메뉴 건너뛰기




Volumn 1854, Issue 1, 2015, Pages 73-83

Specificity studies on Kallikrein-related peptidase 7 (KLK7) and effects of osmolytes and glycosaminoglycans on its peptidase activity

Author keywords

Kallistatin; Kosmotropic salts; Proteolytic enzymes; Semaphorin; Skin

Indexed keywords

AMINO ACID; ANTHRANILIC ACID; GLUTAMIC ACID DERIVATIVE; GLUTAMINYL N [2,4 DINITROPHENYL] ETHYLENEDIAMINE; GLYCOSAMINOGLYCAN; INORGANIC SALT; KALLIKREIN; KININOGEN; PEPTIDASE; PYROGLUTAMIC ACID; RESIN; SEMAPHORIN; SEMAPHORIN 6B; SODIUM CHLORIDE; STRATUM CORNEUM CHYMOTRYPTIC ENZYME; SUBSTANCE P; UNCLASSIFIED DRUG; KALLISTATIN; KLK7 PROTEIN, HUMAN; PEPTIDE; PEPTIDE HYDROLASE; SERINE PROTEINASE INHIBITOR; SOMATOSTATIN;

EID: 84912118536     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.10.018     Document Type: Article
Times cited : (19)

References (75)
  • 2
    • 84912107241 scopus 로고    scopus 로고
    • Genomic structure of the KLK locus
    • V. Magdolen, C.P. Sommerhoff, H. Fritz, M. Schmitt, De Gruyter Berlin, Germany
    • D. Cretu, G.M. Yousef, A. Scorilas, and E.P. Diamandis Genomic structure of the KLK locus V. Magdolen, C.P. Sommerhoff, H. Fritz, M. Schmitt, Kallikrein - Related Peptidases vol. 1 2012 De Gruyter Berlin, Germany 5 29
    • (2012) Kallikrein - Related Peptidases , vol.1 , pp. 5-29
    • Cretu, D.1    Yousef, G.M.2    Scorilas, A.3    Diamandis, E.P.4
  • 3
    • 0034680333 scopus 로고    scopus 로고
    • Sequencing and expression analysis of the serine protease gene cluster located in chromosome 19q13 region
    • L. Gan, I. Lee, R. Smith, R. Argonza-Barrett, H. Lei, J. McCuaig, P. Moss, B. Paeper, and K. Wang Sequencing and expression analysis of the serine protease gene cluster located in chromosome 19q13 region Gene 257 2000 119 130
    • (2000) Gene , vol.257 , pp. 119-130
    • Gan, L.1    Lee, I.2    Smith, R.3    Argonza-Barrett, R.4    Lei, H.5    McCuaig, J.6    Moss, P.7    Paeper, B.8    Wang, K.9
  • 4
    • 0034534350 scopus 로고    scopus 로고
    • Tissue-specific expression patterns and fine mapping of the human kallikrein (KLK) locus on proximal 19q13.4
    • T.J. Harvey, J.D. Hooper, S.A. Myers, S.A. Stephenson, L.K. Ashworth, and J.A. Clements Tissue-specific expression patterns and fine mapping of the human kallikrein (KLK) locus on proximal 19q13.4 J. Biol. Chem. 275 2000 35397 35406
    • (2000) J. Biol. Chem. , vol.275 , pp. 35397-35406
    • Harvey, T.J.1    Hooper, J.D.2    Myers, S.A.3    Stephenson, S.A.4    Ashworth, L.K.5    Clements, J.A.6
  • 5
    • 0034675353 scopus 로고    scopus 로고
    • Genomic organization of the human kallikrein gene family on chromosome 19q13.3 - Q13.4
    • G.M. Yousef, A. Chang, A. Scorilas, and E.P. Diamandis Genomic organization of the human kallikrein gene family on chromosome 19q13.3 - q13.4 Biochem. Biophys. Res. Commun. 276 2000 125 133
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 125-133
    • Yousef, G.M.1    Chang, A.2    Scorilas, A.3    Diamandis, E.P.4
  • 7
    • 0025905696 scopus 로고
    • A chymotrypsin-like proteinase that may be involved in desquamation in plantar stratum corneum
    • T. Egelrud, and A. Lundstrom A chymotrypsin-like proteinase that may be involved in desquamation in plantar stratum corneum Arch. Dermatol. Res. 283 1991 108 112
