In situ AP/MALDI-MS characterization of anchored matrix metalloproteinases (395 views visite)
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2006 Dec; 41(12): 1561-1569.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.945, 5-year impact factor Impact factor a 5 anni: 3.017
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33846021302&partnerID=40&md5=46a54974bb0004c849a19486e5415e04
Keywords Parole chiave: Ap Maldi-Ms, Matrix Metalloproteinases, Mmp Immobilization, Solid-State Assay, Atmospheric Pressure, Bioassay, Enzyme Immobilization, Enzyme Inhibition, Gold, Mass Spectrometry, Molecular Weight, Pathology, Surface Plasmon Resonance, Tumors, Embryogenesis, Matrix Metalloproteinases (mmp), Molecular Mass Identification, Interstitial Collagenase, Macrophage Elastase, Neutrophil Collagenase, Peptidase, Amino Acid Sequence, Conference Paper, Enzyme Activity, Enzyme Analysis, Matrix Assisted Laser Desorption Ionization Time Of Flight Mass Spectrometry, Priority Journal, Protein Determination, Protein Function, Protein Immobilization, Sequence Analysis, Solid State, Humans, Matrix Metalloproteinase 12, Matrix-Assisted Laser Desorption-Ionization, Trypsin,
Affiliations Affiliazioni:
*** IBB - CNR ***
Consorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi Biologici, Via C. Ulpiani 27, Bari, Italy
Magnetic Resonance Center, CERM, University of Florence, Via L. Sacconi, 6, Sesto Fiorentino, Italy
Department of Agricultural Biotechnology, University of Florence, P.le delle Cascine, 24, Florence, Italy
Dipartimento di Scienze Chimiche, Università di Catania, Viale Andrea Doria 6, 95125, Catania, Italy
Istituto Biostrutture e Bioimmagini, CNR, Viale A. Doria 6, Catania, Italy
References Riferimenti:
MacBeath, G., Schreiber, S.L., Printing proteins as microarrays for high-throughput function determination (2000) Science, 289, p. 176
Zhu, H., Bilgin, M., Bangham, R., Hall, D., Casamayor, A., Bertone, P., Lan, N., Snyder, M., Global analysis of protein activities using proteome chips (2001) Science, 293, p. 2101
Houseman, B.T., Huk, J.H., Kron, S.J., Mrksich, M., Peptide chips for the quantitative evaluation of protein kinase activity (2002) Nat. Biotechnol, 20, p. 270
Huber, A., Demartis, S., Neri, D., The use of biosensor technology for the engineering of antibodies and enzymes (1999) J. Mol. Recognit, 12, p. 198
Reymond, J.L., (2006) Enzyme Assays: High-throughput Screening, Genetic Selection and Fingerprinting, , Wiley-VCH Verlag GmbH and Co. KGaA: Weinheim
Min, D., Mrksich, M., Profiling kinase activities by using a peptide chip and mass spectrometry (2004) Angew. Chem., Int. Ed. Engl, 43, p. 5973
Babiak, P., Reymond, J., A high-throughput, low-volume enzyme assay on solid support (2005) Anal. Chem, 77, p. 373
Huber, W., Hoffman, F., A new strategy for improved secondary screening and lead optimization using high-resolution SPR characterization of compound-target interactions (2005) J. Mol. Recognit, 18, p. 273
Nedelkov, D., Nelson, R.W., Surface plasmon resonance mass spectrometry for protein analysis (2006) Methods Mol. Biol, 328, p. 131
Borch, J., Roepstorff, P., Screening for enzyme inhibitors by surface plasmon resonance combined with mass spectrometry (2004) Anal. Chem, 76, p. 5243
Hutchens, T., Yip, T.T., New desorption strategies for the mass spectrometric analysis of macromolecules (1993) Rapid Commun. Mass Spectrom, 7, p. 576
Caputo, E., Moharram, R., Martin, B.M., Methods for on-chip analysis (2003) Anal. Biochem, 321, p. 116
Merchant, M., Weinberger, S.R., Recent advancements in surface-enhanced laser desorption/ionization-time of flight-mass spectrometry (2000) Electrophoresis, 21, p. 1164
Griesser, H.J., Kingshott, P., McArthur, S.L., McLean, K.M., Kinsel, G.R., Timmons, R.B., Surface-MALDI mass spectrometry in biomaterials research (2004) Biomaterials, 25, p. 4861
Clarke, C.H., Buckley, J.A., Fung, E.T., SELDI-TOF-MS proteomics of breast cancer (2005) Clin. Chem. Lab. Med, 43, p. 1314
Bons, J.A.P., Wodzig, W.K.W.H., van Dieijen-Visser, M.P., Protein profiling as a diagnostic tool in clinical chemistry: A review (2005) Clin. Chem. Lab. Med, 43, p. 1281
Issaq, H.J., Conrads, T.P., Prieto, D.A., Tirumalai, R., Veenstra, T.D., SELDI-TOF MS for diagnostic proteomics (2003) Anal. Chem, 1, pp. 149A
