J. Louis

发表

Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping.

A. Gronenborn, C. Bewley, K. Gustafson, 1999, Journal of molecular biology.

Structural basis for SRY-dependent 46-X,Y sex reversal: modulation of DNA bending by a naturally occurring point mutation.

G M Clore, V. Zhurkin, G. Clore, 2001, Journal of molecular biology.

Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding

A. Bax, J. Louis, R. Ghirlando, 2015, Journal of biomolecular NMR.

The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface

Ad Bax, A. Bax, J. Louis, 2010, Proceedings of the National Academy of Sciences.

HIV-1 protease with 20 mutations exhibits extreme resistance to clinical inhibitors through coordinated structural rearrangements.

J. Louis, I. Weber, Chen-Hsiang Shen, 2012, Biochemistry.

Structural Studies of a Rationally Selected Multi-Drug Resistant HIV-1 Protease Reveal Synergistic Effect of Distal Mutations on Flap Dynamics

J. Louis, I. Weber, R. Harrison, 2016, PloS one.

Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function.

J. Louis, D. Torchia, R. Ishima, 1999, Structure.

Structural and kinetic analysis of drug resistant mutants of HIV-1 protease.

J. Louis, I. Weber, R. Harrison, 2000, European journal of biochemistry.

Folded Monomer of HIV-1 Protease*

A. Gronenborn, J. Louis, D. Torchia, 2001, The Journal of Biological Chemistry.

Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations

W. Eaton, J. Louis, R. Best, 2007, Proceedings of the National Academy of Sciences.

Co-Evolutionary Fitness Landscapes for Sequence Design.

Robert B Best, Pengfei Tian, Annie Aniana, 2018, Angewandte Chemie.

Solution Structure of the Mature HIV-1 Protease Monomer

Angela M Gronenborn, Rieko Ishima, A. Gronenborn, 2003, Journal of Biological Chemistry.

Structural implications of drug‐resistant mutants of HIV‐1 protease: High‐resolution crystal structures of the mutant protease/substrate analogue complexes

J. Louis, I. Weber, R. Harrison, 2001, Proteins.

The point mutation A34F causes dimerization of GB1

Angela M Gronenborn, A. Gronenborn, J. Louis, 2007, Proteins.

A captured folding intermediate involved in dimerization and domain-swapping of GB1.

Angela M Gronenborn, A. Gronenborn, J. Louis, 2004, Journal of molecular biology.

A protein contortionist: core mutations of GB1 that induce dimerization and domain swapping.

Angela M Gronenborn, A. Gronenborn, J. Louis, 2003, Journal of molecular biology.

The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures.

Alexander Wlodawer, Angela M Gronenborn, Barry R O'Keefe, 2002, Structure.

Solution NMR Structure of the Barrier-to-Autointegration Factor-Emerin Complex*

G. Clore, J. Louis, R. Ghirlando, 2007, Journal of Biological Chemistry.

Solution structure of the MEF2A–DNA complex: structural basis for the modulation of DNA bending and specificity by MADS‐box transcription factors

G M Clore, G. Clore, J. Louis, 2000, The EMBO journal.

Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIAGlucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system

G M Clore, G. Clore, J. Louis, 2000, The EMBO journal.

Pressure‐induced structural transition of mature HIV‐1 protease from a combined NMR/MD simulation approach

Ad Bax, Julien Roche, A. Bax, 2015, Proteins.

Mutations Proximal to Sites of Autoproteolysis and the α-Helix That Co-evolve under Drug Pressure Modulate the Autoprocessing and Vitality of HIV-1 Protease.

G. Clore, J. Louis, L. Deshmukh, 2015, Biochemistry.

Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease.