    • (1991) Arch. Dermatol. Res. , vol.283 , pp. 108-112
    • Egelrud, T.1    Lundstrom, A.2
  • 8
    • 0027956112 scopus 로고
    • Cloning, expression and characterization of stratum corneum chymotryptic enzyme. A skin - Specific human serine proteinase
    • L. Hansson, M. Stromqvist, A. Backman, P. Wallbrandt, A. Carlstein, and T. Egelrud Cloning, expression and characterization of stratum corneum chymotryptic enzyme. A skin - specific human serine proteinase J. Biol. Chem. 269 1994 19420 19426
    • (1994) J. Biol. Chem. , vol.269 , pp. 19420-19426
    • Hansson, L.1    Stromqvist, M.2    Backman, A.3    Wallbrandt, P.4    Carlstein, A.5    Egelrud, T.6
  • 9
    • 84976223101 scopus 로고    scopus 로고
    • Kallikrein-related peptidases and inhibitors of the skin
    • V. Magdolen, C.P. Sommerhoff, H. Fritz, M. Schmitt, De Gruyter Berlin, Germany
    • M. Brattsand Kallikrein-related peptidases and inhibitors of the skin V. Magdolen, C.P. Sommerhoff, H. Fritz, M. Schmitt, Kallikrein - Related Peptidases vol. 1 2012 De Gruyter Berlin, Germany 329 347
    • (2012) Kallikrein - Related Peptidases , vol.1 , pp. 329-347
    • Brattsand, M.1
  • 13
    • 84883230192 scopus 로고    scopus 로고
    • Regulation of kallikrein-related peptidases in the skin - From physiology to diseases to therapeutic options
    • J. Fischer, and U. Meyer-Hoffert Regulation of kallikrein-related peptidases in the skin - from physiology to diseases to therapeutic options Thromb. Haemost. 110 2013 442 449
    • (2013) Thromb. Haemost. , vol.110 , pp. 442-449
    • Fischer, J.1    Meyer-Hoffert, U.2
  • 14
    • 34547634419 scopus 로고    scopus 로고
    • Distribution of 15 human kallikreins in tissues and biological fluids
    • J.L.V. Shaw, and E.P. Diamandis Distribution of 15 human kallikreins in tissues and biological fluids Clin. Chem. 53 2007 1423 1432
    • (2007) Clin. Chem. , vol.53 , pp. 1423-1432
    • Shaw, J.L.V.1    Diamandis, E.P.2
  • 15
    • 1842608440 scopus 로고    scopus 로고
    • Development of an immunofluorometric assay and quantification of human kallikrein 7 in tissue extracts and biological fluids
    • T. Kishi, A. Soosaipillai, L. Grass, S.P. Little, E.M. Johnstone, and E.P. Diamandis Development of an immunofluorometric assay and quantification of human kallikrein 7 in tissue extracts and biological fluids Clin. Chem. 50 2004 709 716
    • (2004) Clin. Chem. , vol.50 , pp. 709-716
    • Kishi, T.1    Soosaipillai, A.2    Grass, L.3    Little, S.P.4    Johnstone, E.M.5    Diamandis, E.P.6
  • 16
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • I. Schechter, and A. Berger On the size of the active site in proteases. I. Papain Biochem. Biophys. Res. Commun. 27 1967 157 162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 19
    • 40849112916 scopus 로고    scopus 로고
    • Crystal structure of human epidermal kallikrein 7 synthesized directly in its native state in E. Coli: Insights into the atomic basis of its inhibition by LEKTI domain 6
