C. Brouillette

发表

Amphipathic helix motif: Classes and properties

H De Loof, G M Anantharamaiah, G. Anantharamaiah, 1990, Proteins.

Thermodynamic correction of F 508 del-CFTR 1 Ligand binding to a remote site thermodynamically corrects the F 508 del mutation in the human cystic fibrosis transmembrane conductance regulator

J. Riordan, B. Stockwell, N. Dokholyan, 2018 .

Structural stability of purified human CFTR is systematically improved by mutations in nucleotide binding domain 1.

J. Riordan, H. Ding, J. Kappes, 2018, Biochimica et biophysica acta. Biomembranes.

Structural analysis of apolipoprotein A-I: limited proteolysis of methionine-reduced and -oxidized lipid-free and lipid-bound human apo A-I.

T. Shih, L. Roberts, C. Brouillette, 1997, Biochemistry.

Stabilization of a nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator yields insight into disease-causing mutations

J. Riordan, R. Vernon, J. Forman-Kay, 2017, The Journal of Biological Chemistry.

Tethered dimers as NAD synthetase inhibitors with antibacterial activity.

L. DeLucas, C. Luan, S. Velu, 2003, Journal of medicinal chemistry.

Lipolytic surface remnants of triglyceride-rich lipoproteins are cytotoxic to macrophages but not in the presence of high density lipoprotein. A possible mechanism of atherogenesis?

J. Segrest, B. Chung, C. Brouillette, 1989, The Journal of clinical investigation.

Human apolipoprotein A-I: structure determination and analysis of unusual diffraction characteristics.

J. Engler, D. Borhani, C. Brouillette, 1999, Acta crystallographica. Section D, Biological crystallography.

Role of amphipathic helixes in HDL structure/function.

J. Engler, G. Anantharamaiah, J. Segrest, 1991, Advances in experimental medicine and biology.

Structural domains of vesicular stomatitis virus. A study by differential scanning calorimetry, thermal gel analysis, and thermal electron microscopy.

R. Compans, J. Segrest, J. Brandts, 1982, The Journal of biological chemistry.

Characterization of apoA-I-containing lipoprotein subpopulations secreted by HepG2 cells.

C. Bisgaier, M. Cheung, C. Brouillette, 1989, Journal of lipid research.

Storage stability of the solution formulation of sCD4 determined by DSC in comparison with two functional assays

I. Chaiken, D. Myszka, C. Brouillette, 1996 .

CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I

J. Engler, D. Borhani, C. Brouillette, 1998 .

tools for STRUCTUR AL GENOMICS accelerating the structure pipeline

C. Brouillette, S. Mylvaganam, Dr Kal Ramnarayan, 2004 .

Characterization of high density lipoprotein subspecies: structural studies by single vertical spin ultracentrifugation and immunoaffinity chromatography.

G. Anantharamaiah, J. Segrest, J. Albers, 1987, Journal of lipid research.

C h a racte r i zat i o n of a poA- I -co n ta i n i n g I i pop rote i n subpopulations secreted by HepG2 cells

M. Cheung, C. Brouillette, K. Lum, 1989 .

The lipid-free structure of apolipoprotein A-I: effects of amino-terminal deletions.

J. Engler, G. Anantharamaiah, L. Roberts, 1998, Biochemistry.

Studies of synthetic peptide analogs of the amphipathic helix. Competitive displacement of exchangeable apolipoproteins from native lipoproteins.

J. Segrest, B. Chung, C. Brouillette, 1983, The Journal of biological chemistry.

SAR studies for a new class of antibacterial NAD biosynthesis inhibitors.

C. Brouillette, Qingxiang Zhou, W. Brouillette, 2009, Journal of combinatorial chemistry.

Antibacterial nicotinamide adenine dinucleotide synthetase inhibitors: amide- and ether-linked tethered dimers with alpha-amino acid end groups.

L. DeLucas, C. Luan, S. Velu, 2007, Journal of medicinal chemistry.

Studies of synthetic peptide analogs of the amphipathic helix. Correlation of structure with function.

J. Segrest, T. Nishida, B. Chung, 1985, The Journal of biological chemistry.

The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function.

G. Anantharamaiah, J. Segrest, Martin K. Jones, 1992, Journal of lipid research.

His-tag impact on structure.

L. DeLucas, M. Carson, C. Brouillette, 2007, Acta crystallographica. Section D, Biological crystallography.

Studies of synthetic peptide analogs of the amphipathic helix. Structure of complexes with dimyristoyl phosphatidylcholine.

C. Schmidt, T. A. Hughes, G. Anantharamaiah, 1985, The Journal of biological chemistry.

Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis.

