, Hunag S-L, Jao C-L, Ho K-P, Hsu K-C (2012) Peptides derived from Atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors. J Agric Food Chem 60:973–978
    • (2012) J Agric Food Chem , vol.60 , pp. 973-978
    • Li-Chan, E.C.Y.1    Hunag, S.-L.2    Jao, C.-L.3    Ho, K.-P.4    Hsu, K.-C.5
  • 22
    • 84950251031 scopus 로고    scopus 로고
    • Hsu K-C, Tung Y-S, Huang S-L, Jao C-L (2013) Dipeptidyl peptidase-IV inhibitory activity of peptides in porcine skin gelatin hydrolysates. In: Hernández-Ledesma B (ed) Bioactive food peptides in health and disease. In Tech, pp 20
    • Hsu K-C, Tung Y-S, Huang S-L, Jao C-L (2013) Dipeptidyl peptidase-IV inhibitory activity of peptides in porcine skin gelatin hydrolysates. In: Hernández-Ledesma B (ed) Bioactive food peptides in health and disease. In Tech, http://www.intechopen.com/books/bioactive-food-peptides-in-health-and-disease/dipeptidyl-peptidase-iv-inhibitory-activity-of-peptides-in-porcine-skin-gelatin-hydrolysates. DOI: 10.5772/51264, pp 205–218.
  • 23
    • 84926315093 scopus 로고    scopus 로고
    • Porcine skin gelatin hydrolysate as a dipeptidyl peptidase IV inhibitor improves glycemic control in streptozotocin-induced diabetic rats
    • COI: 1:CAS:528:DC%2B
    • Huang S-L, Hung C-C, Jao C-L, Tung Y-S, Hsu K-C (2014) Porcine skin gelatin hydrolysate as a dipeptidyl peptidase IV inhibitor improves glycemic control in streptozotocin-induced diabetic rats. J Funct Foods 11:235–242
    • (2014) J Funct Foods , vol.11 , pp. 235-242
    • Huang, S.-L.1    Hung, C.-C.2    Jao, C.-L.3    Tung, Y.-S.4    Hsu, K.-C.5
  • 24
    • 0021230368 scopus 로고
    • Diprotins A and B, inhibitors of dipeptidyl aminopeptidase IV, produced by bacteria
    • COI: 1:CAS:528:DyaL2
    • Umezawa H, Aoyagi T, Ogawa K, Naganawa H, Hamada M, Takeuchi T (1984) Diprotins A and B, inhibitors of dipeptidyl aminopeptidase IV, produced by bacteria. J Antibiot 37:422–425
    • (1984) J Antibiot , vol.37 , pp. 422-425
    • Umezawa, H.1    Aoyagi, T.2    Ogawa, K.3    Naganawa, H.4    Hamada, M.5    Takeuchi, T.6
  • 25
    • 84900322939 scopus 로고    scopus 로고
    • Savinase the most suitable enzyme for releasing peptides from lentil (Lens culinaris var. Castellana) protein concentrates with multifunctional properties
    • COI: 1:CAS:528:DC%2BC2
    • Garcia Mora P, Peñas E, Frias J, Martinez-Villaluenga C (2014) Savinase the most suitable enzyme for releasing peptides from lentil (Lens culinaris var. Castellana) protein concentrates with multifunctional properties. J Agric Food Chem 62(18):4166–4174
    • (2014) J Agric Food Chem , vol.62 , Issue.18 , pp. 4166-4174
    • Garcia Mora, P.1    Peñas, E.2    Frias, J.3    Martinez-Villaluenga, C.4
  • 26
    • 84895072632 scopus 로고    scopus 로고
    • Structural and functional characterization of hemp seed (Cannabis sativa L.) protein-derived antioxidant and antihypertensive peptides
    • COI: 1:CAS:528:DC%2B
    • Girgih AT, He R, Malomo S, Offengenden M, Wu J, Aluko RE (2014) Structural and functional characterization of hemp seed (Cannabis sativa L.) protein-derived antioxidant and antihypertensive peptides. J Funct Foods 6:384–394
    • (2014) J Funct Foods , vol.6 , pp. 384-394
    • Girgih, A.T.1    He, R.2    Malomo, S.3    Offengenden, M.4    Wu, J.5    Aluko, R.E.6
  • 27
    • 84895882145 scopus 로고    scopus 로고
