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Volumn 87, Issue 3-4 SPEC. ISS., 2005, Pages 265-272

Assays of matrix metalloproteinases (MMPs) activities: A review

Author keywords

Fluorescent substrates; Immunocapture; Metalloprotease assay; Triple helical peptides

Indexed keywords

AMINO ACID; GELATINASE A; GELATINASE B; MATRILYSIN; MATRIX METALLOPROTEINASE; STROMELYSIN;

EID: 15244345731     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2005.01.007     Document Type: Short Survey
Times cited : (97)

References (77)
  • 2
    • 0027139093 scopus 로고
    • The rates of cleavage of insoluble and soluble collagens by tissue collagenases
    • S. Takahashi, and S. Han The rates of cleavage of insoluble and soluble collagens by tissue collagenases Connect. Tissue Res. 30 1993 99 116
    • (1993) Connect. Tissue Res. , vol.30 , pp. 99-116
    • Takahashi, S.1    Han, S.2
  • 3
    • 0030829521 scopus 로고    scopus 로고
    • Elastin degradation by matrix metalloproteinases. Cleavage site specificity and mechanism of elastolysis
    • R.P. Mecham, T.J. Broekelmann, C.J. Fliszar, S.D. Shapiro, H.G. Welgus, and R.M. Senior Elastin degradation by matrix metalloproteinases. Cleavage site specificity and mechanism of elastolysis J. Biol. Chem. 272 1997 18071 18076
    • (1997) J. Biol. Chem. , vol.272 , pp. 18071-18076
    • Mecham, R.P.1    Broekelmann, T.J.2    Fliszar, C.J.3    Shapiro, S.D.4    Welgus, H.G.5    Senior, R.M.6
  • 4
    • 4143145259 scopus 로고    scopus 로고
    • Assay of collagenase activity for native triple-helical collagen using capillary gel electrophoresis with laser-induced fluorescence detection
    • M. Sano, I. Nishino, K. Ueno, and H. Kamimori Assay of collagenase activity for native triple-helical collagen using capillary gel electrophoresis with laser-induced fluorescence detection J. Chromatogr. B 809 2004 251 256
    • (2004) J. Chromatogr. B , vol.809 , pp. 251-256
    • Sano, M.1    Nishino, I.2    Ueno, K.3    Kamimori, H.4
  • 5
    • 0025077334 scopus 로고
    • Purification and properties of extracellular matrix-degrading metalloproteinase overproduced by Rous sarcoma virus-transformed rat liver cell line, and its identification as transin
    • F. Umenishi, H. Yasumitsu, Y. Ashida, J. Yamauti, M. Umeda, and K. Miyazaki Purification and properties of extracellular matrix-degrading metalloproteinase overproduced by Rous sarcoma virus-transformed rat liver cell line, and its identification as transin J. Biochem. (Tokyo) 108 1990 537 543
    • (1990) J. Biochem. (Tokyo) , vol.108 , pp. 537-543
    • Umenishi, F.1    Yasumitsu, H.2    Ashida, Y.3    Yamauti, J.4    Umeda, M.5    Miyazaki, K.6
  • 6
    • 0025647386 scopus 로고
    • Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line
    • K. Miyazaki, Y. Hattori, F. Umenishi, H. Yasumitsu, and M. Umeda Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line Cancer Res. 50 1990 7758 7764
    • (1990) Cancer Res. , vol.50 , pp. 7758-7764
    • Miyazaki, K.1    Hattori, Y.2    Umenishi, F.3    Yasumitsu, H.4    Umeda, M.5
  • 7
    • 0026667311 scopus 로고
    • Induction of 103-kDa gelatinase/type IV collagenase by acidic culture conditions in mouse metastatic melanoma cell lines
    • Y. Kato, Y. Nakayama, M. Umeda, and K. Miyazaki Induction of 103-kDa gelatinase/type IV collagenase by acidic culture conditions in mouse metastatic melanoma cell lines J. Biol. Chem. 267 1992 11424 11430
    • (1992) J. Biol. Chem. , vol.267 , pp. 11424-11430
    • Kato, Y.1    Nakayama, Y.2    Umeda, M.3    Miyazaki, K.4
  • 8
    • 0028345645 scopus 로고
    • Quantitative zymography: Detection of picogram quantities of gelatinases
    • D.E. Kleiner, and W.G. Stetler-Stevenson Quantitative zymography: detection of picogram quantities of gelatinases Anal. Biochem. 218 1994 325 329
    • (1994) Anal. Biochem. , vol.218 , pp. 325-329
    • Kleiner, D.E.1    Stetler-Stevenson, W.G.2