Ge, Y., Gibbs, B.F., Masse, R., Complete chemical and enzymatic treatment of phosphorylated and glycosylated proteins on proteinchip arrays (2005) Anal. Chem, 77, p. 3644
Shen, Z., Go, E.P., Gamez, A., Apon, J.V., Fokin, V., Greig, M., Ventura, M., Siuzdak, G., A mass spectrometry plate reader: Monitoring enzyme activity and inhibition with a Desorption/Ionization on Silicon (DIOS) platform (2004) Chembiochem, 5, p. 921
Min, D., Tang, W., Mrksich, M., Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor (2004) Nat. Biotechnol, 22, p. 717
Bornsen, K.O., Gass, M.A.S., Bruin, G.J.M., von Adrichem, J.H.M., Biro, M.C., Kresbach, G.M., Ehrat, M., Influence of solvents and detergents on matrix-assisted laser desorption/ionization mass spectrometry measurements of proteins and oligonucleotides (1997) Rapid Commun. Mass Spectrom, 11, p. 603
Brockman, A.H., Dodd, B.S., Orlando, N., A desalting approach for MALDI-MS using on-probe hydrofobic self-assembled monolayers (1997) Anal. Chem, 69, p. 4716
Worral, T.A., Cotter, R.J., Woods, A.S., Purification of contaminated peptides on synthetic membrane surfaces for matrix-assisted laser desorption/ionization mass spectrometry (1998) Anal. Chem, 70, p. 750
Warren, M.E., Brockman, A.H., Orlando, R., On-probe solid-phase extraction/MALDI-MS using ion-pairing interactions for the cleanup of peptides and proteins (1998) Anal. Chem, 70, p. 3757
Xu, Y., Watson, J.T., Bruening, M.L., Patterned monolayer/polymer films for analysis of dilute or salt-contaminated protein samples by MALDI-MS (2003) Anal. Chem, 75, p. 185
Wang, Y., Xia, X., Guo, Y., Porous anodic alumina membrane as a sample support for MALDI-TOF MS analysis of salt-containing proteins (2005) J. Am. Soc. Mass Spectrom, 16, p. 1488
Smirnov, I.P., Zhu, X., Taylor, T., Huang, Y., Ross, P., Papayanopoulos, I.A., Martin, S.A., Pappin, D.J., Suppression of α-Cyano-4-hydroxycinnamic acid matrix clusters and reduction of chemical noise in MALDI-TOF mass spectrometry (2004) Anal. Chem, 76, p. 2958
Kim, J.-S., Kim, J.-Y., Kim, H.-J., Suppression of matrix clusters and enhancement of peptide signals in MALDI-TOF mass spectrometry using nitrilotriacetic acid (2005) Anal. Chem, 77, p. 7483
Newton, K.A., McLuckey, S.A., Generation and manipulation of Sodium cationized peptides in the gas phase (2004) J. Am. Soc. Mass Spectrom, 15, p. 607
Su, J., Mrksich, M., Using MALDI-TOF mass spectrometry to characterize interfacial reactions on self-assembled monolayers (2003) Langmuir, 19, p. 4867
Grasso, G., D'Agata, R., Rizzarelli, E., Spoto, G., D'Andrea, L., Pedone, C., Picardi, A., Yeo, K.J., Activity of anchored human matrix metalloproteinase-1 catalytic domain on au (111) surfaces monitored by ESI-MS (2005) J. Mass Spectrom, 40, p. 1565
Massova, I., Kotra, L.P., Fridman, R., Mobashery, S., Matrix metalloproteinases: Structures, evolution, and diversification (1998) FASEB J, 12, p. 1075
Coussens, L.M., Werb, Z., Matrix metalloproteinases and the development of cancer (1996) Chem. Biol, 3, p. 895
Koivunen, E., Arap, W., Valtanen, H., Rainisalo, A., Medina, O.P., Heikkilä, P., Kantor, C., Pasqualini, R., Tumor targeting with a selective gelatinase inhibitor (1999) Nat. Biotechnol, 17, p. 768
Farkas, E., Katz, Y., Bhusare, S., Reich, R., Röschenthaler, G., Königsmann, M., Breuer, E., Carbamoylphosphonate Based Matrix Metalloproteinase (MMP) inhibitor metal complexes-solution studies and stability constants. Towards a zinc selective binding group (2004) J. Biol. Inorg. Chem, 9, p. 307
Schneider, B.B., Lock, C., Covey, T.R., AP and vacuum MALDI on a QqLIT instrument (2005) J. Am. Soc. Mass Spectrom, 16, p. 176
Trimpin, S., Deinzer, M.L., Solvent-free MALDI-MS for the analysis of biological samples via a mini-ball mill approach (2005) J. Am. Soc. Mass Spectrom, 16, p. 542
Whitesides, G., Xia, Y., Soft lithography (1998) Angew. Chem., Int. Ed. Engl, 37, p. 550
Navratilova, I., Eisenstien, E., Myszka, D.G., Measuring long association phases using Biacore (2005) Anal. Biochem, 344, p. 295
Larsericsdotter, H., Oscarsson, S., Buijs, J., Structure, stability, and orientation of BSA adsorbed to silica (2005) J. Colloid Interface Sci, 289, p. 26