L. DeLucas, P. Pruett, Craig D. Smith, 2008, Acta crystallographica. Section F, Structural biology and crystallization communications.

Tethered dimer inhibitors of NAD synthetase: parallel synthesis of an aryl-substituted SAR library.

L. DeLucas, C. Luan, S. Velu, 2005, Journal of combinatorial chemistry.

Stereoselective binding of an enantiomeric pair of stromelysin-1 inhibitors caused by conformational entropy factors.

E. Lunney, D. Ortwine, P. McConnell, 2000, Bioorganic & medicinal chemistry letters.

Minimal size phosphatidylcholine vesicles: effects of radius of curvature on head group packing and conformation.

J. Segrest, C G Brouillette, J P Segrest, 1982, Biochemistry.

Structure and thermal stability of monomeric bacteriorhodopsin in mixed pospholipid/detergent micelles

H. Khorana, L. Stern, C. Brouillette, 1989, Proteins.

A Gene Optimization Strategy that Enhances Production of Fully Functional P-Glycoprotein in Pichia pastoris

G. Chang, A. Ward, Brigitte Gasser, 2011, PloS one.

Membrane protein stability can be compromised by detergent interactions with the extramembranous soluble domains

J. Riordan, L. DeLucas, J. Kappes, 2014, Protein science : a publication of the Protein Society.

pH dependence of bacteriorhodopsin thermal unfolding.

C. Brouillette, D. Muccio, T. K. Finney, 1987, Biochemistry.

Analysis of the two-state behavior of the thermal unfolding serum retinol binding protein containing a single retinol ligand.

C. Brouillette, F. Fish, D. Muccio, 1992, Biochemistry.

Structural models of human apolipoprotein A-I: a critical analysis and review.

J. Engler, G. Anantharamaiah, D. Borhani, 2001, Biochimica et biophysica acta.

Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis.

L. DeLucas, P. Pruett, C. Brouillette, 2007, Acta crystallographica. Section D, Biological crystallography.

The amphipathic alpha helix: a multifunctional structural motif in plasma apolipoproteins.

S. Harvey, G. Anantharamaiah, J. Segrest, 1994, Advances in protein chemistry.

Ligand binding to a remote site thermodynamically corrects the F508del mutation in the human cystic fibrosis transmembrane conductance regulator

J. Riordan, B. Stockwell, N. Dokholyan, 2018, The Journal of Biological Chemistry.

Interactions and cooperativity between P-glycoprotein structural domains determined by thermal unfolding provides insights into its solution structure and function.

I. Urbatsch, C. Brouillette, Zhengrong Yang, 2017, Biochimica et biophysica acta. Biomembranes.

Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation.

J. Engler, D. Borhani, J A Engler, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Intracellular transport and virion incorporation of vpx requires interaction with other virus type-specific components.

J. Kappes, G. Shaw, B. Hahn, 1993, Virology.

Direct Binding of the Corrector VX-809 to Human CFTR NBD1: Evidence of an Allosteric Coupling between the Binding Site and the NBD1:CL4 Interface

Zhengrong Yang, Julie D Forman-Kay, J. Forman-Kay, 2017, Molecular Pharmacology.

Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant.

John F Hunt, Diana Wetmore, Spencer Emtage, 2010, Protein engineering, design & selection : PEDS.

Down-regulation of cell surface receptors is modulated by polar residues within the transmembrane domain.

L. Zaliauskiene, J. Lebowitz, J. Collawn, 2000, Molecular biology of the cell.

Crystallization of truncated human apolipoprotein A-I in a novel conformation.

J. Engler, D. Borhani, C. Brouillette, 1999, Acta crystallographica. Section D, Biological crystallography.

Structural models of human apolipoprotein A-I.

G. Anantharamaiah, C. Brouillette, Christie G. Brouillette, 1995, Biochimica et biophysica acta.

Förster resonance energy transfer measurements are consistent with a helical bundle model for lipid-free apolipoprotein A-I.

J. Engler, W. Dong, C. Brouillette, 2005, Biochemistry.

Thermal stabilities of mutant Escherichia coli tryptophan synthase α subunits

W. Lim, C. Brouillette, J. K. Hardman, 1992 .

NH3-dependent NAD+ synthetase from Bacillus subtilis at 1 A resolution.

K. Moore, L. DeLucas, J. Symerský, 2002, Acta crystallographica. Section D, Biological crystallography.

Deletion of DnaK's lid strengthens binding to the nucleotide exchange factor, GrpE: a kinetic and thermodynamic analysis.