  • 9
    • 0031570725 scopus 로고    scopus 로고
    • Zymography: A single-step staining method for quantitation of proteolytic activity on substrate gels
    • T.M. Leber, and F.R. Balkwill Zymography: a single-step staining method for quantitation of proteolytic activity on substrate gels Anal. Biochem. 249 1997 24 28
    • (1997) Anal. Biochem. , vol.249 , pp. 24-28
    • Leber, T.M.1    Balkwill, F.R.2
  • 10
    • 0032518450 scopus 로고    scopus 로고
    • Collagen zymography as a sensitive and specific technique for the determination of subpicogram levels of interstitial collagenase
    • B. Gogly, N. Groult, W. Hornebeck, G. Godeau, and B. Pellat Collagen zymography as a sensitive and specific technique for the determination of subpicogram levels of interstitial collagenase Anal. Biochem. 255 1998 211 216
    • (1998) Anal. Biochem. , vol.255 , pp. 211-216
    • Gogly, B.1    Groult, N.2    Hornebeck, W.3    Godeau, G.4    Pellat, B.5
  • 11
    • 0035369013 scopus 로고    scopus 로고
    • Heparin-enhanced zymographic detection of matrilysin and collagenases
    • W.H. Yu, and J.F. Woessner Jr. Heparin-enhanced zymographic detection of matrilysin and collagenases Anal. Biochem. 293 2001 38 42
    • (2001) Anal. Biochem. , vol.293 , pp. 38-42
    • Yu, W.H.1    Woessner Jr., J.F.2
  • 13
    • 0031024924 scopus 로고    scopus 로고
    • Quantitative reverse zymography: Analysis of picogram amounts of metalloproteinase inhibitors using gelatinase a and B reverse zymograms
    • G.W. Oliver, J.D. Leferson, W.G. Stetler-Stevenson, and D.E. Kleiner Quantitative reverse zymography: analysis of picogram amounts of metalloproteinase inhibitors using gelatinase A and B reverse zymograms Anal. Biochem. 244 1997 161 166
    • (1997) Anal. Biochem. , vol.244 , pp. 161-166
    • Oliver, G.W.1    Leferson, J.D.2    Stetler-Stevenson, W.G.3    Kleiner, D.E.4
  • 14
    • 0036467706 scopus 로고    scopus 로고
    • Real-time zymography and reverse zymography: A method for detecting activities of matrix metalloproteinases and their inhibitors using FITC-labeled collagen and casein as substrates
    • S. Hattori, H. Fujisaki, T. Kiriyama, T. Yokoyama, and S. Irie Real-time zymography and reverse zymography: a method for detecting activities of matrix metalloproteinases and their inhibitors using FITC-labeled collagen and casein as substrates Anal. Biochem. 301 2002 27 34
    • (2002) Anal. Biochem. , vol.301 , pp. 27-34
    • Hattori, S.1    Fujisaki, H.2    Kiriyama, T.3    Yokoyama, T.4    Irie, S.5
  • 15
    • 0043269218 scopus 로고    scopus 로고
    • Measurement of matrix metalloproteinase activities in the medium of cultured synoviocytes using zymography
    • L. Troeberg, and H. Nagase Measurement of matrix metalloproteinase activities in the medium of cultured synoviocytes using zymography Methods Mol. Biol. 225 2003 77 87
    • (2003) Methods Mol. Biol. , vol.225 , pp. 77-87
    • Troeberg, L.1    Nagase, H.2
  • 16
    • 0027377609 scopus 로고
    • An assay for matrix metalloproteinases and other proteases acting on proteoglycans, casein, or gelatin
    • D.H. Manicourt, and V. Lefebvre An assay for matrix metalloproteinases and other proteases acting on proteoglycans, casein, or gelatin Anal. Biochem. 215 1993 171 179
    • (1993) Anal. Biochem. , vol.215 , pp. 171-179
    • Manicourt, D.H.1    Lefebvre, V.2
  • 17
    • 0042768002 scopus 로고    scopus 로고
    • Assays of matrix metalloproteinases (MMPs) and MMP inhibitors: Bioassays and immunoassays applicable to cell culture medium, serum and synovial fluid
    • J.B. Catterall, and T.E. Cawston Assays of matrix metalloproteinases (MMPs) and MMP inhibitors: bioassays and immunoassays applicable to cell culture medium, serum and synovial fluid Methods Mol. Biol. 225 2003 353 364
    • (2003) Methods Mol. Biol. , vol.225 , pp. 353-364
    • Catterall, J.B.1    Cawston, T.E.2
  • 19
    • 0031543459 scopus 로고    scopus 로고