Tan, P.V., Laiko, V.V., Doroshenko, V.M., Atmospheric pressure MALDI with pulsed dynamic focusing for high-efficiency transmission of ions into a mass spectrometer (2004) Anal. Chem, 75, p. 2462
Bertini, I., Calderone, V., Cosenza, M., Fragai, M., Lee, Y.-M., Luchinat, C., Mangani, S., Turano, P., Conformational variability of matrix metalloproteinases: Beyond a single 3D structure (2005) Proc. Natl. Acad. Sci. U.S.A, 102, p. 5334
Buchardt, J., Schiodt, C.B., Krog-Jensen, C., Delaisse, J.-M., Foged, N.T., Meldal, M., Solid phase combinatorial library of phosphinic peptides for discovery of matrix metalloproteinase inhibitors (2000) J. Comb. Chem, 2, p. 624
Feng, R., Castelhano, A.L., Billedeau, R., Yuan, Z., Study of noncovalent enzyme-inhibitor complexes and metal binding stoichiometry of matrilysin by electrospray ionization mass spectrometry (1995) J. Am. Soc. Mass Spectrom, 6, p. 1105
Sung, J.Y., Park, S.M., Lee, C.-H., Um, J.W., Lee, H.J., Kim, J., Oh, Y.J., Chung, K.C., Proteolytic cleavage of extracellular secreted a-synuclein via matrix metalloproteinases (2005) J. Biol. Chem, 280, pp. 25-216
Lauer-Fields, J.L., Nagase, H., Fields, G.B., Use of edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases (2000) J. Chromatogr., A, 890, p. 117
Gossas, T., Danielason, U.H., Characterization of Ca2+ interactions with matrix metallopeptidase-12: Implications for matrix metallopeptidase regulation (2006) Biochem. J, 398, p. 393
Willenbrock, F., Murphy, G., Phillips, I.R., Brocklehurst, K., The second zinc atom in the matrix metalloproteinase catalytic domain is absent in the full-length enzymes: A possible role for the C-terminal domain (1995) FEBS Lett, 358, p. 189
Knaeuper, V., Docherty, A.J.P., Smith, B., Tschesche, H., Murphy, G., Analysis of the contribution of the hinge region of human neutrophil collagenase (HNC, MMP-8) to stability and collagenolytic activity by alanine scanning mutagenesis (1997) FEBS Lett, 405, p. 60
Kondo, A., Urabe, T., Temperature dependence of activity and conformational changes in a-amylases with different thermostability upon adsorption on ultrafine silica particles (1995) J. Colloid Interface Sci, 174, p. 191
Keller, A., Purvine, S., Nesvizhskii, A., Stolyar, S., Goodlett, D.R., Kolker, E., Experimental protein mixture for validating tandem mass spectral analysis (2002) OMICS, 6, p. 207
Houseman, B. T., Huk, J. H., Kron, S. J., Mrksich, M., Peptide chips for the quantitative evaluation of protein kinase activity (2002) Nat. Biotechnol, 20, p. 270
Reymond, J. L., (2006) Enzyme Assays: High-throughput Screening, Genetic Selection and Fingerprinting, , Wiley-VCH Verlag GmbH and Co. KGaA: Weinheim
Griesser, H. J., Kingshott, P., McArthur, S. L., McLean, K. M., Kinsel, G. R., Timmons, R. B., Surface-MALDI mass spectrometry in biomaterials research (2004) Biomaterials, 25, p. 4861
Clarke, C. H., Buckley, J. A., Fung, E. T., SELDI-TOF-MS proteomics of breast cancer (2005) Clin. Chem. Lab. Med, 43, p. 1314
Bons, J. A. P., Wodzig, W. K. W. H., van Dieijen-Visser, M. P., Protein profiling as a diagnostic tool in clinical chemistry: A review (2005) Clin. Chem. Lab. Med, 43, p. 1281
Issaq, H. J., Conrads, T. P., Prieto, D. A., Tirumalai, R., Veenstra, T. D., SELDI-TOF MS for diagnostic proteomics (2003) Anal. Chem, 1, pp. 149A
Ge, Y., Gibbs, B. F., Masse, R., Complete chemical and enzymatic treatment of phosphorylated and glycosylated proteins on proteinchip arrays (2005) Anal. Chem, 77, p. 3644
Shen, Z., Go, E. P., Gamez, A., Apon, J. V., Fokin, V., Greig, M., Ventura, M., Siuzdak, G., A mass spectrometry plate reader: Monitoring enzyme activity and inhibition with a Desorption/Ionization on Silicon (DIOS) platform (2004) Chembiochem, 5, p. 921
Bornsen, K. O., Gass, M. A. S., Bruin, G. J. M., von Adrichem, J. H. M., Biro, M. C., Kresbach, G. M., Ehrat, M., Influence of solvents and detergents on matrix-assisted laser desorption/ionization mass spectrometry measurements of proteins and oligonucleotides (1997) Rapid Commun. Mass Spectrom, 11, p. 603
Brockman, A. H., Dodd, B. S., Orlando, N., A desalting approach for MALDI-MS using on-probe hydrofobic self-assembled monolayers (1997) Anal. Chem, 69, p. 4716