    • Bioactive peptides and hydrolysates from pulses and their potential use as functional ingredients
    • López‐Barrios L, Gutiérrez‐Uribe JA, Serna‐Saldívar SO (2014) Bioactive peptides and hydrolysates from pulses and their potential use as functional ingredients. J Food Sci 79:R273–R283
    • (2014) J Food Sci , vol.79 , pp. 273-283
    • López‐Barrios, L.1    Gutiérrez‐Uribe, J.A.2    Serna‐Saldívar, S.O.3
  • 28
    • 84894521429 scopus 로고    scopus 로고
    • Functional significance of bioactive peptides derived from soybean
    • COI: 1:CAS:528:DC%2BC2
    • Singh BP, Vij S, Hati S (2014) Functional significance of bioactive peptides derived from soybean. Peptides 54:171–179
    • (2014) Peptides , vol.54 , pp. 171-179
    • Singh, B.P.1    Vij, S.2    Hati, S.3
  • 29
    • 84872837670 scopus 로고    scopus 로고
    • Systematic analysis of a dipeptide library for inhibitor development using human dipeptidyl peptidase IV produced by a Saccharomyces cerevisiae expression system
    • COI: 1:CAS:528:DC%2BC3sX
    • Hikida A, Ito K, Motoyama T, Kato R, Kawarasaki Y (2013) Systematic analysis of a dipeptide library for inhibitor development using human dipeptidyl peptidase IV produced by a Saccharomyces cerevisiae expression system. Biochem Biophys Res Commun 430:1217–1222
    • (2013) Biochem Biophys Res Commun , vol.430 , pp. 1217-1222
    • Hikida, A.1    Ito, K.2    Motoyama, T.3    Kato, R.4    Kawarasaki, Y.5
  • 30
    • 84894541962 scopus 로고    scopus 로고
    • Trp-Arg-Xaa tripeptides act as uncompetitive-type inhibitors of human dipeptidyl peptidase IV
    • COI: 1:CAS:528:DC%2BC2
    • Lan VTT, Ito K, Ito S, Kawarasaki Y (2014) Trp-Arg-Xaa tripeptides act as uncompetitive-type inhibitors of human dipeptidyl peptidase IV. Peptides 54:166–170
    • (2014) Peptides , vol.54 , pp. 166-170
    • Lan, V.T.T.1    Ito, K.2    Ito, S.3    Kawarasaki, Y.4
  • 31
    • 84888165809 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides
    • COI: 1:CAS:528:DC%2B
    • Nongonierma AB, FitzGerald RJ (2013) Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides. Food Funct 4:1843–1849
    • (2013) Food Funct , vol.4 , pp. 1843-1849
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 32
    • 84943353421 scopus 로고    scopus 로고
    • Dietary protein quality evaluation in human nutrition. Report of an FAO Expert Consultation
    • FAO (2013) Dietary protein quality evaluation in human nutrition. Report of an FAO Expert Consultation. FAO Food Nutr Pap 92:1–79
    • (2013) FAO Food Nutr Pap , vol.92 , pp. 1-79
  • 33
    • 84877836950 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: influence of fractionation, stability to simulated gastrointestinal digestion and food-drug interaction
    • COI: 1:CAS:528:DC%2BC3
    • Nongonierma AB, FitzGerald RJ (2013) Dipeptidyl peptidase IV inhibitory properties of a whey protein hydrolysate: influence of fractionation, stability to simulated gastrointestinal digestion and food-drug interaction. Int Dairy J 32:33–39
    • (2013) Int Dairy J , vol.32 , pp. 33-39
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 34
    • 8344266947 scopus 로고    scopus 로고
    • In vitro generation and stability of the lactokinin β-lactoglobulin fragment (142–148)
    • COI: 1:CAS:528:DC%2BD2
    • Walsh DJ et al (2004) In vitro generation and stability of the lactokinin β-lactoglobulin fragment (142–148). J Dairy Sci 87:3845–3857