    • Continuous assay of proteases using a microtiter plate fluorescence reader
    • D.A. Menges, D.L. Ternullo, A.L. Tan-Wilson, and S. Gal Continuous assay of proteases using a microtiter plate fluorescence reader Anal. Biochem. 254 1997 144 147
    • (1997) Anal. Biochem. , vol.254 , pp. 144-147
    • Menges, D.A.1    Ternullo, D.L.2    Tan-Wilson, A.L.3    Gal, S.4
  • 20
    • 0029855186 scopus 로고    scopus 로고
    • Flow cytometric analysis of gelatinase B (MMP-9) activity using immobilized fluorescent substrate on microspheres
    • Y. St-Pierre, M. Desrosiers, P. Tremblay, P.-O. Esteve, and G. Opdenakker Flow cytometric analysis of gelatinase B (MMP-9) activity using immobilized fluorescent substrate on microspheres Cytometry 25 1996 374 380
    • (1996) Cytometry , vol.25 , pp. 374-380
    • St-Pierre, Y.1    Desrosiers, M.2    Tremblay, P.3    Esteve, P.-O.4    Opdenakker, G.5
  • 21
    • 1042275537 scopus 로고    scopus 로고
    • Inhibitors of gelatinase B/matrix metalloproteinase-9 activity. Comparison of a peptidomimetic and polyhistidine with single-chain derivatives of a neutralizing monoclonal antibody
    • J. Hu, P.E. Van:den:Steen, M. Houde, T.T. Ilenchuk, and G. Opdenakker Inhibitors of gelatinase B/matrix metalloproteinase-9 activity. Comparison of a peptidomimetic and polyhistidine with single-chain derivatives of a neutralizing monoclonal antibody Biochem. Pharmacol. 67 2004 1001 1009
    • (2004) Biochem. Pharmacol. , vol.67 , pp. 1001-1009
    • Hu, J.1    Van2    Den3    Steen, P.E.4    Houde, M.5    Ilenchuk, T.T.6    Opdenakker, G.7
  • 23
    • 3242815965 scopus 로고    scopus 로고
    • In vitro inhibition of the activation of pro-matrix metalloproteinase 1 (Pro-MMP-1) and pro-matrix metalloproteinase 9 (pro-MMP-9) by rice and soybean Bowman-Birk inhibitors
    • H.A. Bawadi, T.M. Antunes, F. Shih, and J.N. Losso In vitro inhibition of the activation of pro-matrix metalloproteinase 1 (Pro-MMP-1) and pro-matrix metalloproteinase 9 (pro-MMP-9) by rice and soybean Bowman-Birk inhibitors J. Agric. Food Chem. 52 2004 4730 4736
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4730-4736
    • Bawadi, H.A.1    Antunes, T.M.2    Shih, F.3    Losso, J.N.4
  • 26
    • 1342328148 scopus 로고    scopus 로고
    • Antioxidant activity and inhibition of matrix metalloproteinases by metabolites of maritime pine bark extract (pycnogenol)
    • T. Grimm, A. Schäfer, and P. Högger Antioxidant activity and inhibition of matrix metalloproteinases by metabolites of maritime pine bark extract (pycnogenol) Free Radic. Biol. Med. 36 2004 811 822
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 811-822
    • Grimm, T.1    Schäfer, A.2    Högger, P.3
  • 27
    • 0030921002 scopus 로고    scopus 로고
    • Modified proenzymes as artificial substrates for proteolytic enzymes: Colorimetric assay of bacterial collagenase and matrix metalloproteinase activity using modified pro-urokinase
    • J.H. Verheijen, N.M.E. Nieuwenbroek, B. Beekman, R. Hanemaaijer, H.W. Verspaget, and H.K. Ronday Modified proenzymes as artificial substrates for proteolytic enzymes: colorimetric assay of bacterial collagenase and matrix metalloproteinase activity using modified pro-urokinase Biochem. J. 323 1997 603 609
    • (1997) Biochem. J. , vol.323 , pp. 603-609
    • Verheijen, J.H.1    Nieuwenbroek, N.M.E.2    Beekman, B.3    Hanemaaijer, R.4    Verspaget, H.W.5    Ronday, H.K.6
  • 28
    • 0032428256 scopus 로고    scopus 로고
    • A novel and simple immunocapture assay for determination of gelatinase B (MMP-9) activities in biological fluids: Saliva from patients with Sjögren's syndrome contain increased latent and active gelatinase-B levels
    • R. Hanemaaijer, H. Visser, Y.T. Konttinen, P. Koolwijk, and J.H. Verheijen A novel and simple immunocapture assay for determination of gelatinase B (MMP-9) activities in biological fluids: saliva from patients with Sjögren's syndrome contain increased latent and active gelatinase-B levels Matrix Biol. 17 1998 657 665
