F. Moy

发表

Resistance to receptor-mediated degradation of a murine epidermal growth factor analogue (EGF-Val-47) potentiates its mitogenic activity.

H. Scheraga, A. Burgess, F. Walker, 1990, Biochemistry.

Application of frequency-shifted shaped pulses for overcoming solvent-saturation transfer and preirradiation-associated spin-diffusion effects in aqueous solutions of peptides and proteins

H. Scheraga, G. Montelione, F. Moy, 1992 .

Structure-based design of a novel, potent, and selective inhibitor for MMP-13 utilizing NMR spectroscopy and computer-aided molecular design

Robert Powers, Ramaswamy Nilakantan, R. Powers, 2000 .

Solution structure of human IL-13 and implication for receptor binding.

R. Powers, F. Moy, E. Diblasio, 2001, Journal of molecular biology.

Lead identification to generate 3-cyanoquinoline inhibitors of insulin-like growth factor receptor (IGF-1R) for potential use in cancer treatment.

D. Boschelli, F. Moy, D. Berger, 2008, Bioorganic & medicinal chemistry letters.

Lead identification to generate isoquinolinedione inhibitors of insulin-like growth factor receptor (IGF-1R) for potential use in cancer treatment.

F. Moy, G. Krishnamurthy, L. Di, 2008, Bioorganic & medicinal chemistry letters.

Erratum: Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor (Biochemistry (April 22, 1997) 36:16 (4782-4791))

R. Powers, D. Kitchen, P. Bohlen, 1997 .

Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor.

R. Powers, D. Kitchen, F. Moy, 1997, Biochemistry.

R. Powers, F. Moy, S. Ferrone, 2000, The Journal of Immunology.

qNMR for profiling the production of fungal secondary metabolites

F. Moy, H. Raja, C. Pearce, 2017, Magnetic resonance in chemistry : MRC.

The discovery of anthranilic acid-based MMP inhibitors. Part 1: SAR of the 3-position.

R. Powers, F. Moy, J. Skotnicki, 2001, Bioorganic & medicinal chemistry letters.

Letter to the Editor: 1H, 13C and 15N resonance assignments of human RGSZ1

F. Moy, S. Sukits, W. Hum, 2004, Journal of biomolecular NMR.

Novel synthesis and structural characterization of a high-affinity paramagnetic kinase probe for the identification of non-ATP site binders by nuclear magnetic resonance.

Annette Sievers, Désirée H H Tsao, L. Mosyak, 2010, Journal of medicinal chemistry.

Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints.

H. Scheraga, G. Montelione, Y. Li, 1993, Biochemistry.

Structure-function studies of murine epidermal growth factor: expression and site-directed mutagenesis of epidermal growth factor gene.

H. Scheraga, G. Montelione, F. Moy, 1988, Biochemistry.

Assignments, secondary structure and dynamics of the inhibitor-free catalytic fragment of human fibroblast collagenase

R. Powers, P. Chanda, F. Moy, 1997, Journal of biomolecular NMR.

Chemical Diversity of Metabolites from Fungi, Cyanobacteria, and Plants Relative to FDA-Approved Anticancer Agents.

A. Kinghorn, F. Moy, D. Jarjoura, 2012, ACS medicinal chemistry letters.

Signal transduction in chemotaxis. A propagating conformation change upon phosphorylation of CheY.

F. Dahlquist, P. Domaille, P. Matsumura, 1994, The Journal of biological chemistry.

Analysis by NMR Spectroscopy of the Structural Homology between the Linear and the Cyclic Peptide Recognized by Anti-human Leukocyte Antigen Class I Monoclonal Antibody TP25.99*210

R. Powers, F. Moy, S. Ferrone, 2000, The Journal of Biological Chemistry.

Structural Basis for the Immunogenic Properties of the Meningococcal Vaccine Candidate LP2086*

F. Moy, S. Hoiseth, Jaison Jacob, 2009, Journal of Biological Chemistry.

NMR dynamics and antibody recognition of the meningococcal lipidated outer membrane protein LP2086 in micellar solution.

F. Moy, S. Hoiseth, E. Murphy, 2010, Biochimica et biophysica acta.

3,4-Dihydropyrimido(1,2-a)indol-10(2H)-ones as potent non-peptidic inhibitors of caspase-3.

B. Harrison, A. Robichaud, L. Mosyak, 2009, Bioorganic & medicinal chemistry.

NMR solution structure of the catalytic fragment of human fibroblast collagenase complexed with a sulfonamide derivative of a hydroxamic acid compound.

R. Powers, P. Chanda, F. Moy, 1999, Biochemistry.

The nuclear hormone receptor farnesoid X receptor (FXR) is activated by androsterone.

F. Moy, M. Evans, Shuguang Wang, 2006, Endocrinology.

Homology model for oncostatin M based on NMR structural data.

R. Powers, D. Kitchen, F. Moy, 1998, Biochemistry.

Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy.

F. Dahlquist, P. Domaille, P. Matsumura, 1994, Biochemistry.

Resonance assignments for Oncostatin M, a 24-kDa α-helical protein

R. Powers, B. Castner, C. March, 1996 .

Resonance assignments for Oncostatin M, a 24-kDa alpha-helical protein.

R. Powers, B. Castner, C. March, 1996, Journal of Biomolecular NMR.

1H, 15N, 13C and 13CO assignments and secondary structure determination of basic fibroblast growth factor using 3D heteronuclear NMR spectroscopy

E. Campbell, R. Powers, F. Moy, 1995, Journal of biomolecular NMR.

Solution structure of ZipA, a crucial component of Escherichia coli cell division.

R. Powers, L. Mosyak, F. Moy, 2000, Biochemistry.

High-resolution solution structure of the catalytic fragment of human collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor.

R. Powers, P. Chanda, F. Moy, 2000, Journal of molecular biology.

MS/NMR: a structure-based approach for discovering protein ligands and for drug design by coupling size exclusion chromatography, mass spectrometry, and nuclear magnetic resonance spectroscopy.

R. Powers, K. Haraki, F. Moy, 2001, Analytical chemistry.

Letter to the Editor: 1H, 15N, 13C, and 13CO assignments and secondary structure determination of collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor

R. Powers, P. Chanda, F. Moy, 2000, Journal of biomolecular NMR.

High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR.

R. Powers, P. Chanda, F. Moy, 1998, Biochemistry.

Letter to the Editor: 1H, 15N, 13C, and 13CO assignments and secondary structure determination of RGS4*

R. Powers, P. Chanda, F. Moy, 1999, Journal of biomolecular NMR.

Conformational characterization of a single-site mutant of murine epidermal growth factor (EGF) by 1H NMR provides evidence that leucine-47 is involved in the interactions with the EGF receptor.

H. Scheraga, G. Montelione, F. Moy, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Impact of mobility on structure-based drug design for the MMPs.

R. Powers, T. Rush, P. Chanda, 2002, Journal of the American Chemical Society.

Design and syntheses of 1,6-naphthalene derivatives as selective HCMV protease inhibitors.

F. Moy, A. Gopalsamy, Kitae Lim, 2004, Journal of medicinal chemistry.

NMR structure of free RGS4 reveals an induced conformational change upon binding Galpha.

F. Moy, Mark I. Cockett, Pranab K. Chanda, 2000, Biochemistry.