Worral, T. A., Cotter, R. J., Woods, A. S., Purification of contaminated peptides on synthetic membrane surfaces for matrix-assisted laser desorption/ionization mass spectrometry (1998) Anal. Chem, 70, p. 750
Warren, M. E., Brockman, A. H., Orlando, R., On-probe solid-phase extraction/MALDI-MS using ion-pairing interactions for the cleanup of peptides and proteins (1998) Anal. Chem, 70, p. 3757
Xu, Y., Watson, J. T., Bruening, M. L., Patterned monolayer/polymer films for analysis of dilute or salt-contaminated protein samples by MALDI-MS (2003) Anal. Chem, 75, p. 185
Smirnov, I. P., Zhu, X., Taylor, T., Huang, Y., Ross, P., Papayanopoulos, I. A., Martin, S. A., Pappin, D. J., Suppression of -Cyano-4-hydroxycinnamic acid matrix clusters and reduction of chemical noise in MALDI-TOF mass spectrometry (2004) Anal. Chem, 76, p. 2958
Kim, J. -S., Kim, J. -Y., Kim, H. -J., Suppression of matrix clusters and enhancement of peptide signals in MALDI-TOF mass spectrometry using nitrilotriacetic acid (2005) Anal. Chem, 77, p. 7483
Newton, K. A., McLuckey, S. A., Generation and manipulation of Sodium cationized peptides in the gas phase (2004) J. Am. Soc. Mass Spectrom, 15, p. 607
Coussens, L. M., Werb, Z., Matrix metalloproteinases and the development of cancer (1996) Chem. Biol, 3, p. 895
Schneider, B. B., Lock, C., Covey, T. R., AP and vacuum MALDI on a QqLIT instrument (2005) J. Am. Soc. Mass Spectrom, 16, p. 176
Tan, P. V., Laiko, V. V., Doroshenko, V. M., Atmospheric pressure MALDI with pulsed dynamic focusing for high-efficiency transmission of ions into a mass spectrometer (2004) Anal. Chem, 75, p. 2462
Sung, J. Y., Park, S. M., Lee, C. -H., Um, J. W., Lee, H. J., Kim, J., Oh, Y. J., Chung, K. C., Proteolytic cleavage of extracellular secreted a-synuclein via matrix metalloproteinases (2005) J. Biol. Chem, 280, pp. 25-216
Lauer-Fields, J. L., Nagase, H., Fields, G. B., Use of edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases (2000) J. Chromatogr., A, 890, p. 117
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2006 Dec; 41(12): 1561-1569.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.945, 5-year impact factor Impact factor a 5 anni: 3.017
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33846021302&partnerID=40&md5=46a54974bb0004c849a19486e5415e04
Keywords Parole chiave: Ap Maldi-Ms, Matrix Metalloproteinases, Mmp Immobilization, Solid-State Assay, Atmospheric Pressure, Bioassay, Enzyme Immobilization, Enzyme Inhibition, Gold, Mass Spectrometry, Molecular Weight, Pathology, Surface Plasmon Resonance, Tumors, Embryogenesis, Matrix Metalloproteinases (mmp), Molecular Mass Identification, Interstitial Collagenase, Macrophage Elastase, Neutrophil Collagenase, Peptidase, Amino Acid Sequence, Conference Paper, Enzyme Activity, Enzyme Analysis, Matrix Assisted Laser Desorption Ionization Time Of Flight Mass Spectrometry, Priority Journal, Protein Determination, Protein Function, Protein Immobilization, Sequence Analysis, Solid State, Humans, Matrix Metalloproteinase 12, Matrix-Assisted Laser Desorption-Ionization, Trypsin,
Affiliations Affiliazioni:
*** IBB - CNR ***
Consorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi Biologici, Via C. Ulpiani 27, Bari, Italy
Magnetic Resonance Center, CERM, University of Florence, Via L. Sacconi, 6, Sesto Fiorentino, Italy
Department of Agricultural Biotechnology, University of Florence, P.le delle Cascine, 24, Florence, Italy
Dipartimento di Scienze Chimiche, Università di Catania, Viale Andrea Doria 6, 95125, Catania, Italy
Istituto Biostrutture e Bioimmagini, CNR, Viale A. Doria 6, Catania, Italy
References Riferimenti:
MacBeath, G., Schreiber, S.L., Printing proteins as microarrays for high-throughput function determination (2000) Science, 289, p. 176
Zhu, H., Bilgin, M., Bangham, R., Hall, D., Casamayor, A., Bertone, P., Lan, N., Snyder, M., Global analysis of protein activities using proteome chips (2001) Science, 293, p. 2101
Houseman, B.T., Huk, J.H., Kron, S.J., Mrksich, M., Peptide chips for the quantitative evaluation of protein kinase activity (2002) Nat. Biotechnol, 20, p. 270
Huber, A., Demartis, S., Neri, D., The use of biosensor technology for the engineering of antibodies and enzymes (1999) J. Mol. Recognit, 12, p. 198
Reymond, J.L., (2006) Enzyme Assays: High-throughput Screening, Genetic Selection and Fingerprinting, , Wiley-VCH Verlag GmbH and Co. KGaA: Weinheim