    • (1998) Matrix Biol. , vol.17 , pp. 657-665
    • Hanemaaijer, R.1    Visser, H.2    Konttinen, Y.T.3    Koolwijk, P.4    Verheijen, J.H.5
  • 31
    • 0036453583 scopus 로고    scopus 로고
    • Clinical pharmacokinetics, pharmacodynamics and metabolism of the novel matrix metalloproteinase inhibitor ABT-518
    • M. Crul, L.V. Beerepoot, E. Stokvis, J.S.P. Vermaat, H. Rosing, and J.H. Beijnen Clinical pharmacokinetics, pharmacodynamics and metabolism of the novel matrix metalloproteinase inhibitor ABT-518 Cancer Chemother. Pharmacol. 50 2002 473 478
    • (2002) Cancer Chemother. Pharmacol. , vol.50 , pp. 473-478
    • Crul, M.1    Beerepoot, L.V.2    Stokvis, E.3    Vermaat, J.S.P.4    Rosing, H.5    Beijnen, J.H.6
  • 32
    • 1942487730 scopus 로고    scopus 로고
    • Matrix-metalloproteinase activity in first trimester placental bed biopsies in further complicated and uncomplicated pregnancies
    • M.A. Huisman, A. Timmer, M. Zeinstra, E.K. Serlier, R. Hanemaaijer, and H. Van:Goor Matrix-metalloproteinase activity in first trimester placental bed biopsies in further complicated and uncomplicated pregnancies Placenta 25 2004 253 258
    • (2004) Placenta , vol.25 , pp. 253-258
    • Huisman, M.A.1    Timmer, A.2    Zeinstra, M.3    Serlier, E.K.4    Hanemaaijer, R.5    Van6    Goor, H.7
  • 34
    • 0020032754 scopus 로고
    • Characterization of vertebrate collagenase activity by high-performance liquid chromatography using a synthetic substrate
    • R.D. Gray, and H.H. Saneii Characterization of vertebrate collagenase activity by high-performance liquid chromatography using a synthetic substrate Anal. Biochem. 120 1982 339 346
    • (1982) Anal. Biochem. , vol.120 , pp. 339-346
    • Gray, R.D.1    Saneii, H.H.2
  • 35
    • 0021670540 scopus 로고
    • Human polymorphonuclear leukocyte collagenase and gelatinase. Comparison of certain enzymatic properties
    • H.R. Williams, and T.Y. Lin Human polymorphonuclear leukocyte collagenase and gelatinase. Comparison of certain enzymatic properties Int. J. Biochem. 16 1984 1321 1329
    • (1984) Int. J. Biochem. , vol.16 , pp. 1321-1329
    • Williams, H.R.1    Lin, T.Y.2
  • 36
    • 0022387489 scopus 로고
    • Synthetic substrates of vertebrate collagenase
    • H. Weingarten, R. Martin, and J. Feder Synthetic substrates of vertebrate collagenase Biochemistry 24 1985 6730 6734
    • (1985) Biochemistry , vol.24 , pp. 6730-6734
    • Weingarten, H.1    Martin, R.2    Feder, J.3
  • 37
    • 0022261246 scopus 로고
    • Spectrophotometric assay for vertebrate collagenase
    • H. Weingarten, and J. Feder Spectrophotometric assay for vertebrate collagenase Anal. Biochem. 147 1985 437 440
    • (1985) Anal. Biochem. , vol.147 , pp. 437-440
    • Weingarten, H.1    Feder, J.2
  • 38
    • 0029065458 scopus 로고
    • Fluorimetric assays of proteolytic enzymes
    • C.G. Knight Fluorimetric assays of proteolytic enzymes Methods Enzymol. 248 1995 18 34
    • (1995) Methods Enzymol. , vol.248 , pp. 18-34
    • Knight, C.G.1
  • 39
    • 0024564708 scopus 로고
    • Comparison of vertebrate collagenase and gelatinase using a new fluorogenic substrate peptide
    • M.S. Stack, and R.D. Gray Comparison of vertebrate collagenase and gelatinase using a new fluorogenic substrate peptide J. Biol. Chem. 264 1989 4277 4281
    • (1989) J. Biol. Chem. , vol.264 , pp. 4277-4281
    • Stack, M.S.1    Gray, R.D.2
  • 40
    • 0025915082 scopus 로고
    • Continuously recording fluorescent assays optimized for five human matrix metalloproteinases
    • S. Netzel-Arnett, S.K. Mallya, H. Nagase, H. Birkedal-Hansen, and H.E. Van:Wart Continuously recording fluorescent assays optimized for five human matrix metalloproteinases Anal. Biochem. 195 1991 86 92
    • (1991) Anal. Biochem. , vol.195 , pp. 86-92