J. Louis, D. Davies, F. Dyda, 1998, Biochemistry.

Mutational and Structural Studies Aimed at Characterizing the Monomer of HIV-1 Protease and Its Precursor*

J. Louis, D. Torchia, R. Ishima, 2007, Journal of Biological Chemistry.

A Monoclonal Fab Derived from a Human Nonimmune Phage Library Reveals a New Epitope on gp41 and Neutralizes Diverse Human Immunodeficiency Virus Type 1 Strains

C. Bewley, G. Clore, J. Louis, 2007, Journal of Virology.

Modulation of the monomer-dimer equilibrium and catalytic activity of SARS-CoV-2 main protease by a transition-state analog inhibitor

J. Louis, R. Ghirlando, Annie Aniana, 2022, Communications Biology.

Interactions of different inhibitors with active‐site aspartyl residues of HIV‐1 protease and possible relevance to pepsin

J. Louis, J. M. Sayer, 2009, Proteins.

Preparation of Uniformly Isotope-labeled DNA Oligonucleotides for NMR Spectroscopy*

A. Gronenborn, G. Clore, J. Louis, 1998, The Journal of Biological Chemistry.

The L76V drug resistance mutation decreases the dimer stability and rate of autoprocessing of HIV-1 protease by reducing internal hydrophobic contacts.

J. Louis, I. Weber, R. Harrison, 2011, Biochemistry.

Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET

Kevin J. McHale, J. Louis, Jae-Yeol Kim, 2017, Proceedings of the National Academy of Sciences.

Binding of HIV-1 gp41-Directed Neutralizing and Non-Neutralizing Fragment Antibody Binding Domain (Fab) and Single Chain Variable Fragment (ScFv) Antibodies to the Ectodomain of gp41 in the Pre-Hairpin and Six-Helix Bundle Conformations

C. Bewley, G. Clore, J. Louis, 2014, PloS one.

Importance of time-ordered non-uniform sampling of multi-dimensional NMR spectra of Aβ1–42 peptide under aggregating conditions

A. Bax, J. Louis, Jinfa Ying, 2019, Journal of Biomolecular NMR.

Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1alpha.

G. Clore, J. Louis, M. Caffrey, 2005, Journal of molecular biology.

Characterization and HIV-1 fusion inhibitory properties of monoclonal Fabs obtained from a human non-immune phage library selected against diverse epitopes of the ectodomain of HIV-1 gp41.

C. Bewley, G. Clore, J. Louis, 2005, Journal of molecular biology.

Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation.

C. Bewley, G. Clore, J. Louis, 2005, Biochemistry.

Visualizing Tetrahedral Oxyanion Bound in HIV-1 Protease Using Neutrons: Implications for the Catalytic Mechanism and Drug Design

J. Louis, S. Kent, A. Kovalevsky, 2020, ACS omega.

Substituted Bis-THF Protease Inhibitors with Improved Potency against Highly Resistant Mature HIV-1 Protease PR20.

Arun K. Ghosh, J. Louis, I. Weber, 2015, Journal of medicinal chemistry.

Room Temperature Neutron Crystallography of Drug Resistant HIV-1 Protease Uncovers Limitations of X-ray Structural Analysis at 100 K.

J. Louis, I. Weber, A. Kovalevsky, 2017, Journal of medicinal chemistry.

The C34 Peptide Fusion Inhibitor Binds to the Six-Helix Bundle Core Domain of HIV-1 gp41 by Displacement of the C-Terminal Helical Repeat Region.

G. Clore, J. Louis, J. Baber, 2015, Biochemistry.

Covalent Trimers of the Internal N-terminal Trimeric Coiled-coil of gp41 and Antibodies Directed against Them Are Potent Inhibitors of HIV Envelope-mediated Cell Fusion*

C. Bewley, G. Clore, J. Louis, 2003, Journal of Biological Chemistry.

β‐Adrenergic regulation of c‐fos gene expression in an epithelial cell line

J. Louis, C. Yeh, E. Kousvelari, 1988 .

Global Dynamics of a Protein on the Surface of Anisotropic Lipid Nanoparticles Derived from Relaxation-Based NMR Spectroscopy.

G. Clore, J. Louis, V. Tugarinov, 2022, Journal of Physical Chemistry B.

Temperature-dependent intermediates in HIV-1 envelope glycoprotein-mediated fusion revealed by inhibitors that target N- and C-terminal helical regions of HIV-1 gp41.

S. A. Gallo, C. Bewley, G. Clore, 2004, Biochemistry.

Kinetic, stability, and structural changes in high-resolution crystal structures of HIV-1 protease with drug-resistant mutations L24I, I50V, and G73S.