    • I.S. Fernández, L. Ständker, H.-J. Mägert, W.-G. Forssmann, G.G. Gallego, and A. Romero Crystal structure of human epidermal kallikrein 7 synthesized directly in its native state in E. coli: insights into the atomic basis of its inhibition by LEKTI domain 6 J. Mol. Biol. 377 2008 1488 1497
    • (2008) J. Mol. Biol. , vol.377 , pp. 1488-1497
    • Fernández, I.S.1    Ständker, L.2    Mägert, H.-J.3    Forssmann, W.-G.4    Gallego, G.G.5    Romero, A.6
  • 21
    • 0028264809 scopus 로고
    • Portion-mixing peptide libraries of quenched fluorogenic substrates for complete subsite mapping of endoprotease specificity
    • M. Meldal, I. Svendsen, K. Breddam, and F.I. Auzanneau Portion-mixing peptide libraries of quenched fluorogenic substrates for complete subsite mapping of endoprotease specificity Proc. Natl. Acad. Sci. U. S. A. 91 1994 3314 3318
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 3314-3318
    • Meldal, M.1    Svendsen, I.2    Breddam, K.3    Auzanneau, F.I.4
  • 22
    • 34547218898 scopus 로고    scopus 로고
    • Controlled peptide solvation in portion-mixing libraries of FRET peptides: Improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S
    • F.M. Alves, I.Y. Hirata, I.E. Gouvea, M.F. Alves, M. Meldal, D. Brömme, L. Juliano, and M.A. Juliano Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S J. Comb. Chem. 9 2007 627 634
    • (2007) J. Comb. Chem. , vol.9 , pp. 627-634
    • Alves, F.M.1    Hirata, I.Y.2    Gouvea, I.E.3    Alves, M.F.4    Meldal, M.5    Brömme, D.6    Juliano, L.7    Juliano, M.A.8
  • 25
    • 0029058938 scopus 로고
    • Primary substrate specificity of recombinant human stratum corneum chymotryptic enzyme
    • A. Skytt, M. Stromqvis, and T. Egelrud Primary substrate specificity of recombinant human stratum corneum chymotryptic enzyme Biochem. Biophys. Res. Commun. 211 1995 586 589
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 586-589
    • Skytt, A.1    Stromqvis, M.2    Egelrud, T.3
  • 26
    • 0032698231 scopus 로고    scopus 로고
    • Somatostatin for upper gastrointestinal hemorrhage and pancreatic surgery. A review of its pharmacology and safety
    • C. Scarpignato, and I. Pelosini Somatostatin for upper gastrointestinal hemorrhage and pancreatic surgery. A review of its pharmacology and safety Digestion 60 Suppl. 3 1999 1 16
    • (1999) Digestion , vol.60 , pp. 1-16
    • Scarpignato, C.1    Pelosini, I.2
  • 27
    • 79959356243 scopus 로고    scopus 로고
    • Somatostatin receptors are strongly expressed in palmoplantar sweat glands and ducts: Studies of normal and palmoplantar pustulosis skin
    • E. Hagforsen, G. Michaëlsson, and M. Stridsberg Somatostatin receptors are strongly expressed in palmoplantar sweat glands and ducts: studies of normal and palmoplantar pustulosis skin Clin. Exp. Dermatol. 36 2011 521 527
    • (2011) Clin. Exp. Dermatol. , vol.36 , pp. 521-527
    • Hagforsen, E.1    Michaëlsson, G.2    Stridsberg, M.3
  • 29
    • 79952112171 scopus 로고    scopus 로고
    • Somatostatin regulates tight junction function and composition in human keratinocytes
    • M. Vockel, U. Breitenbach, H.J. Kreienkamp, and J.M. Brandner Somatostatin regulates tight junction function and composition in human keratinocytes Exp. Dermatol. 19 2010 888 894
    • (2010) Exp. Dermatol. , vol.19 , pp. 888-894