    • Netzel-Arnett, S.1    Mallya, S.K.2    Nagase, H.3    Birkedal-Hansen, H.4    Van5    Wart, H.E.6
  • 41
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitive continuous assays of matrix metalloproteinases
    • C.G. Knight, F. Willenbrock, and G. Murphy A novel coumarin-labelled peptide for sensitive continuous assays of matrix metalloproteinases FEBS Lett. 296 1992 263 266
    • (1992) FEBS Lett. , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3
  • 42
    • 0027201881 scopus 로고
    • A high throughput fluorogenic substrate for interstitial collagenase (MMP-1) and gelatinase (MMP-9)
    • D.M. Bickett, M.D. Green, J. Berman, M. Dezube, A.S. Howe, and P.J. Brown A high throughput fluorogenic substrate for interstitial collagenase (MMP-1) and gelatinase (MMP-9) Anal. Biochem. 212 1993 58 64
    • (1993) Anal. Biochem. , vol.212 , pp. 58-64
    • Bickett, D.M.1    Green, M.D.2    Berman, J.3    Dezube, M.4    Howe, A.S.5    Brown, P.J.6
  • 43
    • 2142828483 scopus 로고    scopus 로고
    • 2, a fluorogenic substrate with increased specificity constants for collagenases and tumor necrosis factor converting enzyme
    • 2, a fluorogenic substrate with increased specificity constants for collagenases and tumor necrosis factor converting enzyme Anal. Biochem. 328 2004 166 173
    • (2004) Anal. Biochem. , vol.328 , pp. 166-173
    • Neumann, U.1    Kubota, H.2    Frei, K.3    Ganu, V.4    Leppert, D.5
  • 44
    • 0025099455 scopus 로고
    • Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer
    • E.D. Matayoshi, G.T. Wang, G.A. Krafft, and J. Erickson Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer Science 247 1990 954 958
    • (1990) Science , vol.247 , pp. 954-958
    • Matayoshi, E.D.1    Wang, G.T.2    Krafft, G.A.3    Erickson, J.4
  • 46
    • 0030597963 scopus 로고    scopus 로고
    • Convenient fluorometric assay for matrix metalloproteinase activity and its application in biological media
    • B. Beekman, J.W. Drijfhout, W. Bloemhoff, H.K. Ronday, P.P. Tak, and J.M. Te:Koppele Convenient fluorometric assay for matrix metalloproteinase activity and its application in biological media FEBS Lett. 390 1996 221 225
    • (1996) FEBS Lett. , vol.390 , pp. 221-225
    • Beekman, B.1    Drijfhout, J.W.2    Bloemhoff, W.3    Ronday, H.K.4    Tak, P.P.5    Te6    Koppele, J.M.7
  • 47
    • 0030721640 scopus 로고    scopus 로고
    • Highly increased levels of active stromelysin in rheumatoid synovial fluid determined by a selective fluorogenic assay
    • B. Beekman, B. van El, J.W. Drijfhout, H.K. Ronday, and J.M. Te:Koppele Highly increased levels of active stromelysin in rheumatoid synovial fluid determined by a selective fluorogenic assay FEBS Lett. 418 1997 305 309
    • (1997) FEBS Lett. , vol.418 , pp. 305-309
    • Beekman, B.1    El V., B.2    Drijfhout, J.W.3    Ronday, H.K.4    Te5    Koppele, J.M.6
  • 48
    • 0027689305 scopus 로고
    • Site-directed double fluorescent tagging of human renin and collagenase (MMP-1) substrate peptides using the periodate oxidation of N-terminal serine. An apparently general strategy for provision of energy-transfer substrates for proteases
    • K.F. Geoghegan, M.J. Emery, W.H. Martin, A.S. McColl, and G.O. Daumy Site-directed double fluorescent tagging of human renin and collagenase (MMP-1) substrate peptides using the periodate oxidation of N-terminal serine. An apparently general strategy for provision of energy-transfer substrates for proteases Bioconjug. Chem. 4 1993 537 544
    • (1993) Bioconjug. Chem. , vol.4 , pp. 537-544
    • Geoghegan, K.F.1    Emery, M.J.2    Martin, W.H.3    McColl, A.S.4    Daumy, G.O.5
  • 49
    • 0030135847 scopus 로고    scopus 로고
    • Improved method for converting an unmodified peptide to an energy-transfer substrate for a proteinase
    • K.F. Geoghegan Improved method for converting an unmodified peptide to an energy-transfer substrate for a proteinase Bioconjug. Chem. 7 1996 385 391