J. Louis, I. Weber, R. Harrison, 2006, Journal of molecular biology.

Regulation of proto-oncogenes in rat parotid acinar cells in vitro after stimulation of beta-adrenergic receptors.

J. Louis, L. H. Huang, T. Curran, 1988, Experimental cell research.

Diverse Folding Pathways of HIV-1 Protease Monomer on a Rugged Energy Landscape.

J. Louis, Janghyun Yoo, H. Chung, 2019, Biophysical journal.

Fast three-color single-molecule FRET using statistical inference

J. Louis, Jae-Yeol Kim, Janghyun Yoo, 2020, Nature Communications.

Co-Evolutionary Fitness Landscapes for Sequence Design.

J. Louis, R. Best, J. Baber, 2018, Angewandte Chemie.

Enhanced stability of monomer fold correlates with extreme drug resistance of HIV-1 protease.

J. Louis, J. Roche, Annie Aniana, 2013, Biochemistry.

Unmasking the Conformational Stability and Inhibitor Binding to SARS-CoV-2 Main Protease Active Site Mutants and Miniprecursor

J. Louis, R. Ghirlando, L. Coates, 2022, Journal of Molecular Biology.

Autoprocessing and oxyanion loop reorganization upon GC373 and nirmatrelvir binding of monomeric SARS-CoV-2 main protease catalytic domain

J. Louis, R. Ghirlando, L. Coates, 2022, Communications Biology.

Evolution of cyclic peptide protease inhibitors

Peter G. Schultz, Stephen J. Benkovic, John M. Louis, 2011, Proceedings of the National Academy of Sciences.

Real-time exchange of the lipid-bound intermediate and post-fusion states of the HIV-1 gp41 ectodomain.

A. Bax, J. Louis, R. Best, 2022, Journal of molecular biology.

Dependence of distance distributions derived from double electron-electron resonance pulsed EPR spectroscopy on pulse-sequence time.

G. Clore, J. Louis, J. Baber, 2015, Angewandte Chemie.

Tilted, Uninterrupted, Monomeric HIV-1 gp41 Transmembrane Helix from Residual Dipolar Couplings.

A. Bax, J. Louis, R. Ghirlando, 2018, Journal of the American Chemical Society.

Structural Basis of HIV-1 Neutralization by Affinity Matured Fabs Directed against the Internal Trimeric Coiled-Coil of gp41

C. Bewley, G. Clore, D. E. Anderson, 2010, PLoS Pathogens.

Revealing the dimer dissociation and existence of a folded monomer of the mature HIV‐2 protease

J. Louis, R. Ishima, Annie Aniana, 2009, Protein science : a publication of the Protein Society.

Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease: room-temperature X-ray and neutron crystallography, binding thermodynamics, and antiviral activity

J. Louis, P. Bonnesen, K. Weiss, 2022, Research square.

Caught in the Act: the 1.5 A resolution crystal structures of the HIV-1 protease and the I54V mutant reveal a tetrahedral reaction intermediate.

Irene T Weber, J. Louis, I. Weber, 2007, Biochemistry.

Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV‐1 protease: Relevance to drug resistance

J. Louis, I. Weber, J. Agniswamy, 2010, Protein science : a publication of the Protein Society.

Carbonyl carbon transverse relaxation dispersion measurements and ms-μs timescale motion in a protein hydrogen bond network

J. Louis, D. Torchia, J. Baber, 2004 .

Long-Range Electrostatics-Induced Two-Proton Transfer Captured by Neutron Crystallography in an Enzyme Catalytic Site.

Jerry M. Parks, Jeremy C. Smith, J. Louis, 2016, Angewandte Chemie.

Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation

A. Bax, J. Louis, J. Lorieau, 2011, Journal of the American Chemical Society.

Comparison of methyl rotation axis order parameters derived from model-free analyses of (2)H and (13)C longitudinal and transverse relaxation rates measured in the same protein sample.

J. Louis, D. Torchia, R. Ishima, 2001, Journal of the American Chemical Society.

Kinetic and modeling studies of S3-S3' subsites of HIV proteinases.