Min, D., Mrksich, M., Profiling kinase activities by using a peptide chip and mass spectrometry (2004) Angew. Chem., Int. Ed. Engl, 43, p. 5973
Babiak, P., Reymond, J., A high-throughput, low-volume enzyme assay on solid support (2005) Anal. Chem, 77, p. 373
Huber, W., Hoffman, F., A new strategy for improved secondary screening and lead optimization using high-resolution SPR characterization of compound-target interactions (2005) J. Mol. Recognit, 18, p. 273
Nedelkov, D., Nelson, R.W., Surface plasmon resonance mass spectrometry for protein analysis (2006) Methods Mol. Biol, 328, p. 131
Borch, J., Roepstorff, P., Screening for enzyme inhibitors by surface plasmon resonance combined with mass spectrometry (2004) Anal. Chem, 76, p. 5243
Hutchens, T., Yip, T.T., New desorption strategies for the mass spectrometric analysis of macromolecules (1993) Rapid Commun. Mass Spectrom, 7, p. 576
Caputo, E., Moharram, R., Martin, B.M., Methods for on-chip analysis (2003) Anal. Biochem, 321, p. 116
Merchant, M., Weinberger, S.R., Recent advancements in surface-enhanced laser desorption/ionization-time of flight-mass spectrometry (2000) Electrophoresis, 21, p. 1164
Griesser, H.J., Kingshott, P., McArthur, S.L., McLean, K.M., Kinsel, G.R., Timmons, R.B., Surface-MALDI mass spectrometry in biomaterials research (2004) Biomaterials, 25, p. 4861
Clarke, C.H., Buckley, J.A., Fung, E.T., SELDI-TOF-MS proteomics of breast cancer (2005) Clin. Chem. Lab. Med, 43, p. 1314
Bons, J.A.P., Wodzig, W.K.W.H., van Dieijen-Visser, M.P., Protein profiling as a diagnostic tool in clinical chemistry: A review (2005) Clin. Chem. Lab. Med, 43, p. 1281
Issaq, H.J., Conrads, T.P., Prieto, D.A., Tirumalai, R., Veenstra, T.D., SELDI-TOF MS for diagnostic proteomics (2003) Anal. Chem, 1, pp. 149A
Ge, Y., Gibbs, B.F., Masse, R., Complete chemical and enzymatic treatment of phosphorylated and glycosylated proteins on proteinchip arrays (2005) Anal. Chem, 77, p. 3644
Shen, Z., Go, E.P., Gamez, A., Apon, J.V., Fokin, V., Greig, M., Ventura, M., Siuzdak, G., A mass spectrometry plate reader: Monitoring enzyme activity and inhibition with a Desorption/Ionization on Silicon (DIOS) platform (2004) Chembiochem, 5, p. 921
Min, D., Tang, W., Mrksich, M., Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor (2004) Nat. Biotechnol, 22, p. 717
Bornsen, K.O., Gass, M.A.S., Bruin, G.J.M., von Adrichem, J.H.M., Biro, M.C., Kresbach, G.M., Ehrat, M., Influence of solvents and detergents on matrix-assisted laser desorption/ionization mass spectrometry measurements of proteins and oligonucleotides (1997) Rapid Commun. Mass Spectrom, 11, p. 603
Brockman, A.H., Dodd, B.S., Orlando, N., A desalting approach for MALDI-MS using on-probe hydrofobic self-assembled monolayers (1997) Anal. Chem, 69, p. 4716
Worral, T.A., Cotter, R.J., Woods, A.S., Purification of contaminated peptides on synthetic membrane surfaces for matrix-assisted laser desorption/ionization mass spectrometry (1998) Anal. Chem, 70, p. 750
Warren, M.E., Brockman, A.H., Orlando, R., On-probe solid-phase extraction/MALDI-MS using ion-pairing interactions for the cleanup of peptides and proteins (1998) Anal. Chem, 70, p. 3757
Xu, Y., Watson, J.T., Bruening, M.L., Patterned monolayer/polymer films for analysis of dilute or salt-contaminated protein samples by MALDI-MS (2003) Anal. Chem, 75, p. 185
Wang, Y., Xia, X., Guo, Y., Porous anodic alumina membrane as a sample support for MALDI-TOF MS analysis of salt-containing proteins (2005) J. Am. Soc. Mass Spectrom, 16, p. 1488
Smirnov, I.P., Zhu, X., Taylor, T., Huang, Y., Ross, P., Papayanopoulos, I.A., Martin, S.A., Pappin, D.J., Suppression of α-Cyano-4-hydroxycinnamic acid matrix clusters and reduction of chemical noise in MALDI-TOF mass spectrometry (2004) Anal. Chem, 76, p. 2958
Kim, J.-S., Kim, J.-Y., Kim, H.-J., Suppression of matrix clusters and enhancement of peptide signals in MALDI-TOF mass spectrometry using nitrilotriacetic acid (2005) Anal. Chem, 77, p. 7483
Newton, K.A., McLuckey, S.A., Generation and manipulation of Sodium cationized peptides in the gas phase (2004) J. Am. Soc. Mass Spectrom, 15, p. 607