    • (1996) Bioconjug. Chem. , vol.7 , pp. 385-391
    • Geoghegan, K.F.1
  • 50
    • 3142730512 scopus 로고    scopus 로고
    • Development of an assay suitable for high-throughput screening to measure matrix metalloprotease activity
    • J. Peppard, Q. Pham, A. Clark, D. Farley, Y. Sakane, and R. Graves Development of an assay suitable for high-throughput screening to measure matrix metalloprotease activity Assay Drug Dev. Technol. 1 2003 425 433
    • (2003) Assay Drug Dev. Technol. , vol.1 , pp. 425-433
    • Peppard, J.1    Pham, Q.2    Clark, A.3    Farley, D.4    Sakane, Y.5    Graves, R.6
  • 51
    • 0041888479 scopus 로고    scopus 로고
    • Evaluation of an imaging platform during the development of a FRET protease assay
    • J. George, M.L. Teear, C.G. Norey, and D.D. Burns Evaluation of an imaging platform during the development of a FRET protease assay J. Biomol. Screen. 8 2003 72 80
    • (2003) J. Biomol. Screen. , vol.8 , pp. 72-80
    • George, J.1    Teear, M.L.2    Norey, C.G.3    Burns, D.D.4
  • 52
    • 0035219994 scopus 로고    scopus 로고
    • Using fluorogenic peptide substrates to assay matrix metalloproteinases
    • G.B. Fields Using fluorogenic peptide substrates to assay matrix metalloproteinases Methods Mol. Biol. 151 2001 495 518
    • (2001) Methods Mol. Biol. , vol.151 , pp. 495-518
    • Fields, G.B.1
  • 54
    • 0032535442 scopus 로고    scopus 로고
    • Design and synthesis of fluorogenic trypsin peptide substrates based on resonance energy transfer
    • S. Grahn, D. Ullmann, and H.-D. Jakubke Design and synthesis of fluorogenic trypsin peptide substrates based on resonance energy transfer Anal. Biochem. 265 1998 225 231
    • (1998) Anal. Biochem. , vol.265 , pp. 225-231
    • Grahn, S.1    Ullmann, D.2    Jakubke, H.-D.3
  • 55
    • 0030958569 scopus 로고    scopus 로고
    • Flow injection analysis for measurement of activity of matrix metalloproteinase-7 (MMP-7)
    • M. Itoh, M. Osaki, T. Chiba, K. Masuda, T. Akizawa, and M. Yoshioka Flow injection analysis for measurement of activity of matrix metalloproteinase-7 (MMP-7) J. Pharm. Biomed. Anal. 15 1997 1417 1426
    • (1997) J. Pharm. Biomed. Anal. , vol.15 , pp. 1417-1426
    • Itoh, M.1    Osaki, M.2    Chiba, T.3    Masuda, K.4    Akizawa, T.5    Yoshioka, M.6
  • 56
    • 0027130489 scopus 로고
    • Solid-phase synthesis and stability of triple-helical peptides incorporating native collagen sequences
    • C.G. Fields, C.M. Lovdahl, A.J. Miles, V.L. Mathias-Hagen, and G.B. Fields Solid-phase synthesis and stability of triple-helical peptides incorporating native collagen sequences Biopolymers 33 1993 1695 1707
    • (1993) Biopolymers , vol.33 , pp. 1695-1707
    • Fields, C.G.1    Lovdahl, C.M.2    Miles, A.J.3    Mathias-Hagen, V.L.4    Fields, G.B.5
  • 57
    • 0027230410 scopus 로고
    • Melanoma cell adhesion and spreading activities of a synthetic 124-residue triple-helical 'mini-collagen'
    • C.G. Fields, D.J. Mickelson, S.L. Drake, J.B. McCarthy, and G.B. Fields Melanoma cell adhesion and spreading activities of a synthetic 124-residue triple-helical 'mini-collagen' J. Biol. Chem. 268 1993 14153 14160
    • (1993) J. Biol. Chem. , vol.268 , pp. 14153-14160
    • Fields, C.G.1    Mickelson, D.J.2    Drake, S.L.3    McCarthy, J.B.4    Fields, G.B.5
  • 58
    • 0030482156 scopus 로고    scopus 로고
    • Self-assembling amphiphiles for construction of protein molecular architecture
    • Y.-C. Yu, P. Berndt, M. Tirrell, and G.B. Fields Self-assembling amphiphiles for construction of protein molecular architecture J. Am. Chem. Soc. 118 1996 12515 12520
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12515-12520
    • Yu, Y.-C.1    Berndt, P.2    Tirrell, M.3    Fields, G.B.4
  • 59
    • 0032494447 scopus 로고    scopus 로고
    • Minimal lipidation stabilizes protein-like molecular architecture
