C. McKnight

发表

Ligand-induced conformational changes allosterically activate Toll-like receptor 9

B. Monks, D. Golenbock, E. Latz, 2007, Nature Immunology.

R. Sauer, C. McKnight, M. Cordes, 1999, Science.

An evolutionary bridge to a new protein fold

Robert T. Sauer, R. Sauer, C. McKnight, 2000, Nature Structural Biology.

Combined Molecular Dynamics Simulations and Experimental Studies of the Structure and Dynamics of Poly-Amido-Saccharides.

J. Straub, M. Grinstaff, C. McKnight, 2016, Journal of the American Chemical Society.

Limited proteolysis and biophysical characterization of the lipovitellin homology region in apolipoprotein B.

C. McKnight, Z. Jiang, M. Carraway, 2005, Biochemistry.

Synthesis of Altrose Poly-amido-saccharides with β-N-(1→2)-d-amide Linkages: A Right-Handed Helical Conformation Engineered in at the Monomer Level.

M. Grinstaff, C. McKnight, Eric L Dane, 2017, Journal of the American Chemical Society.

The unusual internal motion of the villin headpiece subdomain

A. Wand, Kyle W. Harpole, C. McKnight, 2016, Protein science : a publication of the Protein Society.

IcmQ in the Type 4b secretion system contains a novel NAD + binding domain

C. Akey, J. Gumbart, I. V. Akey, 2013 .

Characterization of the MUC1-C Cytoplasmic Domain as a Cancer Target

D. Kufe, S. Kharbanda, D. Raina, 2015, PloS one.

Surface Tensiometry of Apolipoprotein B Domains at Lipid Interfaces Suggests a New Model for the Initial Steps in Triglyceride-rich Lipoprotein Assembly*

Jeffrey W. Brown, C. McKnight, D. Small, 2014, The Journal of Biological Chemistry.

Interfacial properties of apolipoprotein B292-593 (B6.4-13) and B611-782 (B13-17). Insights into the structure of the lipovitellin homology region in apolipoprotein B.

C. McKnight, D. Small, Z. Jiang, 2010, Biochemistry.

Identifying Competitive Protein Antagonists for F-Actin with Reverse-Phase HPLC

Jeffrey W. Brown, C. McKnight, 2010 .

High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity.

C. McKnight, Yeming Wang, J. Head, 2005, Biochemistry.

Gelsolin-like activation of villin: calcium sensitivity of the long helix in domain 6.

Fengli Zhang, Alshakim Nelson, C. McKnight, 2013, Biochemistry.

On the unyielding hydrophobic core of villin headpiece

Jeffrey W. Brown, C. McKnight, J. Farelli, 2012, Protein science : a publication of the Protein Society.

Competition between intradomain and interdomain interactions: a buried salt bridge is essential for villin headpiece folding and actin binding.

D. Raleigh, C. McKnight, B. Song, 2011, Biochemistry.

Identifying competitive protein antagonists for F-actin with reverse-phase high-performance liquid chromatography.

Jeffrey W. Brown, C. McKnight, 2010, Analytical biochemistry.

How to arm a supervillin: designing F-actin binding activity into supervillin headpiece.

Jeffrey W. Brown, C. McKnight, Didem Vardar-Ulu, 2009, Journal of molecular biology.

Heterogeneity and dynamics in villin headpiece crystal structures.

C. McKnight, J. Meng, 2009, Acta crystallographica. Section D, Biological crystallography.

Dematin exhibits a natively unfolded core domain and an independently folded headpiece domain

A. Chishti, Anwara . Khan, C. McKnight, 2009, Protein science : a publication of the Protein Society.

Phosphorylation-induced changes in backbone dynamics of the dematin headpiece C-terminal domain

C. McKnight, L. Vugmeyster, 2009, Journal of biomolecular NMR.

The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence.

D. Hoyt, N. Isern, C. McKnight, 2007, Biochemistry.

Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: contribution of His41 to the pH-dependent stability of the N-terminal subdomain.

D. Raleigh, A. Palmer, E. Alexov, 2006, Journal of molecular biology.

Zinc and copper bind to unique sites of histatin 5

C. McKnight, J. Grogan, F. Oppenheim, 2001, FEBS letters.

Biophysical studies of signal peptides: Implications for signal sequence functions and the involvement of lipid in protein export

Jeffrey D. Jones, L. Gierasch, C. McKnight, 1990, Journal of bioenergetics and biomembranes.

Conformations and orientations of a signal peptide interacting with phospholipid monolayers.

L. Gierasch, C. McKnight, R. Dluhy, 1989, Biochemistry.

Minimum length of a sequence-specific DNA binding peptide.

P. S. Kim, R. Rutkowski, C. McKnight, 1992, Biochemistry.

Sequence-specific DNA binding by a short peptide dimer.

P. S. Kim, C. McKnight, McKnight Cj, 1990, Science.

NMR structure of the 35-residue villin headpiece subdomain

Paul T. Matsudaira, P. S. Kim, P. Matsudaira, 1997, Nature Structural Biology.

Molecular Model of the Microvillar Cytoskeleton and Organization of the Brush Border

Jeffrey W. Brown, C. McKnight, James McKnight, 2010, PloS one.

The Physiological Molecular Shape of Spectrin: A Compact Supercoil Resembling a Chinese Finger Trap

Esther Bullitt, Jeffrey W. Brown, Sira Sriswasdi, 2015, PLoS Comput. Biol..