Su, J., Mrksich, M., Using MALDI-TOF mass spectrometry to characterize interfacial reactions on self-assembled monolayers (2003) Langmuir, 19, p. 4867
Grasso, G., D'Agata, R., Rizzarelli, E., Spoto, G., D'Andrea, L., Pedone, C., Picardi, A., Yeo, K.J., Activity of anchored human matrix metalloproteinase-1 catalytic domain on au (111) surfaces monitored by ESI-MS (2005) J. Mass Spectrom, 40, p. 1565
Massova, I., Kotra, L.P., Fridman, R., Mobashery, S., Matrix metalloproteinases: Structures, evolution, and diversification (1998) FASEB J, 12, p. 1075
Coussens, L.M., Werb, Z., Matrix metalloproteinases and the development of cancer (1996) Chem. Biol, 3, p. 895
Koivunen, E., Arap, W., Valtanen, H., Rainisalo, A., Medina, O.P., Heikkilä, P., Kantor, C., Pasqualini, R., Tumor targeting with a selective gelatinase inhibitor (1999) Nat. Biotechnol, 17, p. 768
Farkas, E., Katz, Y., Bhusare, S., Reich, R., Röschenthaler, G., Königsmann, M., Breuer, E., Carbamoylphosphonate Based Matrix Metalloproteinase (MMP) inhibitor metal complexes-solution studies and stability constants. Towards a zinc selective binding group (2004) J. Biol. Inorg. Chem, 9, p. 307
Schneider, B.B., Lock, C., Covey, T.R., AP and vacuum MALDI on a QqLIT instrument (2005) J. Am. Soc. Mass Spectrom, 16, p. 176
Trimpin, S., Deinzer, M.L., Solvent-free MALDI-MS for the analysis of biological samples via a mini-ball mill approach (2005) J. Am. Soc. Mass Spectrom, 16, p. 542
Whitesides, G., Xia, Y., Soft lithography (1998) Angew. Chem., Int. Ed. Engl, 37, p. 550
Navratilova, I., Eisenstien, E., Myszka, D.G., Measuring long association phases using Biacore (2005) Anal. Biochem, 344, p. 295
Larsericsdotter, H., Oscarsson, S., Buijs, J., Structure, stability, and orientation of BSA adsorbed to silica (2005) J. Colloid Interface Sci, 289, p. 26
Tan, P.V., Laiko, V.V., Doroshenko, V.M., Atmospheric pressure MALDI with pulsed dynamic focusing for high-efficiency transmission of ions into a mass spectrometer (2004) Anal. Chem, 75, p. 2462
Bertini, I., Calderone, V., Cosenza, M., Fragai, M., Lee, Y.-M., Luchinat, C., Mangani, S., Turano, P., Conformational variability of matrix metalloproteinases: Beyond a single 3D structure (2005) Proc. Natl. Acad. Sci. U.S.A, 102, p. 5334
Buchardt, J., Schiodt, C.B., Krog-Jensen, C., Delaisse, J.-M., Foged, N.T., Meldal, M., Solid phase combinatorial library of phosphinic peptides for discovery of matrix metalloproteinase inhibitors (2000) J. Comb. Chem, 2, p. 624
Feng, R., Castelhano, A.L., Billedeau, R., Yuan, Z., Study of noncovalent enzyme-inhibitor complexes and metal binding stoichiometry of matrilysin by electrospray ionization mass spectrometry (1995) J. Am. Soc. Mass Spectrom, 6, p. 1105
Sung, J.Y., Park, S.M., Lee, C.-H., Um, J.W., Lee, H.J., Kim, J., Oh, Y.J., Chung, K.C., Proteolytic cleavage of extracellular secreted a-synuclein via matrix metalloproteinases (2005) J. Biol. Chem, 280, pp. 25-216
Lauer-Fields, J.L., Nagase, H., Fields, G.B., Use of edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases (2000) J. Chromatogr., A, 890, p. 117
Gossas, T., Danielason, U.H., Characterization of Ca2+ interactions with matrix metallopeptidase-12: Implications for matrix metallopeptidase regulation (2006) Biochem. J, 398, p. 393
Willenbrock, F., Murphy, G., Phillips, I.R., Brocklehurst, K., The second zinc atom in the matrix metalloproteinase catalytic domain is absent in the full-length enzymes: A possible role for the C-terminal domain (1995) FEBS Lett, 358, p. 189
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In situ AP/MALDI-MS characterization of anchored matrix metalloproteinases
Several different procedures are available for the immobilization of proteins on solid supports, as many advantages derive from this approach, such as the possibility to develop new protein solid-state assays. Enzymes that are anchored on gold surfaces can interact with several different molecules in a tag-free environment, opening the way to surface plasmon resonance (SPR) investigations. Nevertheless, it is often important to know the identity of the affinity-retained analyte, and mass spectrometric analysis, via its unique molecular mass identification, represents a very valuable complementary method. There are many pieces of evidence to suggest that matrix