Michael G. Sehorn, C. Brouillette, S. N. Witt, 2003, Biochemistry.

A Guide to Differential Scanning Calorimetry of Membrane and Soluble Proteins in Detergents.

C. Brouillette, Zhengrong Yang, 2016, Methods in enzymology.

Kinetic and calorimetric evidence for two distinct scaffolding protein binding populations within the bacteriophage P22 procapsid.

P. Prevelige, C. Brouillette, M. Parker, 2001, Biochemistry.

Use of synthetic peptide analogues to localize lecithin:cholesterol acyltransferase activating domain in apolipoprotein A-I.

G. Anantharamaiah, J. Segrest, C. Brouillette, 1990, Arteriosclerosis.

Structural studies of apolipoprotein A-I/phosphatidylcholine recombinants by high-field proton NMR, nondenaturing gradient gel electrophoresis, and electron microscopy.

J. Segrest, B. Chung, C. Brouillette, 1984, Biochemistry.

Truncation of the amino terminus of human apolipoprotein A-I substantially alters only the lipid-free conformation.

J. Engler, G. Anantharamaiah, L. Roberts, 1997, Biochemistry.

Analysis of the binding of hydroxamic acid and carboxylic acid inhibitors to the stromelysin-1 (matrix metalloproteinase-3) catalytic domain by isothermal titration calorimetry.

C. Humblet, E. Lunney, A. Pavlovsky, 1999, Biochemistry.

Virtual screening to identify lead inhibitors for bacterial NAD synthetase (NADs).

Zhengrong Yang, C. Brouillette, W. Brouillette, 2009, Bioorganic & medicinal chemistry letters.

Restoration of NBD1 thermal stability is necessary and sufficient to correct ∆F508 CFTR folding and assembly.

Zhengrong Yang, Lihua He, J. Riordan, 2015, Journal of molecular biology.

Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis

Zhengrong Yang, Shane Atwell, Chi Wang, 2010, Protein science : a publication of the Protein Society.

Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide‐binding domain 1

Zhengrong Yang, John F Hunt, Diana Wetmore, 2010, Protein science : a publication of the Protein Society.

Conformational Changes Relevant to Channel Activity and Folding within the first Nucleotide Binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator*

Hanoch Senderowitz, Julie D. Forman-Kay, Efrat Noy, 2012, The Journal of Biological Chemistry.

Mechanism of dual pharmacological correction and potentiation of human CFTR

J. Kappes, R. Grassucci, G. Lukács, 2022, bioRxiv.

Interdomain communication of T-cell CD4 studied by absorbance and fluorescence difference spectroscopy measurements of urea-induced unfolding.

I. Chaiken, D. Myszka, R. Sweet, 1995, Biochemistry.

Structural domains in vesicular stomatitis virus membrane as studied by differential scanning calorimetry.

R. Compans, J. Segrest, J. Brandts, 1982, Biophysical journal.

Dimethyl sulfoxide at 2.5% (v/v) alters the structural cooperativity and unfolding mechanism of dimeric bacterial NAD+ synthetase

L. DeLucas, C. Brouillette, W. Brouillette, 2004, Protein science : a publication of the Protein Society.

Kinetic and structural analysis of mutant CD4 receptors that are defective in HIV gp120 binding.

W. Hendrickson, I. Chaiken, D. Myszka, 1996, Proceedings of the National Academy of Sciences of the United States of America.

The Structure of Human Lipoprotein A-I

P. Axelsen, J. Engler, V. Koppaka, 1999, The Journal of Biological Chemistry.

Structural analysis of apolipoprotein A-I: effects of amino- and carboxy-terminal deletions on the lipid-free structure.

J. Engler, L. Roberts, C. Brouillette, 1998, Biochemistry.

Novel laser breakdown spectrometer for environmental monitoring

Yurii V. Orlovskii, Lawrence J. DeLucas, Ivan N. Vorob'ev, 1999, Optics East.

Stabilization of active-site loops in NH3-dependent NAD+ synthetase from Bacillus subtilis.

L. DeLucas, J. Symerský, D. Chattopadhyay, 2001, Acta crystallographica. Section D, Biological crystallography.

Restoration of NBD1 thermal stability is necessary and sufficient to correct ∆F508 CFTR folding and assembly.

J. Riordan, A. Aleksandrov, Lihua He, 2015, Journal of molecular biology.

Direct Binding of the Corrector VX-809 to Human CFTR NBD1: Evidence of an Allosteric Coupling between the Binding Site and the NBD1:CL4 Interface

J. Forman-Kay, P. A. Chong, P. Thomas, 2017, Molecular Pharmacology.