    • Vockel, M.1    Breitenbach, U.2    Kreienkamp, H.J.3    Brandner, J.M.4
  • 33
    • 0033561266 scopus 로고    scopus 로고
    • Specificity of human tissue kallikrein towards substrates containing Phe - Phe pair of amino acids
    • D.C. Pimenta, J. Chao, L. Chao, M.A. Juliano, and L. Juliano Specificity of human tissue kallikrein towards substrates containing Phe - Phe pair of amino acids Biochem. J. 339 1999 473 479
    • (1999) Biochem. J. , vol.339 , pp. 473-479
    • Pimenta, D.C.1    Chao, J.2    Chao, L.3    Juliano, M.A.4    Juliano, L.5
  • 35
    • 80052079878 scopus 로고    scopus 로고
    • Substrate specificity of kallikrein-related peptidase 13 activated by salts or glycosaminoglycans and a search for natural substrate candidates
    • D. Andrade, D.M. Assis, J.A. Santos, F.M. Alves, I.Y. Hirata, M.S. Araujo, S.I. Blaber, M. Blaber, M.A. Juliano, and L. Juliano Substrate specificity of kallikrein-related peptidase 13 activated by salts or glycosaminoglycans and a search for natural substrate candidates Biochimie 93 2011 1701 1709
    • (2011) Biochimie , vol.93 , pp. 1701-1709
    • Andrade, D.1    Assis, D.M.2    Santos, J.A.3    Alves, F.M.4    Hirata, I.Y.5    Araujo, M.S.6    Blaber, S.I.7    Blaber, M.8    Juliano, M.A.9    Juliano, L.10
  • 37
    • 84883230192 scopus 로고    scopus 로고
    • Regulation of kallikrein-related peptidases in the skin - From physiology to diseases to therapeutic options
    • J. Fisher, and U.F. Hoffert Regulation of kallikrein-related peptidases in the skin - from physiology to diseases to therapeutic options Thromb. Haemost. 110 2013 442 449
    • (2013) Thromb. Haemost. , vol.110 , pp. 442-449
    • Fisher, J.1    Hoffert, U.F.2
  • 38
    • 34548242780 scopus 로고    scopus 로고
    • Tissue kallikrein proteolytic cascade pathways in normal physiology and cancer
    • G. Pampalakis, and G. Sotiropoulou Tissue kallikrein proteolytic cascade pathways in normal physiology and cancer Biochim. Biophys. Acta 1776 2007 22 31
    • (2007) Biochim. Biophys. Acta , vol.1776 , pp. 22-31
    • Pampalakis, G.1    Sotiropoulou, G.2
  • 39
    • 49549119209 scopus 로고    scopus 로고
    • Effect of corneodesmosome degradation on the intercellular delamination of human stratum corneum
    • K. Levi, J. Baxter, H. Meldrum, M. Misra, E. Pashkovski, and R.H. Dauskardt Effect of corneodesmosome degradation on the intercellular delamination of human stratum corneum J. Invest. Dermatol. 128 2008 2345 2347
    • (2008) J. Invest. Dermatol. , vol.128 , pp. 2345-2347
    • Levi, K.1    Baxter, J.2    Meldrum, H.3    Misra, M.4    Pashkovski, E.5    Dauskardt, R.H.6
  • 40
    • 0032934075 scopus 로고    scopus 로고
    • Stratum corneum chymotryptic enzyme in psoriasis
    • E. Ekholm, and T. Egelrud Stratum corneum chymotryptic enzyme in psoriasis Arch. Dermatol. Res. 291 1999 195 200
    • (1999) Arch. Dermatol. Res. , vol.291 , pp. 195-200
    • Ekholm, E.1    Egelrud, T.2
  • 43
    • 34249800666 scopus 로고    scopus 로고
    • Skin hydration: A review on its molecular mechanisms
    • S.V. Sévrain, and F. Bonté Skin hydration: a review on its molecular mechanisms J. Cosmet. Dermatol. 6 2007 75 82
    • (2007) J. Cosmet. Dermatol. , vol.6 , pp. 75-82
    • Sévrain, S.V.1    Bonté, F.2
