C. Fowler

发表

Efficient and precise measurement of Hα–Cα, Cα–C′, Cα–Cβ and HN–N residual dipolar couplings from 2D HN–N correlation spectra

V. Gaponenko, R. Byrd, R. McFeeters, 2005 .

Rapid determination of protein folds using residual dipolar couplings.

J H Prestegard, J. Prestegard, H. Al‐Hashimi, 2000, Journal of molecular biology.

Direct measurement of 1H-1H dipolar couplings in proteins: A complement to traditional NOE measurements

J. Prestegard, F. Tian, E. Zartler, 2000, Journal of biomolecular NMR.

Ubiquitin Regulates Caspase Recruitment Domain-mediated Signaling by Nucleotide-binding Oligomerization Domain-containing Proteins NOD1 and NOD2*

S. Ramaswamy, R. Piper, A. V. Heul, 2013, The Journal of Biological Chemistry.

Structural, Biochemical, and in Vivo Characterization of the First Virally Encoded Cyclophilin from the Mimivirus

E. Eisenmesser, D. Kern, D. Raoult, 2007, Journal of Molecular Biology.

The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains

A. Pardi, M. Sousa, T. A. Walton, 2009, Proceedings of the National Academy of Sciences.

Nuclear magnetic resonance solution structure of the peptidoglycan-binding SPOR domain from Escherichia coli DamX: insights into septal localization.

D. Popham, S. Arends, Kyle B. Williams, 2013, Biochemistry.

Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel NaV1.2.

M. A. Shea, Liping Yu, Dagan C. Marx, 2017, Biophysical chemistry.

Distinct Roles for Conformational Dynamics in Protein-Ligand Interactions.

Liping Yu, Sarah R. Hengel, L. Gakhar, 2016, Structure.

Backbone and side-chain resonance assignments of (Ca2+)4–calmodulin bound to beta calcineurin A CaMBD peptide

M. A. Shea, Liping Yu, S. E. O’Donnell, 2017, Biomolecular NMR Assignments.

Backbone and side-chain resonance assignments of (Ca2+)4–calmodulin bound to beta calcineurin A CaMBD peptide

M. A. Shea, Liping Yu, S. E. O’Donnell, 2017, Biomolecular NMR assignments.

Recognition of β–calcineurin by the domains of calmodulin: Thermodynamic and structural evidence for distinct roles

M. A. Shea, Liping Yu, Susan E. O'Donnell, 2011, Proteins.

ON THE MECHANISM OF THE REACTION OF NINHYDRIN WITH a-AMINO ACIDS

Nathalie, C. Fowler, 2003 .

Identification of FDA-Approved Small Molecules Capable of Disrupting the Calmodulin-Adenylyl Cyclase 8 Interaction through Direct Binding to Calmodulin.

Monica Soto-Velasquez, V. Watts, Val J Watts, 2017, ACS chemical neuroscience.

Supplemental Information Distinct Roles for Conformational Dynamics in Protein-Ligand Interactions

Liping Yu, L. Gakhar, Young Joo Sun, 2016 .

Solution NMR structures of the C‐domain of Tetrahymena cytoskeletal protein Tcb2 reveal distinct calcium‐induced structural rearrangements

H. Sleister, J. Honts, C. Fowler, 2016, Proteins.

Backbone and side-chain chemical shift assignments for the C-terminal domain of Tcb2, a cytoskeletal calcium-binding protein from Tetrahymena thermophila

H. Sleister, J. Honts, C. Fowler, 2016, Biomolecular NMR Assignments.