Missense Mutations in APOB within the βα1 Domain of Human APOB-100 Result in Impaired Secretion of ApoB and ApoB-containing Lipoproteins in Familial Hypobetalipoproteinemia*

R. Hegele, D. Vance, R. McLeod, 2007, Journal of Biological Chemistry.

A Novel Nontruncating APOB Gene Mutation, R463W, Causes Familial Hypobetalipoproteinemia*

B. Miskie, R. Hegele, Jing Shan, 2003, The Journal of Biological Chemistry.

Beat Vögeli, D. Ostrovsky, C. McKnight, 2018, Journal of Biomolecular NMR.

On unsatisfied hydrogen bonds in the N-terminal subdomain of villin headpiece.

Jeffrey W. Brown, C. McKnight, J. Farelli, 2011, Journal of molecular biology.

Corrigendum: Ligand-induced conformational changes allosterically activate Toll-like receptor 9

B. Monks, D. Golenbock, E. Latz, 2007, Nature Immunology.

Optimized purification of a fusion protein by reversed-phase high performance liquid chromatography informed by the linear solvent strength model.

C. Mant, R. Hodges, C. McKnight, 2017, Journal of chromatography. A.

Novel missense MTTP gene mutations causing abetalipoproteinemia.

C. McKnight, F. V. van Bockxmeer, J. Burnett, 2014, Biochimica et biophysica acta.

A novel missense HGD gene mutation, K57N, in a patient with alkaptonuria.

Jeffrey W. Brown, C. McKnight, J. Burnett, 2009, Clinica chimica acta; international journal of clinical chemistry.

Structural analysis of reconstituted lipoproteins containing the N-terminal domain of apolipoprotein B.

J. Wall, C. McKnight, M. Simon, 2007, Biophysical journal.

Slow methyl axes motions in perdeuterated villin headpiece subdomain probed by cross-correlated NMR relaxation measurements.

Beat Vögeli, D. Ostrovsky, C. McKnight, 2023, Magnetochemistry.

Deuteration of nonexchangeable protons on proteins affects their thermal stability, side‐chain dynamics, and hydrophobicity

C. Mant, R. Hodges, Beat Vögeli, 2020, Protein science : a publication of the Protein Society.

Slow motions in chicken villin headpiece subdomain probed by cross-correlated NMR relaxation of amide NH bonds in successive residues.

C. McKnight, L. Vugmeyster, 2008, Biophysical journal.

Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein.

D. Raleigh, A. Palmer, C. McKnight, 2002, Journal of molecular biology.

Characterization of circulating microparticle-associated CD39 family ecto-nucleotidases in human plasma

S. Robson, E. Csizmadia, C. McKnight, 2014, Purinergic Signalling.

A phosphorylation-induced conformation change in dematin headpiece.

C. McKnight, Z. Jiang, 2006, Structure.

NMR structure of an F-actin-binding "headpiece" motif from villin.

C. McKnight, D. Buckley, D. Vardar, 1999, Journal of molecular biology.

A thermostable 35-residue subdomain within villin headpiece.

P S Kim, P. S. Kim, P. Matsudaira, 1996, Journal of molecular biology.

The Differential Impact of Disulfide Bonds and N-Linked Glycosylation on the Stability and Function of CD14*

D. Golenbock, C. McKnight, P. Parroche, 2008, Journal of Biological Chemistry.

Reconstituting initial events during the assembly of apolipoprotein B-containing lipoproteins in a cell-free system.

C. McKnight, Yuhang Liu, D. Atkinson, 2008, Journal of molecular biology.

The N-terminal 17% of apoB binds tightly and irreversibly to emulsions modeling nascent very low density lipoproteins.

D. Gantz, C. McKnight, D. Small, 2001, Journal of lipid research.

The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain

C James McKnight, C. McKnight, D. Buckley, 2002, Protein science : a publication of the Protein Society.

Defining lipid-interacting domains in the N-terminal region of apolipoprotein B.

D. Gantz, C. McKnight, E. Bullitt, 2006, Biochemistry.

The NMR Structure of Dematin Headpiece Reveals a Dynamic Loop That Is Conformationally Altered upon Phosphorylation at a Distal Site*

A. Chishti, C. McKnight, D. Vardar, 2004, Journal of Biological Chemistry.

The Allosteric Mechanism Induced by Protein Kinase A (PKA) Phosphorylation of Dematin (Band 4.9)*

Jeffrey W. Brown, C. McKnight, D. Hatters, 2013, The Journal of Biological Chemistry.

Villin-type headpiece domains show a wide range of F-actin-binding affinities.

A. Noegel, M. Schleicher, A. Chishti, 2002, Cell motility and the cytoskeleton.

Helix formation and stability in a signal sequence.

L. Gierasch, C. McKnight, L M Gierasch, 1989, Biochemistry.

Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.

Yuefeng Tang, C James McKnight, D. Raleigh, 2003, Journal of the American Chemical Society.

Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties.

L. Gierasch, C. McKnight, M. S. Briggs, 1989, The Journal of biological chemistry.

IcmQ in the Type 4b secretion system contains an NAD+ binding domain.

C. Akey, J. Gumbart, I. V. Akey, 2013, Structure.

Beat Vögeli, D. Ostrovsky, C. McKnight, 2018, Journal of biomolecular NMR.

Solution Structure of Switch Arc, a Mutant with 310 Helices Replacing a Wild-type β-Ribbon

R. Sauer, C. McKnight, M. Cordes, 2003 .

Solution structure of switch Arc, a mutant with 3(10) helices replacing a wild-type beta-ribbon.

R. Sauer, C. McKnight, M. Cordes, 2003, Journal of molecular biology.

Networking at the Protein Society Symposium

C James McKnight, Matthew H J Cordes, C. McKnight, 2005, Nature chemical biology.