    • (2004) J Dairy Sci , vol.87 , pp. 3845-3857
    • Walsh, D.J.1
  • 36
    • 58749101498 scopus 로고    scopus 로고
    • Bitterness in Bacillus proteinase hydrolysates of whey proteins
    • COI: 1:CAS:528:DC%2BD1
    • Spellman D, O’Cuinn G, FitzGerald RJ (2009) Bitterness in Bacillus proteinase hydrolysates of whey proteins. Food Chem 114:440–446
    • (2009) Food Chem , vol.114 , pp. 440-446
    • Spellman, D.1    O’Cuinn, G.2    FitzGerald, R.J.3
  • 37
    • 84865324339 scopus 로고    scopus 로고
    • Tryptophan-containing milk protein-derived dipeptides inhibit xanthine oxidase
    • COI: 1:CAS:528:DC%2B
    • Nongonierma AB, FitzGerald RJ (2012) Tryptophan-containing milk protein-derived dipeptides inhibit xanthine oxidase. Peptides 37:263–272
    • (2012) Peptides , vol.37 , pp. 263-272
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 38
    • 0026638586 scopus 로고
    • Extensive comparison of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching
    • COI: 1:CAS:528:DyaK3
    • Groen H, Meldal M, Breddam K (1992) Extensive comparison of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching. Biochemistry 31:6011–6018
    • (1992) Biochemistry , vol.31 , pp. 6011-6018
    • Groen, H.1    Meldal, M.2    Breddam, K.3
  • 39
    • 84910110593 scopus 로고    scopus 로고
    • Peptide array on cellulose support—a screening tool to identify peptides with dipeptidyl-peptidase IV inhibitory activity within the sequence of α-lactalbumin
    • COI: 1:CAS:528:DC%2B
    • Lacroix IM, Li-Chan EC (2014) Peptide array on cellulose support—a screening tool to identify peptides with dipeptidyl-peptidase IV inhibitory activity within the sequence of α-lactalbumin. Int J Mol Sci 15:20846–20858
    • (2014) Int J Mol Sci , vol.15 , pp. 20846-20858
    • Lacroix, I.M.1    Li-Chan, E.C.2
  • 40
    • 84888440672 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV (DPP-IV) by proline containing peptides
    • COI: 1:CAS:528:DC%2B
    • Nongonierma AB, FitzGerald RJ (2013) Inhibition of dipeptidyl peptidase IV (DPP-IV) by proline containing peptides. J Funct Foods 5:1909–1917
    • (2013) J Funct Foods , vol.5 , pp. 1909-1917
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 41
    • 84937977214 scopus 로고    scopus 로고
    • Characterisation of the potential of β-lactoglobulin and α-lactalbumin as sources of bioactive peptides affecting incretin function: in silico and in vitro comparative studies. Int Dairy J
    • Tulipano G, Faggi L, Nardone A, Cocchi D, Caroli AM (2015) Characterisation of the potential of β-lactoglobulin and α-lactalbumin as sources of bioactive peptides affecting incretin function: in silico and in vitro comparative studies. Int Dairy J. doi:10.1016/j.idairyj.2015.01.008
    • (2015) doi:10.1016/j.idairyj.2015.01.008
    • Tulipano, G.1    Faggi, L.2    Nardone, A.3    Cocchi, D.4    Caroli, A.M.5
  • 42
    • 84884602268 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides
    • COI: 1:CAS:528:DC%2BC3
    • Nongonierma AB, Mooney C, Shields DC, FitzGerald RJ (2013) Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides. Food Chem 141:644–653
    • (2013) Food Chem , vol.141 , pp. 644-653
    • Nongonierma, A.B.1    Mooney, C.2    Shields, D.C.3    FitzGerald, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.