    • Y.-C. Yu, M. Tirrell, and G.B. Fields Minimal lipidation stabilizes protein-like molecular architecture J. Am. Chem. Soc. 120 1998 9979 9987
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9979-9987
    • Yu, Y.-C.1    Tirrell, M.2    Fields, G.B.3
  • 60
    • 0033514426 scopus 로고    scopus 로고
    • Structure and dynamics of peptide amphiphiles incorporating triple-helical protein like molecular architecture
    • Y.-C. Yu, V. Roontga, V.A. Daragan, K.H. Mayo, M. Tirrell, and G.B. Fields Structure and dynamics of peptide amphiphiles incorporating triple-helical protein like molecular architecture Biochemistry 38 1999 1659 1668
    • (1999) Biochemistry , vol.38 , pp. 1659-1668
    • Yu, Y.-C.1    Roontga, V.2    Daragan, V.A.3    Mayo, K.H.4    Tirrell, M.5    Fields, G.B.6
  • 61
    • 0034683146 scopus 로고    scopus 로고
    • Use of Edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases
    • J.L. Lauer-Fields, H. Nagase, and G.B. Fields Use of Edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases J. Chromatogr. A 890 2000 117 125
    • (2000) J. Chromatogr. a , vol.890 , pp. 117-125
    • Lauer-Fields, J.L.1    Nagase, H.2    Fields, G.B.3
  • 62
    • 0034607873 scopus 로고    scopus 로고
    • Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases
    • J.L. Lauer-Fields, K.A. Tuzinski, K. Shimokawa, H. Nagase, and G.B. Fields Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases J. Biol. Chem. 275 2000 13282 13290
    • (2000) J. Biol. Chem. , vol.275 , pp. 13282-13290
    • Lauer-Fields, J.L.1    Tuzinski, K.A.2    Shimokawa, K.3    Nagase, H.4    Fields, G.B.5
  • 63
    • 0035873874 scopus 로고    scopus 로고
    • Kinetic analysis of matrix metalloproteinase activity using fluorogenic triple-helical substrates
    • J.L. Lauer-Fields, T. Broder, T. Sritharan, L. Chung, H. Nagase, and G.B. Fields Kinetic analysis of matrix metalloproteinase activity using fluorogenic triple-helical substrates Biochemistry 40 2001 5795 5803
    • (2001) Biochemistry , vol.40 , pp. 5795-5803
    • Lauer-Fields, J.L.1    Broder, T.2    Sritharan, T.3    Chung, L.4    Nagase, H.5    Fields, G.B.6
  • 64
    • 0030602223 scopus 로고    scopus 로고
    • Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot. Models for collagen catabolism by matrix-metalloproteases
    • J. Ottl, R. Battistuta, M. Pieper, H. Tschesche, W. Bode, and K. Kühn Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot. Models for collagen catabolism by matrix-metalloproteases FEBS Lett. 398 1996 31 36
    • (1996) FEBS Lett. , vol.398 , pp. 31-36
    • Ottl, J.1    Battistuta, R.2    Pieper, M.3    Tschesche, H.4    Bode, W.5    Kühn, K.6
  • 65
    • 0033518557 scopus 로고    scopus 로고
    • Disulfide-bridged heterotrimeric collagen peptides containing the collagenase cleavage site of collagen type I. Synthesis and conformational properties
    • J. Ottl, and L. Moroder Disulfide-bridged heterotrimeric collagen peptides containing the collagenase cleavage site of collagen type I. Synthesis and conformational properties J. Am. Chem. Soc. 121 1999 653 661
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 653-661
    • Ottl, J.1    Moroder, L.2
  • 66
    • 0040182518 scopus 로고    scopus 로고
    • Heterotrimeric collagen peptides as fluorogenic collagenase substrates: Synthesis, conformational properties, and enzymatic digestion
    • J.C.D. Müller, J. Ottl, and L. Moroder Heterotrimeric collagen peptides as fluorogenic collagenase substrates: synthesis, conformational properties, and enzymatic digestion Biochemistry 39 2000 5111 5116
    • (2000) Biochemistry , vol.39 , pp. 5111-5116
    • Müller, J.C.D.1    Ottl, J.2    Moroder, L.3
  • 67
    • 0036391436 scopus 로고    scopus 로고
    • Matrix metalloproteinases and collagen catabolism
    • J.L. Lauer-Fields, D. Juska, and G.B. Fields Matrix metalloproteinases and collagen catabolism Biopolymers 66 2002 19 32
    • (2002) Biopolymers , vol.66 , pp. 19-32