J. Louis, I. Weber, A. Gustchina, 1992, Biochemistry.

The effect of salt on the Michaelis Menten constant of the HIV‐1 protease correlates with the Hofmeister series

J. Louis, S. Oroszlan, E. Wondrak, 1991, FEBS letters.

Binding kinetics and substrate selectivity in HIV-1 protease−Gag interactions probed at atomic resolution by chemical exchange NMR

G. Clore, J. Louis, L. Deshmukh, 2017, Proceedings of the National Academy of Sciences.

Design of a Novel Peptide Inhibitor of HIV Fusion That Disrupts the Internal Trimeric Coiled-coil of gp41*

G. Marius Clore, John M. Louis, Rodolfo Ghirlando, 2002, The Journal of Biological Chemistry.

MWC allosteric model explains unusual hemoglobin-oxygen binding curves from sickle cell drug binding

E. Henry, W. Eaton, J. Louis, 2021, Biophysical journal.

Allosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease

E. Henry, J. Hofrichter, W. Eaton, 2020, Proceedings of the National Academy of Sciences.

Extreme multidrug resistant HIV-1 protease with 20 mutations is resistant to novel protease inhibitors with P1'-pyrrolidinone or P2-tris-tetrahydrofuran.

Arun K. Ghosh, J. Louis, I. Weber, 2013, Journal of medicinal chemistry.

Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors

J. Louis, I. Weber, Annie Aniana, 2011, Proceedings of the National Academy of Sciences.

Autoprocessing of HIV-1 protease is tightly coupled to protein folding

G. Marius Clore, John M. Louis, Angela M. Gronenborn, 1999, Nature Structural Biology.

Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease

G. Clore, J. Louis, Annie Aniana, 2008, Nature.

Cloning of the bovine leukemia virus proteinase in Escherichia coli and comparison of its specificity to that of human T-cell leukemia virus proteinase.

J. Louis, T. Copeland, J. Tözsér, 2000, Biochimica et biophysica acta.

pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR

A. Bax, J. Louis, C. Schwieters, 2012, Proceedings of the National Academy of Sciences.

Effect of salt on the kinetic parameters of retroviral and mammalian aspartic acid proteases

J. Louis, D. Jerina, J. Tropea, 1992 .

The Regulation of Dictyostelium Development by Transmembrane Signalling

J. Louis, C. Saxe, A. Kimmel, 1995, The Journal of eukaryotic microbiology.

Constraints on the Structure of Fibrils Formed by a Racemic Mixture of Amyloid-β Peptides from Solid-State NMR, Electron Microscopy, and Theory.

J. Louis, R. Tycko, W. Yau, 2021, Journal of the American Chemical Society.

Observation of β-Amyloid Peptide Oligomerization by Pressure-Jump NMR Spectroscopy.

A. Bax, J. Louis, P. Anfinrud, 2019, Journal of the American Chemical Society.

Three-Color Single-Molecule FRET and Fluorescence Lifetime Analysis of Fast Protein Folding.

J. Louis, Janghyun Yoo, H. Chung, 2018, The journal of physical chemistry. B.

Analysis of Fluorescence Lifetime and Energy Transfer Efficiency in Single-Molecule Photon Trajectories of Fast-Folding Proteins.

J. Louis, H. Chung, I. Gopich, 2016, The journal of physical chemistry. B.

Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories.

W. Eaton, J. Louis, H. Chung, 2013, Chemical physics.

Distinguishing between protein dynamics and dye photophysics in single-molecule FRET experiments.

W. Eaton, J. Louis, H. Chung, 2010, Biophysical journal.

Dimerization of the class A G protein-coupled neurotensin receptor NTS1 alters G protein interaction

Joseph Shiloach, Reinhard Grisshammer, J. Louis, 2007, Proceedings of the National Academy of Sciences.

Cross-reactive HIV-1 neutralizing monoclonal antibodies selected by screening of an immune human phage library against an envelope glycoprotein (gp140) isolated from a patient (R2) with broadly HIV-1 neutralizing antibodies.

S. Rybak, C. Broder, J. Louis, 2007, Virology.

Extracting rate coefficients from single-molecule photon trajectories and FRET efficiency histograms for a fast-folding protein.

William A Eaton, Kevin J. McHale, Troy Cellmer, 2011, The journal of physical chemistry. A.

Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories

William A Eaton, W. Eaton, J. Louis, 2009, Proceedings of the National Academy of Sciences.

NMR solution structure of a cyanovirin homolog from wheat head blight fungus

A. Gronenborn, J. Louis, J. Jee, 2011, Proteins.

Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease

J. Louis, P. Bonnesen, K. Weiss, 2022, Nature Communications.

Solution structure of a circular-permuted variant of the potent HIV-inactivating protein cyanovirin-N: structural basis for protein stability and oligosaccharide interaction.

A. Gronenborn, J. Louis, P. Seeberger, 2003, Journal of molecular biology.

Design and initial characterization of a circular permuted variant of the potent HIV‐inactivating protein cyanovirin‐N

A. Gronenborn, M. Boyd, J. Louis, 2002, Proteins.

Unmasking the Conformational Stability and Inhibitor Binding to SARS-CoV-2 Miniprecursor

J. Louis, R. Ghirlando, L. Coates, 2022 .

Structural, Electronic, and Electrostatic Determinants for Inhibitor Binding to Subsites S1 and S2 in SARS-CoV-2 Main Protease

J. Louis, A. Ramanathan, M. Head, 2021, Journal of medicinal chemistry.

The structure of a replication initiator unites diverse aspects of nucleic acid metabolism

A. Gronenborn, J. Louis, R. Campos-Olivas, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Design and Properties of NCCG-gp41, a Chimeric gp41 Molecule with Nanomolar HIV Fusion Inhibitory Activity*

C. Bewley, G. Clore, J. Louis, 2001, The Journal of Biological Chemistry.

Letter to the Editor: 1H, 13C, 15N resonance assignments and fold verification of a circular permuted variant of the potent HIV-inactivating protein cyanovirin-N*

András Fiser, John M. Louis, Angela M. Gronenborn, 2001, Journal of biomolecular NMR.

The GB1 amyloid fibril: recruitment of the peripheral beta-strands of the domain swapped dimer into the polymeric interface.

U. Baxa, A. Gronenborn, J. Louis, 2005, Journal of molecular biology.

Terminal interface conformations modulate dimer stability prior to amino terminal autoprocessing of HIV-1 protease.

J. Louis, I. Weber, J. Agniswamy, 2012, Biochemistry.

Structure and dynamics of KH domains from FBP bound to single-stranded DNA

G. Clore, J. Louis, D. Levens, 2002, Nature.

The cAMP receptor CAR4 regulates axial patterning and cellular differentiation during late development of Dictyostelium.

J. Louis, A. Kimmel, G. Ginsburg, 1994, Genes & development.

Novel macromolecular inhibitors of human immunodeficiency virus-1 protease.

J. Louis, R. Ishima, J. Tözsér, 2008, Protein engineering, design & selection : PEDS.

Measurement of 15N relaxation in the detergent-solubilized tetrameric KcsA potassium channel

Ad Bax, A. Bax, J. Louis, 2006, Journal of biomolecular NMR.

The phosphoprotein p53 is down-regulated post-transcriptionally during embryogenesis in vertebrates.

J. Louis, P. May, P. Mora, 1988, Biochimica et biophysica acta.

Sequence-specific protein interaction with a transcriptional enhancer involved in the autoregulated expression of cAMP receptor 1 in Dictyostelium.

J. Louis, A. Kimmel, X. Mu, 1998, Development.

Stabilization from Autoproteolysis and Kinetic Characterization of the Human T-cell Leukemia Virus Type 1 Proteinase*

John M. Louis, J. Louis, J. Tözsér, 1999, The Journal of Biological Chemistry.

CAR2, a prestalk cAMP receptor required for normal tip formation and late development of Dictyostelium discoideum.

J. Louis, P. Devreotes, C. Saxe, 1993, Genes & development.

Transient lipid-bound states of spike protein heptad repeats provide insights into SARS-CoV-2 membrane fusion

A. Bax, J. Louis, R. Ghirlando, 2021, Science advances.

Dissociation of the trimeric gp41 ectodomain at the lipid–water interface suggests an active role in HIV-1 Env-mediated membrane fusion

A. Bax, J. Louis, A. Grishaev, 2014, Proceedings of the National Academy of Sciences.

Internal dynamics of the homotrimeric HIV-1 viral coat protein gp41 on multiple time scales.

