His primary areas of study are Biochemistry, Matrix metalloproteinase, Stereochemistry, Peptide and Peptide sequence. His research investigates the connection between Biochemistry and topics such as Type I collagen that intersect with issues in Tube formation. Gregg B. Fields has researched Matrix metalloproteinase in several fields, including Proteases, Cathepsin, Wound healing, Triple helix and Extracellular matrix.
His biological study spans a wide range of topics, including Active site, Solvent and Peptide synthesis. His work deals with themes such as Crystallography and Cell adhesion, which intersect with Peptide. His study in Peptide sequence is interdisciplinary in nature, drawing from both Matrix Metalloproteinase 3 and Sequence.
His primary areas of investigation include Matrix metalloproteinase, Biochemistry, Peptide, Stereochemistry and Cell biology. His work carried out in the field of Matrix metalloproteinase brings together such families of science as Proteolysis, Extracellular matrix, Binding site and Triple helix. As part of the same scientific family, he usually focuses on Biochemistry, concentrating on Biophysics and intersecting with Lipid bilayer.
His research integrates issues of Amino acid, Covalent bond, Molecular biology, Cell adhesion and Combinatorial chemistry in his study of Peptide. His Combinatorial chemistry research incorporates elements of Phase and Solid-phase synthesis. His work in Stereochemistry addresses subjects such as Cleavage, which are connected to disciplines such as Collagenase.
His primary scientific interests are in Matrix metalloproteinase, Biochemistry, Peptide, Cancer research and Proteolysis. The concepts of his Matrix metalloproteinase study are interwoven with issues in Cancer, Stereochemistry, Triple helix and Binding site. His Stereochemistry study incorporates themes from Peptide sequence, Crystal structure and Peptide synthesis.
His Peptide research is multidisciplinary, relying on both Combinatorial chemistry, Molecular biology and Drug delivery. His Cancer research research is multidisciplinary, incorporating perspectives in Protease, Metalloproteinase and Proteomics. His studies deal with areas such as Proteases and Biophysics as well as Proteolysis.
The scientist’s investigation covers issues in Matrix metalloproteinase, Binding site, Cancer research, Peptide and Matrix metalloproteinase inhibitor. His Matrix metalloproteinase research includes themes of Wound healing, Cancer, Angiogenesis and Stereochemistry. Binding site is a subfield of Biochemistry that he investigates.
The concepts of his Peptide study are interwoven with issues in Transition state analog, Peptide sequence and Triple helix. His study looks at the intersection of Matrix metalloproteinase inhibitor and topics like Clinical trial with Pancreatic cancer and Mediator. Gregg B. Fields works mostly in the field of In vitro, limiting it down to topics relating to Amino acid and, in certain cases, Combinatorial chemistry, as a part of the same area of interest.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Solid phase peptide synthesis utilizing 9‐fluorenylmethoxycarbonyl amino acids
Gregg B. Fields;Richard L. Noble.
International Journal of Peptide and Protein Research (2009)
Synthetic matrix metalloproteinase-sensitive hydrogels for the conduction of tissue regeneration: Engineering cell-invasion characteristics
M. P. Lutolf;J. L. Lauer-Fields;H. G. Schmoekel;H. G. Schmoekel;A. T. Metters.
Proceedings of the National Academy of Sciences of the United States of America (2003)
A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis.
David S. King;Cynthia G. Fields;Gregg B. Fields.
International Journal of Peptide and Protein Research (2009)
Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis
Linda Chung;Linda Chung;Deendayal Dinakarpandian;Naoto Yoshida;Janelle L Lauer-Fields;Janelle L Lauer-Fields.
The EMBO Journal (2004)
Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides.
Hideaki Nagase;Gregg B. Fields.
Biopolymers (1996)
Self-assembling amphiphiles for construction of protein molecular architecture
Ying-Ching Yu;Peter Berndt;Matthew Tirrell;Gregg B. Fields.
Journal of the American Chemical Society (1996)
Synthetic lipidation of peptides and amino acids: monolayer structure and properties.
Peter Berndt;Gregg B. Fields;Matthew Tirrell.
Journal of the American Chemical Society (1995)
Design and characterization of a fluorogenic substrate selectively hydrolyzed by stromelysin 1 (matrix metalloproteinase-3)
H Nagase;C G Fields;G B Fields.
Journal of Biological Chemistry (1994)
Matrix metalloproteinases and collagen catabolism
Janelle L. Lauer-Fields;Darius Juska;Gregg B. Fields.
Biopolymers (2002)
Regulation of Collagenase Activities of Human Cathepsins by Glycosaminoglycans
Zhenqiang Li;Yoshiyuki Yasuda;Weijie Li;Matthew Bogyo.
Journal of Biological Chemistry (2004)
Journal of Cellular Physiology
(Impact Factor: 6.513)
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