☰

Janelle Lauer-Fields, Ph.D. - Publications

Affiliations: 
2007 Florida Atlantic University, Boca Raton, FL, United States 
Area:
Biochemistry
Tree Info Similar researchers PubMed Report error

34 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2009 Cudic M, Burstein GD, Fields GB, Lauer-Fields J. Analysis of flavonoid-based pharmacophores that inhibit aggrecanases (ADAMTS-4 and ADAMTS-5) and matrix metalloproteinases through the use of topologically constrained peptide substrates. Chemical Biology & Drug Design. 74: 473-82. PMID 19793184 DOI: 10.1111/J.1747-0285.2009.00885.X  0.552
2009 Lauer-Fields JL, Chalmers MJ, Busby SA, Minond D, Griffin PR, Fields GB. Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity. The Journal of Biological Chemistry. 284: 24017-24. PMID 19574232 DOI: 10.1074/Jbc.M109.016873  0.62
2009 Lauer-Fields JL, Minond D, Chase PS, Baillargeon PE, Saldanha SA, Stawikowska R, Hodder P, Fields GB. High throughput screening of potentially selective MMP-13 exosite inhibitors utilizing a triple-helical FRET substrate. Bioorganic & Medicinal Chemistry. 17: 990-1005. PMID 18358729 DOI: 10.1016/J.Bmc.2008.03.004  0.565
2009 Lauer-Fields J, Fields G. Identification of non-catalytic matrix metalloproteinase 1 residues that participate in collagenolysis. Cancer Research. 69: 2063. DOI: 10.1158/0008-5472.Sabcs-2063  0.618
2008 Bhaskaran R, Palmier MO, Lauer-Fields JL, Fields GB, Van Doren SR. MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity. The Journal of Biological Chemistry. 283: 21779-88. PMID 18539597 DOI: 10.1074/Jbc.M709966200  0.523
2008 Lauer-Fields JL, Whitehead JK, Li S, Hammer RP, Brew K, Fields GB. Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition. The Journal of Biological Chemistry. 283: 20087-95. PMID 18499673 DOI: 10.1074/Jbc.M801438200  0.71
2008 Lauer-Fields JL, Spicer TP, Chase PS, Cudic M, Burstein GD, Nagase H, Hodder P, Fields GB. Screening of potential a disintegrin and metalloproteinase with thrombospondin motifs-4 inhibitors using a collagen model fluorescence resonance energy transfer substrate. Analytical Biochemistry. 373: 43-51. PMID 17949675 DOI: 10.1016/J.Ab.2007.09.014  0.416
2008 Cudic M, Patel DA, Lauer-Fields JL, Brew K, Fields GB. Development of a convenient peptide-based assay for lysyl hydroxylase. Biopolymers. 90: 330-8. PMID 17610258 DOI: 10.1002/Bip.20799  0.503
2007 Lauer-Fields JL, Minond D, Brew K, Fields GB. Application of topologically constrained mini-proteins as ligands, substrates, and inhibitors. Methods in Molecular Biology (Clifton, N.J.). 386: 125-66. PMID 18604945 DOI: 10.1007/978-1-59745-430-8_5  0.586
2007 Lauer-Fields J, Brew K, Whitehead JK, Li S, Hammer RP, Fields GB. Triple-helical transition state analogues: a new class of selective matrix metalloproteinase inhibitors. Journal of the American Chemical Society. 129: 10408-17. PMID 17672455 DOI: 10.1021/Ja0715849  0.707
2007 Lauer-Fields JL, Cudic M, Wei S, Mari F, Fields GB, Brew K. Engineered sarafotoxins as tissue inhibitor of metalloproteinases-like matrix metalloproteinase inhibitors. The Journal of Biological Chemistry. 282: 26948-55. PMID 17626018 DOI: 10.1074/Jbc.M611612200  0.648
2007 Rezler EM, Khan DR, Lauer-Fields J, Cudic M, Baronas-Lowell D, Fields GB. Targeted drug delivery utilizing protein-like molecular architecture. Journal of the American Chemical Society. 129: 4961-72. PMID 17397150 DOI: 10.1021/Ja066929M  0.307
2007 Minond D, Lauer-Fields JL, Cudic M, Overall CM, Pei D, Brew K, Moss ML, Fields GB. Differentiation of secreted and membrane-type matrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences. Biochemistry. 46: 3724-33. PMID 17338550 DOI: 10.1021/Bi062199J  0.696
2007 Lauer-Fields JL, Minond D, Sritharan T, Kashiwagi M, Nagase H, Fields GB. Substrate conformation modulates aggrecanase (ADAMTS-4) affinity and sequence specificity. Suggestion of a common topological specificity for functionally diverse proteases. The Journal of Biological Chemistry. 282: 142-50. PMID 17095512 DOI: 10.1074/Jbc.M605236200  0.402
2006 Minond D, Lauer-Fields JL, Cudic M, Overall CM, Pei D, Brew K, Visse R, Nagase H, Fields GB. The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity. The Journal of Biological Chemistry. 281: 38302-13. PMID 17065155 DOI: 10.1074/Jbc.M606004200  0.688
2005 Möller C, Rahmankhah S, Lauer-Fields J, Bubis J, Fields GB, Marí F. A novel conotoxin framework with a helix-loop-helix (Cs alpha/alpha) fold. Biochemistry. 44: 15986-96. PMID 16331958 DOI: 10.1021/Bi0511181  0.401