A. Bax, J. Louis, A. Grishaev, 2013, Angewandte Chemie.

The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics.

A. Bax, J. Louis, J. Lorieau, 2013, Biopolymers.

Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings.

A. Bax, J. Louis, G. Kontaxis, 2002, Journal of molecular biology.

Rapid structural fluctuations of the free HIV protease flaps in solution: Relationship to crystal structures and comparison with predictions of dynamics calculations

Rieko Ishima, J. Louis, Yun-Xing Wang, 2002, Protein science : a publication of the Protein Society.

Characterization of two hydrophobic methyl clusters in HIV-1 protease by NMR spin relaxation in solution.

J. Louis, D. Torchia, R. Ishima, 2001, Journal of molecular biology.

Comparison of the substrate specificity of the human T-cell leukemia virus and human immunodeficiency virus proteinases.

J. Louis, I. Weber, R. Harrison, 2000, European journal of biochemistry.

The gag precursor contains a specific HIV‐1 protease cleavage site between the NC (P7) and P1 proteins

J. Louis, B. Roques, J. Chermann, 1993, FEBS letters.

Purification of HIV‐1 wild‐type protease and characterization of proteolytically inactive HIV‐1 protease mutants by pepstatin A affinity chromatography

J. Louis, P. Mora, S. Oroszlan, 1991, FEBS letters.

A solid phase assay for the protease of human immunodeficiency virus.

J. Louis, T. Copeland, S. Oroszlan, 1990, Analytical Biochemistry.

Chemical synthesis and expression of the HIV-1 protease gene in E. coli.

J. Louis, C. Smith, P. Mora, 1989, Biochemical and biophysical research communications.

Dysregulated interactions triggered by a neuropathy-causing mutation in the IPV motif of HSP27

J. Louis, B. Asselbergh, T. Alderson, 2019, bioRxiv.

Dysregulated interactions triggered by a neuropathy-causing mutation in the IPV motif of HSP27

J. Louis, B. Asselbergh, T. Alderson, 2019, bioRxiv.

A weakened interface in the P182L variant of HSP27 associated with severe Charcot‐Marie‐Tooth neuropathy causes aberrant binding to interacting proteins

J. Louis, B. Asselbergh, A. Baldwin, 2021, The EMBO journal.

Antiviral agent based on the non-structural protein targeting the maturation process of HIV-1: expression and susceptibility of chimeric Vpr as a substrate for cleavage by HIV-1 protease.

J. Louis, I. Weber, R. Harrison, 2000, Protein engineering.

HIV-I protease: Maturation, enzyme specificity, and drug resistance

A. Gronenborn, G. Clore, J. Louis, 2000 .

Continuous spectrophotometric assay for retroviral proteases of HIV-1 and AMV.

J. Louis, D. Jerina, P. Mora, 1989, Biochemical and biophysical research communications.

Effect of sequence polymorphism and drug resistance on two HIV-1 Gag processing sites.

Irene T Weber, Robert W Harrison, Péter Bagossi, 2002, European journal of biochemistry.

A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles*

A. Bax, J. Louis, J. Chou, 2001, Journal of biomolecular NMR.

Transient HIV-1 Gag–protease interactions revealed by paramagnetic NMR suggest origins of compensatory drug resistance mutations

G. Clore, J. Louis, L. Deshmukh, 2016, Proceedings of the National Academy of Sciences.

Evidence of Distinct Channel Conformations and Substrate Binding Affinities for the Mitochondrial Outer Membrane Protein Translocase Pore Tom40*

J. Louis, T. Lithgow, S. Buchanan, 2015, The Journal of Biological Chemistry.

Evidence for distinct Tom 40 substrate binding conformations 1 Evidence of distinct channel conformations and substrate binding affinities for the mitochondrial outer membrane protein translocase pore Tom 40 *

J. Louis, T. Lithgow, S. Buchanan, 2015 .

Revisiting Monomeric HIV-1 Protease

Angela M Gronenborn, Rieko Ishima, L. Pannell, 2003, The Journal of Biological Chemistry.