  • 44
    • 71949111527 scopus 로고    scopus 로고
    • Natural moisturizing factor components in the stratum corneum as biomarkers of filaggrin genotype: Evaluation of minimally invasive methods
    • S. Kezic, A. Kammeyer, F. Calkoen, J.W. Fluhr, and J.D. Bos Natural moisturizing factor components in the stratum corneum as biomarkers of filaggrin genotype: evaluation of minimally invasive methods Br. J. Dermatol. 161 2009 1098 1104
    • (2009) Br. J. Dermatol. , vol.161 , pp. 1098-1104
    • Kezic, S.1    Kammeyer, A.2    Calkoen, F.3    Fluhr, J.W.4    Bos, J.D.5
  • 45
    • 0035797899 scopus 로고    scopus 로고
    • Modulation of recombinant human prostate specific antigen: Activation by Hofmeister salts and inhibition by azapeptides. Appendix: Thermodynamic interpretation of the activation by concentrated salts
    • X. Huang, C.T. Knoell, G. Frey, M. Hazegh-Azam, A.H. Tashjian, L. Hedstrom, R.H. Abeles, and S.N. Timasheff Modulation of recombinant human prostate specific antigen: activation by Hofmeister salts and inhibition by azapeptides. Appendix: thermodynamic interpretation of the activation by concentrated salts Biochemistry 40 2001 11734 11741
    • (2001) Biochemistry , vol.40 , pp. 11734-11741
    • Huang, X.1    Knoell, C.T.2    Frey, G.3    Hazegh-Azam, M.4    Tashjian, A.H.5    Hedstrom, L.6    Abeles, R.H.7    Timasheff, S.N.8
  • 46
    • 0020455397 scopus 로고
    • The effect of cations on the activity of human urinary kallikrein
    • W. Lieberthal, N.B. Oza, D.B. Bernard, and N.G. Levinsky The effect of cations on the activity of human urinary kallikrein J. Biol. Chem. 257 1982 10827 10830
    • (1982) J. Biol. Chem. , vol.257 , pp. 10827-10830
    • Lieberthal, W.1    Oza, N.B.2    Bernard, D.B.3    Levinsky, N.G.4
  • 47
    • 0028788601 scopus 로고
    • Evaluation of the extent of the binding site in human tissue kallikrein by synthetic substrates with sequences of human kininogen fragments
    • E. Del Nery, J.R. Chagas, M.A. Juliano, E.S. Prado, and L. Juliano Evaluation of the extent of the binding site in human tissue kallikrein by synthetic substrates with sequences of human kininogen fragments Biochem. J. 312 1995 233 238
    • (1995) Biochem. J. , vol.312 , pp. 233-238
    • Del Nery, E.1    Chagas, J.R.2    Juliano, M.A.3    Prado, E.S.4    Juliano, L.5
  • 48
    • 4444246989 scopus 로고    scopus 로고
    • The effect of cations on the amidase activity of human tissue kallikrein: Linear competitive inhibition by sodium, potassium, calcium and magnesium. Linear mixed inhibition by aluminium
    • M.O. Sousa, M.M. Santoro, and A.F. Figueiredo The effect of cations on the amidase activity of human tissue kallikrein: linear competitive inhibition by sodium, potassium, calcium and magnesium. Linear mixed inhibition by aluminium J. Enzyme Inhib. Med. Chem. 19 2004 317 325
    • (2004) J. Enzyme Inhib. Med. Chem. , vol.19 , pp. 317-325
    • Sousa, M.O.1    Santoro, M.M.2    Figueiredo, A.F.3
  • 49
    • 13944276781 scopus 로고    scopus 로고
    • 1.70 A X-ray structure of human apo kallikrein 1: Structural changes upon peptide inhibitor/substrate binding
