Aggregation and fibril structure of AbetaM01-42 and Abeta1-42
Silvers, R., Colvin, M. T., Frederick, K. K., Jacavone, A. C., Lindquist, S., Linse, S., & Griffin, R. G.
Biochemistry 56, 4850-4859 (2017) PMID28792214

Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in register
Frederick, K. K.*, Michaelis, V. K., Caporini, M. A., Andreas, L. B., Debelouchina, G. T., Griffin, R. G., & Lindquist, S. (* Corresponding Author)
Proc. Natl. Acad. Sci. 144, 3642-3647 (2017) PMID28330994

Sensitivity-enhanced NMR reveals alterations in protein structure by cellular milieus
Frederick, K. K.*, Michaelis, V. K., Corzilius, B., Ong, T. C., Jacavone, A. C., Griffin, R. G.* & Lindquist, S* (* Corresponding Authors)
Cell, 163, 620-628 (2015) PMC4621972

Highlighted in MIT News Analyzing protein structures in their native environments

Highlighted in SpectroscopyNOW Into the fold: Sensitivity-enhanced NMR

Highlighted in Nature Methods (Structural Biology Research Highlight) A. Doerr Structure in the cellular context Nat. Meth. 12, 1112-1113 (2015)

Orientation of aromatic residues in amyloid cores: structural insights into prion diversity
Reymer, A., Frederick, K. K., Rocha, S., Beke-Somfai, T., Kitts, C. C., Lindquist, S. & Nordén, B.
Proc. Natl. Acad. Sci. 111, 17158-17163 (2014) PMC4260602

Distinct prion strains are defined by amyloid core structure and chaperone binding dynamics
Frederick, K. K., Debelouchina, G. T., Kayatekin, C., Dorminy, T*., Jacavone, A. C., Griffin, R. G. & Lindquist, S.  (* Undergraduate author.)
Chemistry & Biology 21, 295-305 (2014) PMC4030713

Highlighted in Chemistry & Biology (Previews) Tuite, Howard & Xue
Dynamic Prions Revealed by Magic. Chem & Biol. 21, 172-173 (2014)

The role of conformational entropy in molecular recognition by calmodulin
Marlow, M. S.*, Dogan, J.*, Frederick, K. K., Valentine, K. G., & Wand, A. J.
Nature Chemical Biology 6, 352-358 (2010) PMC3050676

Highlighted in Nature Chemical Biology (News & Views) Schwalbe & Rinnenthal
Thermodynamics: The world is flat. Nat. Chem. Biol. 6, 312-313 (2010)

Conformational Entropy in Molecular Recognition
Valentine, K. G., Marlow, M. S., Wand, A. J., Frederick, K. K.
International Patent Application No. PCT/US2008/070436.  Published Jan 22, 2009.

Re-evaluation of the model-free analysis of the fast internal motion in proteins using NMR relaxation
Frederick, K. K., Sharp, K. A., Warischalk, N., & Wand, A. J.
J. Phys. Chem. B 112, 12095-103 (2008) PMC2556886

Conformational entropy in molecular recognition by proteins
Frederick, K. K., Marlow, M. S., Valentine, K. G. & Wand, A. J.
Nature 448, 325-329 (2007) PMC4156320

Highlighted in Faculty of 1000http://f1000.com/1088988

Characterization of the backbone and side chain dynamics of the CaM:CaMK1p complex reveals microscopic contributions to protein conformational entropy
Frederick, K. K., Kranz, J. K., & Wand, A. J.
Biochemistry 45, 9841-9848 (2006) PMID16893184

Characterization of the fast dyanmics of protein amino acid side chains using NMR relaxation
Igumenova, T. I., Frederick, K. K., & Wand, A. J.
Chemical Reviews 106, 1672-1699. (2006) [Review] PMC2547146

Arylamide derivatives as peptidomimetic inhibitors of calmodulin
Yin, H., Frederick, K. K., Lui, D., Wand, A. J. & DeGrado, W. F.
Organic Letters 8, 233-225 (2006) PMID16408880

Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase
Frederick, K. K., & Palfey, B. A.
Biochemistry 44, 13304-13314. (2005) PMID16201756

Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-correlated NMR relaxation measurements
Wang, T., Frederick, K. K., Igumenova, T. I., Wand, A. J., & Zuiderweg, E. R. P.
J. Am. Chem. Soc. 127, 828-829 (2005) PMID15656608

Control of adenosylmethionine-dependent radical generation in biotin synthase: a kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB
Ugulava, N. B., Frederick, K. K., & Jarrett, J. T.
Biochemistry 42, 2708-2719 (2003) PMC1540705

Highlighted in Faculty of 1000http://f1000.com/1012528

The role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutant
Palfey, B. A., Basu, R., Frederick, K. K., Entsch, B., & Ballou, D. P.
Biochemistry 41, 8438-8446 (2002) PMID12081493

Protein dynamics control proton transfers to the substrate of the His72Asn mutant of p-hydroxybenzoate hydroxylase
Frederick, K. K., Ballou, D. P., & Palfey, B. A.
Biochemistry 40, 3891-3899 (2001) PMID11300768

SELECTED SYMPOSIA PAPERS

Cyclopropylglycolate, a new substrate and inactivator for long-chain hydroxy-acid oxidase and flavocytochrome b2.
Boubacar, A. K., Frederick, K. K., Miskiniene, V., Ceñas, N. & Lederer, F.
Flavins and Flavoproteins 2005, Nishino, Miura, Tanokura & Fukui eds.
ARchiTect, Inc. Tokyo. 419-423 (2005)

The fast internal dynamics of flavodoxin from Cyanobacterium anabaena using NMR relaxation.
Frederick, K. K., Liu, W., & Wand, A. J.
Flavins and Flavoproteins 2002, Perhman, Chapman & Scrutton editors.
Agency for Scientific Publications, Berlin 551-556 (2002).

Wavin’ flavins and passwords: dynamics and control in the reactions of p-hydroxybenzoate hydroxyls.
Palfey, B. A., Frederick, K. K., Basu, R., Xu, D., Ballou, D. P. & Massey, V.
Flavins and Flavoproteins 1999, Ghisla, Kroneck, Macheroux & Sund. eds.
Agency for Scientific Publications, Berlin 351-358 (1999).

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