Characterization of the cholesteric phase of filamentous bacteriophage fd for molecular alignment.

A. Gronenborn, J. Louis, L. Barrientos, 2001, Journal of magnetic resonance.

Effects of an HIV-1 maturation inhibitor on the structure and dynamics of CA-SP1 junction helices in virus-like particles

J. Louis, R. Tycko, Sebanti Gupta, 2020, Proceedings of the National Academy of Sciences.

Probing the mechanism of inhibition of amyloid-β(1–42)–induced neurotoxicity by the chaperonin GroEL

G. Clore, J. Louis, R. Ghirlando, 2018, Proceedings of the National Academy of Sciences.

Structures of brain-derived 42-residue amyloid-β fibril polymorphs with unusual molecular conformations and intermolecular interactions

J. Louis, R. Tycko, W. Yau, 2023, Proceedings of the National Academy of Sciences of the United States of America.

Contribution of the catalytic dyad of SARS-CoV-2 main protease to binding covalent and noncovalent inhibitors

J. Louis, P. Bonnesen, L. Coates, 2023, Journal of Biological Chemistry.

Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114.

Irene T Weber, Robert W Harrison, Arun K. Ghosh, 2006, Journal of molecular biology.

High resolution crystal structures of HIV-1 protease with a potent non-peptide inhibitor (UIC-94017) active against multi-drug-resistant clinical strains.

Irene T Weber, Robert W Harrison, Yuan-Fang Wang, 2004, Journal of molecular biology.

Single-Molecule Fluorescence Experiments Determine Protein Folding Transition Path Times

Kevin J. McHale, W. Eaton, J. Louis, 2012, Science.

Concentration-dependent structural transition of the HIV-1 gp41 MPER peptide into α-helical trimers.

A. Bax, J. Louis, S. Chiliveri, 2020, Angewandte Chemie.

Concentration-dependent structural transition of the HIV-1 gp41 MPER peptide into α-helical trimers.

A. Bax, J. Louis, S. Chiliveri, 2020, Angewandte Chemie.

Antibody elicited against the gp41 N-heptad repeat (NHR) coiled-coil can neutralize HIV-1 with modest potency but non-neutralizing antibodies also bind to NHR mimetics.

D. Richman, D. Burton, C. Bewley, 2008, Virology.

Mechanism of dissociative inhibition of HIV protease and its autoprocessing from a precursor.

J. Louis, Annie Aniana, J. M. Sayer, 2012, Journal of molecular biology.

Testing Landscape Theory for Biomolecular Processes with Single Molecule Fluorescence Spectroscopy.

William A Eaton, Katherine Truex, W. Eaton, 2015, Physical review letters.

Biophysical Characterization of gp41 Aggregates Suggests a Model for the Molecular Mechanism of HIV-associated Neurological Damage and Dementia*

L. Pannell, L. Liotta, G. Clore, 2000, The Journal of Biological Chemistry.

Conformation of Inhibitor‐Free HIV‐1 Protease Derived from NMR Spectroscopy in a Weakly Oriented Solution

A. Bax, J. Louis, Julien Roche, 2015, Chembiochem : a European journal of chemical biology.

Inhibition of HIV Maturation via Selective Unfolding and Cross-Linking of Gag Polyprotein by a Mercaptobenzamide Acetylator.

G. Clore, J. Louis, L. Deshmukh, 2019, Journal of the American Chemical Society.

Proteolytic Processing of HIV-1 Protease Precursor, Kinetics and Mechanism*

J. Louis, P. Wingfield, A. Kimmel, 1999, The Journal of Biological Chemistry.

Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein.

J. Louis, D. Jerina, K. Parris, 1994, Proceedings of the National Academy of Sciences of the United States of America.

HIV-1 protease: structure, dynamics, and inhibition.

Irene T Weber, Rieko Ishima, J. Louis, 2007, Advances in pharmacology.

Critical differences in HIV‐1 and HIV‐2 protease specificity for clinical inhibitors

Arun K. Ghosh, J. Louis, I. Weber, 2012, Protein science : a publication of the Protein Society.

Structural evidence for effectiveness of darunavir and two related antiviral inhibitors against HIV-2 protease.

Arun K. Ghosh, J. Louis, I. Weber, 2008, Journal of molecular biology.

