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Gregg B. Fields

Researcher at Florida Atlantic University

Publications -  278
Citations -  16155

Gregg B. Fields is an academic researcher from Florida Atlantic University. The author has contributed to research in topics: Matrix metalloproteinase & Peptide. The author has an hindex of 63, co-authored 264 publications receiving 15092 citations. Previous affiliations of Gregg B. Fields include Imperial College London & Auburn University.

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Solid phase peptide synthesis utilizing 9‐fluorenylmethoxycarbonyl amino acids

TL;DR: The great variety of conditions under which Fmoc solid phase peptide synthesis may be carried out represents a truly "orthogonal" scheme, and thus offers many unique opportunities for bioorganic chemistry.
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Synthetic matrix metalloproteinase-sensitive hydrogels for the conduction of tissue regeneration: Engineering cell-invasion characteristics

TL;DR: Gels used to deliver recombinant human bone morphogenetic protein-2 to the site of critical defects in rat cranium were completely infiltrated by cells and remodeled into bony tissue within 4 wk at a dose of 5 μg per defect.
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A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis.

TL;DR: Synthesis and cleavage of 10 peptides demonstrated the complementarity of Fmoc chemistry with Reagent K for efficient synthesis of complex peptides and assessed the relative effectiveness of various scavengers in suppressing side reactions.
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Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis

TL;DR: It is reported that collagenases bind and locally unwind the triple‐helical structure before hydrolyzing the peptide bonds and shows that MMP‐1 preferentially interacts with the α2(I) chain of type I collagen and cleaves the three α chains in succession.
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Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides.

TL;DR: A variety of sequence specificity studies have been performed using collagen sequence-based peptides and MMP family members, demonstrating that these peptides may not be very good models of native MMP substrates, and that the additivity principle is not always applicable for designing synthetic M MP substrates.