    • Lauer-Fields, J.L.1    Juska, D.2    Fields, G.B.3
  • 68
    • 0036660865 scopus 로고    scopus 로고
    • Triple-helical peptide analysis of collagenolytic protease activity
    • J.L. Lauer-Fields, and G.B. Fields Triple-helical peptide analysis of collagenolytic protease activity Biol. Chem. 383 2002 1095 1105
    • (2002) Biol. Chem. , vol.383 , pp. 1095-1105
    • Lauer-Fields, J.L.1    Fields, G.B.2
  • 69
    • 0037705345 scopus 로고    scopus 로고
    • Selective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9
    • J.L. Lauer-Fields, T. Sritharan, M.S. Stack, H. Nagase, and G.B. Fields Selective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9 J. Biol. Chem. 278 2003 18140 18145
    • (2003) J. Biol. Chem. , vol.278 , pp. 18140-18145
    • Lauer-Fields, J.L.1    Sritharan, T.2    Stack, M.S.3    Nagase, H.4    Fields, G.B.5
  • 70
    • 0042696223 scopus 로고    scopus 로고
    • Analysis of matrix metalloproteinase triple-helical peptidase activity with substrates incorporating fluorogenic l- or d- amino acids
    • J.L. Lauer-Fields, P. Kele, G. Sui, H. Nagase, R.M. Leblanc, and G.B. Fields Analysis of matrix metalloproteinase triple-helical peptidase activity with substrates incorporating fluorogenic l- or d- amino acids Anal. Biochem. 321 2003 105 115
    • (2003) Anal. Biochem. , vol.321 , pp. 105-115
    • Lauer-Fields, J.L.1    Kele, P.2    Sui, G.3    Nagase, H.4    Leblanc, R.M.5    Fields, G.B.6
  • 71
    • 4444290999 scopus 로고    scopus 로고
    • Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability
    • D. Minond, J.L. Lauer-Fields, H. Nagase, and G.B. Fields Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability Biochemistry 43 2004 11474 11481
    • (2004) Biochemistry , vol.43 , pp. 11474-11481
    • Minond, D.1    Lauer-Fields, J.L.2    Nagase, H.3    Fields, G.B.4
  • 73
    • 0034705501 scopus 로고    scopus 로고
    • Cleavage of bovine collagen I by neutrophil collagenase MMP-8. Effect of pH on the catalytic properties as compared to synthetic substrates
    • S. Marini, G.F. Fasciglione, G. de:Sanctis, S. D'Alessio, V. Politi, and M. Coletta Cleavage of bovine collagen I by neutrophil collagenase MMP-8. Effect of pH on the catalytic properties as compared to synthetic substrates J. Biol. Chem. 275 2000 18657 18663
    • (2000) J. Biol. Chem. , vol.275 , pp. 18657-18663
    • Marini, S.1    Fasciglione, G.F.2    De3    Sanctis, G.4    D'Alessio, S.5    Politi, V.6    Coletta, M.7
  • 74
    • 0032837017 scopus 로고    scopus 로고
    • Fluorogenic MMP activity assay for plasma including MMPs complexed to alpha 2-macroglobulin
    • B. Beekman, J.W. Drijfhout, H.K. Ronday, and J.M. Te:Koppele Fluorogenic MMP activity assay for plasma including MMPs complexed to alpha 2-macroglobulin Ann. N. Y. Acad. Sci. 878 1999 150 158
    • (1999) Ann. N. Y. Acad. Sci. , vol.878 , pp. 150-158
    • Beekman, B.1    Drijfhout, J.W.2    Ronday, H.K.3    Te4    Koppele, J.M.5
  • 76
    • 1542744002 scopus 로고    scopus 로고
    • Use of a multiple-enzyme/multiple-reagent assay system to quantify activity levels in samples containing mixtures of matrix metalloproteinases
    • F.H. Rasmussen, N. Yeung, L. Kiefer, G. Murphy, C. Lopez-Otin, and M.P. Vitek Use of a multiple-enzyme/multiple-reagent assay system to quantify activity levels in samples containing mixtures of matrix metalloproteinases Biochemistry 43 2004 2987 2995
    • (2004) Biochemistry , vol.43 , pp. 2987-2995
    • Rasmussen, F.H.1    Yeung, N.2    Kiefer, L.3    Murphy, G.4    Lopez-Otin, C.5    Vitek, M.P.6
  • 77
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: A new challenge for proteomics
    • C. Lopez-Otin, and C.M. Overall Protease degradomics: a new challenge for proteomics Nat. Rev. Mol. Cell Biol. 3 2002 509 519
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 509-519
    • Lopez-Otin, C.1    Overall, C.M.2


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