metalloproteinases (MMPs) are involved in normal and pathological processes, including embryogenesis, wound healing, inflammation, arthritis and cancer, but presumably also exhibiting other functions. The search for new inhibitors of MMI's has prompted research towards the development of new solid-state assays for the rapid evaluation of NIMP activity. We have already reported the possibility of measuring the activity of NIMP-1 anchored on solid support by coupling SPR with ESI-MS analysis. In this work, we show the in situ atmospheric pressure (AP) MALDI-MS characterization of MMPs anchored on a gold chip with known surface coverage. The study extends the MS analysis to different proteins, and sequence coverage is reported for different digestion and MS procedures. Copyright (c) 2006 John Wiley & Sons, Ltd.
Several different procedures are available for the immobilization of proteins on solid supports, as many advantages derive from this approach, such as the possibility to develop new protein solid-state assays. Enzymes that are anchored on gold surfaces can interact with several different molecules in a tag-free environment, opening the way to surface plasmon resonance (SPR) investigations. Nevertheless, it is often important to know the identity of the affinity-retained analyte, and mass spectrometric analysis, via its unique molecular mass identification, represents a very valuable complementary method. There are many pieces of evidence to suggest that matrix metalloproteinases (MMPs) are involved in normal and pathological processes, including embryogenesis, wound healing, inflammation, arthritis and cancer, but presumably also exhibiting other functions. The search for new inhibitors of MMI's has prompted research towards the development of new solid-state assays for the rapid evaluation of NIMP activity. We have already reported the possibility of measuring the activity of NIMP-1 anchored on solid support by coupling SPR with ESI-MS analysis. In this work, we show the in situ atmospheric pressure (AP) MALDI-MS characterization of MMPs anchored on a gold chip with known surface coverage. The study extends the MS analysis to different proteins, and sequence coverage is reported for different digestion and MS procedures. Copyright (c) 2006 John Wiley & Sons, Ltd.
In situ AP/MALDI-MS characterization of anchored matrix metalloproteinases
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In situ AP/MALDI-MS characterization of anchored matrix metalloproteinases
Squeglia F, Ruggiero A, Berisio R
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16 Records (16 escludendo Abstract e Conferenze).
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Impact factor a 5 anni totale: 60.939 (60.939 escludendo Abstract e Conferenze).
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Squeglia F, Ruggiero A, Berisio R
* Collagen degradation in tuberculosis pathogenesis: the biochemical consequences of hosting an undesired guest (359 visite)
Biochem J (ISSN: 1470-8728electronic, 0264-6021linking, 0264-6021print), 2018 Oct 11; 475(19): 3123-3140.
Impact Factor: 4.897
Dettagli Esporta in BibTeX Esporta in EndNote
Zinnhardt B, Viel T, Wachsmuth L, Vrachimis A, Wagner S, Breyholz HJ, Faust A, Hermann S, Kopka K, Faber C, Dolle F, Pappata S, Planas AM, Tavitian B, Schafers M, Sorokin LM, Kuhlmann MT, Jacobs AH
* Multimodal imaging reveals temporal and spatial microglia and matrix metalloproteinase activity after experimental stroke (295 visite)
J Cerebr Blood F Met (ISSN: 0271-678x), 2015 Nov; 35(11): 1711-1721.
Impact Factor: 4.929
Dettagli Esporta in BibTeX Esporta in EndNote
Catanzaro V, Gringeri CV, Menchise V, Padovan S, Boffa C, Dastru W, Chaabane L, Digilio G, Aime S
* A R2p/R1p ratiometric procedure to assess matrix metalloproteinase-2 activity by magnetic resonance imaging (344 visite)
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Impact Factor: 11.336
Dettagli Esporta in BibTeX Esporta in EndNote
Gringeri CV, Menchise V, Rizzitelli S, Cittadino E, Catanzaro V, Dati G, Chaabane L, Digilio G, Aime S
* Novel Gd(III)-based probes for MR molecular imaging of matrix metalloproteinases (445 visite)
Contrast Media Mol Imaging (ISSN: 1555-4309, 1555-4309linking), 2012 Mar; 7(2): 175-184.