2004 Lauer-Fields JL, Nagase H, Fields GB. Development of a solid-phase assay for analysis of matrix metalloproteinase activity. Journal of Biomolecular Techniques : Jbt. 15: 305-16. PMID 15585827  0.505
2004 Minond D, Lauer-Fields JL, Nagase H, Fields GB. Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability. Biochemistry. 43: 11474-81. PMID 15350133 DOI: 10.1021/Bi048938I  0.614
2004 Xu X, Wang Y, Lauer-Fields JL, Fields GB, Steffensen B. Contributions of the MMP-2 collagen binding domain to gelatin cleavage. Substrate binding via the collagen binding domain is required for hydrolysis of gelatin but not short peptides. Matrix Biology : Journal of the International Society For Matrix Biology. 23: 171-81. PMID 15296945 DOI: 10.1016/J.Matbio.2004.05.002  0.604
2004 Baronas-Lowell D, Lauer-Fields JL, Borgia JA, Sferrazza GF, Al-Ghoul M, Minond D, Fields GB. Differential modulation of human melanoma cell metalloproteinase expression by alpha2beta1 integrin and CD44 triple-helical ligands derived from type IV collagen. The Journal of Biological Chemistry. 279: 43503-13. PMID 15292257 DOI: 10.1074/Jbc.M405979200  0.437
2004 Chung L, Dinakarpandian D, Yoshida N, Lauer-Fields JL, Fields GB, Visse R, Nagase H. Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. The Embo Journal. 23: 3020-30. PMID 15257288 DOI: 10.1038/Sj.Emboj.7600318  0.606
2003 Lauer-Fields JL, Kele P, Sui G, Nagase H, Leblanc RM, Fields GB. Analysis of matrix metalloproteinase triple-helical peptidase activity with substrates incorporating fluorogenic L- or D-amino acids. Analytical Biochemistry. 321: 105-15. PMID 12963061 DOI: 10.1016/S0003-2697(03)00460-3  0.558
2003 Sweeney SM, DiLullo G, Slater SJ, Martinez J, Iozzo RV, Lauer-Fields JL, Fields GB, San Antonio JD. Angiogenesis in collagen I requires alpha2beta1 ligation of a GFP*GER sequence and possibly p38 MAPK activation and focal adhesion disassembly. The Journal of Biological Chemistry. 278: 30516-24. PMID 12788934 DOI: 10.1074/Jbc.M304237200  0.317
2003 Malkar NB, Lauer-Fields JL, Juska D, Fields GB. Characterization of peptide-amphiphiles possessing cellular activation sequences. Biomacromolecules. 4: 518-28. PMID 12741765 DOI: 10.1021/Bm0256597  0.362
2003 Lutolf MP, Lauer-Fields JL, Schmoekel HG, Metters AT, Weber FE, Fields GB, Hubbell JA. Synthetic matrix metalloproteinase-sensitive hydrogels for the conduction of tissue regeneration: engineering cell-invasion characteristics. Proceedings of the National Academy of Sciences of the United States of America. 100: 5413-8. PMID 12686696 DOI: 10.1073/Pnas.0737381100  0.467
2003 Lauer-Fields JL, Sritharan T, Stack MS, Nagase H, Fields GB. Selective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9. The Journal of Biological Chemistry. 278: 18140-5. PMID 12642591 DOI: 10.1074/Jbc.M211330200  0.591
2003 Baronas-Lowell D, Lauer-Fields JL, Fields GB. Defining the roles of collagen and collagen-like proteins within the proteome Journal of Liquid Chromatography and Related Technologies. 26: 2225-2254. DOI: 10.1081/Jlc-120023245  0.355
2002 Lauer-Fields JL, Fields GB. Triple-helical peptide analysis of collagenolytic protease activity. Biological Chemistry. 383: 1095-105. PMID 12437092 DOI: 10.1515/Bc.2002.118  0.644
2002 Lauer-Fields JL, Juska D, Fields GB. Matrix metalloproteinases and collagen catabolism. Biopolymers. 66: 19-32. PMID 12228918 DOI: 10.1002/Bip.10201  0.587
2001 Lauer-Fields JL, Broder T, Sritharan T, Chung L, Nagase H, Fields GB. Kinetic analysis of matrix metalloproteinase activity using fluorogenic triple-helical substrates Biochemistry. 40: 5795-5803. PMID 11341845 DOI: 10.1021/Bi0101190  0.631
2000 Lauer-Fields JL, Nagase H, Fields GB. Use of Edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectrometry in designing substrates for matrix metalloproteinases Journal of Chromatography A. 890: 117-125. PMID 10976799 DOI: 10.1016/S0021-9673(00)00396-4  0.605
2000 Lauer-Fields JL, Tuzinski KA, Shimokawa KI, Nagase H, Fields GB. Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases Journal of Biological Chemistry. 275: 13282-13290. PMID 10788434 DOI: 10.1074/Jbc.275.18.13282  0.591
2000 Lauer-Fields JL, Fields GB. Matrix metalloproteinase inhibitors and cancer Expert Opinion On Therapeutic Patents. 10: 1873-1884. DOI: 10.1517/13543776.10.12.1873  0.546
2000 Lauer-Fields JL, Fields GB. Matrix metalloproteinase inhibitors and cancer Expert Opinion On Therapeutic Patents. 10: 1873-1884.  0.546
Show low-probability matches.