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  Gregg B. Fields
Robert A. Welch Foundation Distinguished University Professor in Chemistry

Office Phone: : (210) 567-1312
Office:542C.1 Medical School Building
University of Texas Health Science Center at San Antonio (UTHSCSA)
Department of Biochemistry
7703 Floyd Curl Drive


Areas of Specialization
• Solid-Phase Chemistry
• Extracellular Matrix Biochemistry
                                             • Chemical Biology
Research Interest
My laboratory’s research interests are in the use of chemical approaches to better understand how protein three-dimensional structures influence cellular and enzymatic behaviors. Early studies included the systematic examination of mild methodologies for solid-phase synthesis of small proteins. Chemical approaches have been used to develop “mini-protein” models for the study of cellular recognition processes, which in turn allowed for the mapping of protein domains involved in tumor cell binding and signal transduction. Mini-protein models have subsequently been utilized to dissect the mechanisms of collagen catabolism, and in the process have provided new avenues for protease inhibitor design.

Selected Publications


Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity.
Lauer-Fields JL, Chalmers MJ, Busby SA, Minond D, Griffin PR, Fields GB.
J Biol Chem. 2009 Jul 1. [Epub ahead of print]
PMID: 19574232



Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition.
Lauer-Fields JL, Whitehead JK, Li S, Hammer RP, Brew K, Fields GB
J Biol Chem. 2008 Jul 18;283(29):20087-95.
PMID: 18499673




High throughput screening of potentially selective MMP-13 exosite inhibitors utilizing a triple-helical FRET substrate.
Lauer-Fields JL, Minond D, Chase PS, Baillargeon PE, Saldanha SA, Stawikowska R, Hodder P, Fields GB.
Bioorg Med Chem. 2009 Feb 1;17(3):990-1005.
PMID: 18358729



Screening of potential a disintegrin and metalloproteinase with thrombospondin motifs-4 inhibitors using a collagen model fluorescence resonance energy transfer substrate.
Lauer-Fields JL, Spicer TP, Chase PS, Cudic M, Burstein GD, Nagase H, Hodder P, Fields GB.
Anal Biochem. 2008 Feb 1;373(1):43-51.
PMID: 17949675



Triple-helical transition state analogues: a new class of selective matrix metalloproteinase inhibitors.
Lauer-Fields J, Brew K, Whitehead JK, Li S, Hammer RP, Fields GB.
J Am Chem Soc. 2007 Aug 29;129(34):10408-17.
PMID: 17672455



Synthesis and solid-phase application of suitably protected gamma-hydroxyvaline building blocks.
Cudic M, Marí F, Fields GB.
J Org Chem. 2007 Jul 20;72(15):5581-6.
PMID: 17583956



Targeted drug delivery utilizing protein-like molecular architecture.
Rezler EM, Khan DR, Lauer-Fields J, Cudic M, Baronas-Lowell D, Fields GB.
J Am Chem Soc. 2007 Apr 25;129(16):4961-72.
PMID: 17397150



Differentiation of secreted and membrane-type matrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences.
Minond D, Lauer-Fields JL, Cudic M, Overall CM, Pei D, Brew K, Moss ML, Fields GB.
Biochemistry. 2007 Mar 27;46(12):3724-33.
PMID: 17338550



. Substrate conformation modulates aggrecanase (ADAMTS-4) affinity and sequence specificity. Suggestion of a common topological specificity for functionally diverse proteases
Lauer-Fields JL, Minond D, Sritharan T, Kashiwagi M, Nagase H, Fields GB..
J Biol Chem. 2007 Jan 5;282(1):142-50.
PMID: 17095512



The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity.
Minond D, Lauer-Fields JL, Cudic M, Overall CM, Pei D, Brew K, Visse R, Nagase H, Fields GB.
J Biol Chem. 2006 Dec 15;281(50):38302-13.
PMID: 17065155





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