    • G. Laxmikanthan, S.I. Blaber, M.J. Bernett, I.A. Scarisbrick, M.A. Juliano, and M. Blaber 1.70 A X-ray structure of human apo kallikrein 1: structural changes upon peptide inhibitor/substrate binding Proteins 58 2005 802 814
    • (2005) Proteins , vol.58 , pp. 802-814
    • Laxmikanthan, G.1    Blaber, S.I.2    Bernett, M.J.3    Scarisbrick, I.A.4    Juliano, M.A.5    Blaber, M.6
  • 50
    • 0015546107 scopus 로고
    • Determination of the operational molarity of solutions of bovine alpha-chymotrypsin, trypsin, thrombin and factor Xa by spectrofluorimetric titration
    • G.W. Jameson, D.V. Roberts, R.W. Adams, W.S.A. Kyle, and D.T. Elmore Determination of the operational molarity of solutions of bovine alpha-chymotrypsin, trypsin, thrombin and factor Xa by spectrofluorimetric titration Biochem. J. 131 1973 107 117
    • (1973) Biochem. J. , vol.131 , pp. 107-117
    • Jameson, G.W.1    Roberts, D.V.2    Adams, R.W.3    Kyle, W.S.A.4    Elmore, D.T.5
  • 51
    • 34249758919 scopus 로고
    • Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs
    • I. Hirata, M.H.C. Cezari, C.R. Nakaie, P. Boshcov, A.S. Ito, M.A. Juliano, and L. Juliano Internally quenched fluorogenic protease substrates: solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs Lett. Pept. Sci. 1 1994 299 308
    • (1994) Lett. Pept. Sci. , vol.1 , pp. 299-308
    • Hirata, I.1    Cezari, M.H.C.2    Nakaie, C.R.3    Boshcov, P.4    Ito, A.S.5    Juliano, M.A.6    Juliano, L.7
  • 52
    • 44949182000 scopus 로고    scopus 로고
    • Measuring elastase, proteinase 3, and cathepsin G activities at the surface of human neutrophils with fluorescence energy transfer substrates
    • B. Korkmaz, S. Attucci, M.A. Juliano, T. Kalupov, M.L. Jourdan, L. Juliano, and F. Gauthier Measuring elastase, proteinase 3, and cathepsin G activities at the surface of human neutrophils with fluorescence energy transfer substrates Nat. Protoc. 3 2008 991 1000
    • (2008) Nat. Protoc. , vol.3 , pp. 991-1000
    • Korkmaz, B.1    Attucci, S.2    Juliano, M.A.3    Kalupov, T.4    Jourdan, M.L.5    Juliano, L.6    Gauthier, F.7
  • 53
    • 8844268400 scopus 로고    scopus 로고
    • High capacity poly (ethylene glycol) based amino polymers for peptide and organic synthesis
    • M. Roice, I. Johannsen, and M. Meldal High capacity poly (ethylene glycol) based amino polymers for peptide and organic synthesis QSAR Comb. Chem. 23 2004 662 673
    • (2004) QSAR Comb. Chem. , vol.23 , pp. 662-673
    • Roice, M.1    Johannsen, I.2    Meldal, M.3
  • 54
    • 0032061391 scopus 로고    scopus 로고
    • Structure of heparan sulfate: Identification of variable and constant oligosaccharide domains in eight heparan sulfates of different origins
    • C.P. Dietrich, I.L. Tersariol, L. Toma, C.T. Moraes, M.A. Porcionatto, F.W. Oliveira, and H.B. Nader Structure of heparan sulfate: identification of variable and constant oligosaccharide domains in eight heparan sulfates of different origins Cell. Mol. Biol. 44 1998 417 429
    • (1998) Cell. Mol. Biol. , vol.44 , pp. 417-429
    • Dietrich, C.P.1    Tersariol, I.L.2    Toma, L.3    Moraes, C.T.4    Porcionatto, M.A.5    Oliveira, F.W.6    Nader, H.B.7
  • 55
    • 0035336234 scopus 로고    scopus 로고