Impact Factor: 2.872
Dettagli Esporta in BibTeX Esporta in EndNote
Spoto G, Grasso G
* Spatially resolved mass spectrometry in the study of art and archaeological objects (186 visite)
Trac Trends In Analytical Chemistry (ISSN: 0165-9936), 2011 Jun; 30(6): 856-863.
Impact Factor: 6.273
Dettagli Esporta in BibTeX Esporta in EndNote
Del Vecchio S, Zannetti A, Iommelli F, Lettieri A, Brunetti A, Salvatore M
* Molecular imaging of tumor microenvironment (427 visite)
Q J Nucl Med Mol Im (ISSN: 1824-4785, 1824-4478, 1824-4785linking), 2010 Jun; 54(3): 243-258.
Impact Factor: 1.724
Dettagli Esporta in BibTeX Esporta in EndNote
Del Vecchio S, Zannetti A, Iommelli F, Lettieri A, Brunetti A, Salvatore M
* Molecular imaging of tumor microenvironment: Challenges and perspectives (557 visite)
Q J Nucl Med Mol Im (ISSN: 1824-4785, 1824-4478, 1824-4785linking), 2010 Jun; 54(3): 249-258.
Impact Factor: 1.724
Dettagli Esporta in BibTeX Esporta in EndNote
Giurato P, Candura A, Grasso G, Spoto G
* In situ identification of organic components of ink used in books from the 1900s by atmospheric pressure matrix assisted laser desorption ionization mass spectrometry (266 visite)
Appl Phys A (ISSN: 0947-8396), 2009 Nov; 97(2): 263-269.
Impact Factor: 1.595
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso G, Rizzarelli E, Spoto G
* The proteolytic activity of insulin-degrading enzyme: a mass spectrometry study (385 visite)
J Mass Spectrom (ISSN: 1096-9888, 1076-5174), 2009 May; 44(5): 735-741.
Impact Factor: 3.411
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso G, Bush AI, D'Agata R, Rizzarelli E, Spoto G
* Enzyme solid-state support assays: a surface plasmon resonance and mass spectrometry coupled study of immobilized insulin degrading enzyme (356 visite)
Eur Biophys J (ISSN: 1432-1017, 0175-7571), 2009 Apr; 38(4): 407-414.
Impact Factor: 2.437
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso G, D'Urso L, Messina E, Cataldo F, Puglisi O, Spoto G, Compagnini G
* A mass spectrometry and surface enhanced Raman spectroscopy study of the interaction between linear carbon chains and noble metals (438 visite)
Carbon (ISSN: 0008-6223), 2009; 47(11): 2611-2619.
Impact Factor: 4.504
Dettagli Esporta in BibTeX Esporta in EndNote
Gioia M, Monaco S, Van Den Steen PE, Sbardella D, Grasso G, Marini S, Overall CM, Opdenakker G, Coletta M
* The Collagen Binding Domain of Gelatinase A Modulates Degradation of Collagen IV by Gelatinase (413 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009; 386(2): 419-434.
Impact Factor: 3.871
Dettagli Esporta in BibTeX Esporta in EndNote
Licciardello MP, D'Agata R, Grasso G, Simone S, Spoto G
* Atmospheric Pressure Laser Desorption Mass Spectrometry based methods for the study of traditional painting materials (208 visite)
Lasers Conserv Artworks Proc Int Conf Lacona Vii (ISSN: 9780-4154), 2008; N/D: 67-72.
Impact Factor: 0
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso G, Fragai M, Rizzarelli E, Spoto G, Yeo KJ
* A new methodology for monitoring the activity of cdMMP-12 anchored and freeze-dried on Au (111) (311 visite)
Journal Of The American Society For Mass Spectrometry (ISSN: 1044-0305), 2007 May; 18(5): 961-969.
Impact Factor: 3.664
Dettagli Esporta in BibTeX Esporta in EndNote
D'Agata R, Grasso G, Parlato S, Simone S, Spoto G
* The use of atmospheric pressure laser desorption mass spectrometry for the study of iron-gall ink (259 visite)
Appl Phys A (ISSN: 0947-8396), 2007; 89(1): 91-95.
Impact Factor: 1.857
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso G, D'Agata R, Rizzarelli E, Spoto G, D'Andrea LD, Pedone C, Picardi A, Romanelli A, Fragai M, Yeo KJ
* Activity of anchored human matrix metalloproteinase-1 catalytic domain on Au(111) surfaces monitored by ESI-MS (499 visite)
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2005 Dec; 40(12): 1565-1571.
Impact Factor: 3.574
Dettagli Esporta in BibTeX Esporta in EndNote
16 Records (16 escludendo Abstract e Conferenze).
Impact factor totale: 58.668 (58.668 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 60.939 (60.939 escludendo Abstract e Conferenze).
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