    • Human semaphorin 6B [(HSA)SEMA6B], a novel human class 6 semaphorin gene: Alternative splicing and all-trans-retinoic acid-dependent down regulation in glioblastoma cell lines
    • R.G. Correa, R.M. Sasahara, M.H. Bengtson, M.L.H. Katayama, A.C.M. Salim, M.M. Brentani, M.C. Sogayar, S.J. Souza, and A.J.G. Simpson Human semaphorin 6B [(HSA)SEMA6B], a novel human class 6 semaphorin gene: alternative splicing and all-trans-retinoic acid-dependent down regulation in glioblastoma cell lines Genomics 73 2001 343 348
    • (2001) Genomics , vol.73 , pp. 343-348
    • Correa, R.G.1    Sasahara, R.M.2    Bengtson, M.H.3    Katayama, M.L.H.4    Salim, A.C.M.5    Brentani, M.M.6    Sogayar, M.C.7    Souza, S.J.8    Simpson, A.J.G.9
  • 56
    • 0034946412 scopus 로고    scopus 로고
    • Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
    • B.E. Turk, L.L. Huang, E.T. Piro, and L.C. Cantley Determination of protease cleavage site motifs using mixture-based oriented peptide libraries Nat. Biotechnol. 19 2001 661 667
    • (2001) Nat. Biotechnol. , vol.19 , pp. 661-667
    • Turk, B.E.1    Huang, L.L.2    Piro, E.T.3    Cantley, L.C.4
  • 57
    • 84896321226 scopus 로고    scopus 로고
    • Itch and nerve fibers with special reference to atopic dermatitis: Therapeutic implications
    • M. Tominaga, and K. Takamori Itch and nerve fibers with special reference to atopic dermatitis: therapeutic implications J. Dermatol. 41 2014 205 212
    • (2014) J. Dermatol. , vol.41 , pp. 205-212
    • Tominaga, M.1    Takamori, K.2
  • 59
    • 84877790516 scopus 로고    scopus 로고
    • Aberrant epidermal expression of semaphorin 3A and nerve growth factor in prurigo nodularis
    • S. Takada, K. Kou, Y. Nagashima, Z. Ikezawa, and M. Aihara Aberrant epidermal expression of semaphorin 3A and nerve growth factor in prurigo nodularis J. Dermatol. 40 2013 404 406
    • (2013) J. Dermatol. , vol.40 , pp. 404-406
    • Takada, S.1    Kou, K.2    Nagashima, Y.3    Ikezawa, Z.4    Aihara, M.5
  • 61
    • 67649617069 scopus 로고    scopus 로고
    • Subsite cooperativity in protease specificity
    • N.M. Ng, R.N. Pike, and S.E. Boyd Subsite cooperativity in protease specificity Biol. Chem. 390 2009 401 407
    • (2009) Biol. Chem. , vol.390 , pp. 401-407
    • Ng, N.M.1    Pike, R.N.2    Boyd, S.E.3
  • 62
    • 0030693961 scopus 로고    scopus 로고
    • Hydrolysis of somatostatin by human tissue kallikrein after the amino acid pair Phe - Phe
    • D.C. Pimenta, M.A. Juliano, and L. Juliano Hydrolysis of somatostatin by human tissue kallikrein after the amino acid pair Phe - Phe Biochem. J. 327 1997 27 30
    • (1997) Biochem. J. , vol.327 , pp. 27-30
    • Pimenta, D.C.1    Juliano, M.A.2    Juliano, L.3
  • 63
    • 84890285273 scopus 로고    scopus 로고
    • Octreotide: A drug often used in the critical care setting but not well understood
    • M.M. Chan, M.M. Chan, J.A. Mengshol, N. Fish, and E.D. Chan Octreotide: a drug often used in the critical care setting but not well understood Chest 144 2013 1937 1945
    • (2013) Chest , vol.144 , pp. 1937-1945
    • Chan, M.M.1    Chan, M.M.2    Mengshol, J.A.3    Fish, N.4    Chan, E.D.5
  • 65
    • 84891415326 scopus 로고    scopus 로고
    • Netherton syndrome: Skin inflammation and allergy by loss of protease inhibition
    • A. Hovnanian Netherton syndrome: skin inflammation and allergy by loss of protease inhibition Cell Tissue Res. 351 2013 289 300
    • (2013) Cell Tissue Res. , vol.351 , pp. 289-300
    • Hovnanian, A.1
  • 68
    • 84896756828 scopus 로고    scopus 로고
    • Citrate - New functions for an old metabolite
    • V. Iacobazzi, and V. Infantino Citrate - new functions for an old metabolite Biol. Chem. 395 2014 387 399
    • (2014) Biol. Chem. , vol.395 , pp. 387-399
    • Iacobazzi, V.1    Infantino, V.2
  • 69
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • S.B. Zimmerman, and A.P. Minton Macromolecular crowding: biochemical, biophysical, and physiological consequences Annu. Rev. Biophys. Biomol. Struct. 22 1993 27 65
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 70
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • R.J. Ellis Macromolecular crowding: obvious but underappreciated Trends Biochem. Sci. 26 2001 597 604
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 71
    • 70349232202 scopus 로고    scopus 로고
    • Effect of macromolecular crowding on protein folding dynamics at the secondary structure level
    • S. Mukherjee, M.M. Waegele, P. Chowdhury, L. Guo, and F. Gai Effect of macromolecular crowding on protein folding dynamics at the secondary structure level J. Mol. Biol. 393 2009 227 236
    • (2009) J. Mol. Biol. , vol.393 , pp. 227-236
    • Mukherjee, S.1    Waegele, M.M.2    Chowdhury, P.3    Guo, L.4    Gai, F.5
  • 72
    • 33646536078 scopus 로고    scopus 로고
    • The influence of macromolecular crowding on HIV-1 protease internal dynamics
    • D.D.L. Minh, C. Chang, J. Trylska, V. Tozzini, and J.A. McCammon The influence of macromolecular crowding on HIV-1 protease internal dynamics J. Am. Chem. Soc. 128 2006 6006 6007
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6006-6007
    • Minh, D.D.L.1    Chang, C.2    Trylska, J.3    Tozzini, V.4    McCammon, J.A.5
  • 73
    • 33846613819 scopus 로고    scopus 로고
    • Activity of subtilisin Carlsberg in macromolecular crowding
    • A.K. Shaw, and S.K. Pal Activity of subtilisin Carlsberg in macromolecular crowding J. Photochem. Photobiol. B 86 2007 199 206
    • (2007) J. Photochem. Photobiol. B , vol.86 , pp. 199-206
    • Shaw, A.K.1    Pal, S.K.2
  • 74
    • 0015746510 scopus 로고
    • The concentration of pyroglutamic acid (2-pyrrolidone-5-carboxylic acid) in normal and psoriatic epidermis, determined on a microgram scale by gas chromatography
    • S. Marstein, E. Jellum, and L. Eldjarn The concentration of pyroglutamic acid (2-pyrrolidone-5-carboxylic acid) in normal and psoriatic epidermis, determined on a microgram scale by gas chromatography Clin. Chim. Acta 49 1973 389 395
    • (1973) Clin. Chim. Acta , vol.49 , pp. 389-395
    • Marstein, S.1    Jellum, E.2    Eldjarn, L.3
  • 75
    • 84864826447 scopus 로고    scopus 로고
    • Pyroglutamic acid: Throwing light on a lightly studied metabolite
    • A. Kumar, and A.K. Bachhawat Pyroglutamic acid: throwing light on a lightly studied metabolite Curr. Sci. 102 2012 288 297
    • (2012) Curr. Sci. , vol.102 , pp. 288-297
    • Kumar, A.1    Bachhawat, A.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.