Binding of Clinical Inhibitors to a Model Precursor of a Rationally Selected Multidrug Resistant HIV-1 Protease Is Significantly Weaker Than That to the Released Mature Enzyme.

J. Louis, I. Weber, R. Harrison, 2016, Biochemistry.

A Transient Precursor of the HIV-1 Protease

J. Louis, D. Jerina, N. Nashed, 1996, The Journal of Biological Chemistry.

Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli.

J. Louis, D. Jerina, P. Mora, 1991, European journal of biochemistry.

Substitution mutations of the highly conserved arginine 87 of HIV-1 protease result in loss of proteolytic activity.

J. Louis, C. Smith, P. Mora, 1989, Biochemical and biophysical research communications.

Michaelis-like complex of SARS-CoV-2 main protease visualized by room-temperature X-ray crystallography

J. Louis, Qiu Zhang, L. Coates, 2021, IUCrJ.

Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR.

A. Gronenborn, J. Louis, K. Ding, 2004, Journal of molecular biology.

Insights into the Conformation of the Membrane Proximal Regions Critical to the Trimerization of the HIV-1 gp41 Ectodomain Bound to Dodecyl Phosphocholine Micelles

A. Bax, J. Louis, R. Ghirlando, 2016, PloS one.

Transverse1H Cross Relaxation in1H–15N Correlated1H CPMG Experiments

J. Louis, D. Torchia, R. Ishima, 1999 .

Evolution under Drug Pressure Remodels the Folding Free-Energy Landscape of Mature HIV-1 Protease.

J. Louis, Julien Roche, 2016, Journal of molecular biology.

Probing the Interaction between HIV‐1 Protease and the Homodimeric p66/p66’ Reverse Transcriptase Precursor by Double Electron‐Electron Resonance EPR Spectroscopy

G. Clore, J. Louis, T. Schmidt, 2020, Chembiochem : a European journal of chemical biology.

Synergistic inhibition of HIV-1 envelope-mediated membrane fusion by inhibitors targeting the N and C-terminal heptad repeats of gp41.

C. Bewley, G. Clore, J. Louis, 2006, Journal of molecular biology.

Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies

A. Gronenborn, J. Louis, K. Valentine, 2003, Journal of biomolecular NMR.

Complexes of Neutralizing and Non-Neutralizing Affinity Matured Fabs with a Mimetic of the Internal Trimeric Coiled-Coil of HIV-1 gp41

S. Subramaniam, G. Clore, J. Louis, 2013, PloS one.

NMR study of the tetrameric KcsA potassium channel in detergent micelles

Ad Bax, Christopher Miller, A. Bax, 2006, Protein science : a publication of the Protein Society.

Crystal structures of HIV protease V82A and L90M mutants reveal changes in the indinavir-binding site.

Irene T Weber, Robert W Harrison, Yuan-Fang Wang, 2004, European journal of biochemistry.

A rapid method to attain isotope labeled small soluble peptides for NMR studies

J. Louis, B. Koenig, M. Rogowski, 2003, Journal of biomolecular NMR.

A solution NMR study of the binding kinetics and the internal dynamics of an HIV‐1 protease‐substrate complex

A. Gronenborn, J. Louis, T. Yamazaki, 2003, Protein science : a publication of the Protein Society.

Effect of serine and tyrosine phosphorylation on retroviral proteinase substrates.

J. Louis, T. Copeland, E. Majerová, 1999, European journal of biochemistry.

Combining mutations in HIV‐1 protease to understand mechanisms of resistance

Irene T Weber, Robert W Harrison, Yuan-Fang Wang, 2002, Proteins.

Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR.

A. Bax, J. Louis, F. Delaglio, 2007, Biochimica et biophysica acta.

Modulation of Human Immunodeficiency Virus Type 1 Protease Autoprocessing by Charge Properties of Surface Residue 69

J. Louis, J. M. Sayer, Chaoping Chen, 2009, Journal of Virology.

Effect of substrate residues on the P2' preference of retroviral proteinases.

J. Louis, T. Copeland, J. Tözsér, 1999, European journal of biochemistry.

Studies on the Symmetry and Sequence Context Dependence of the HIV-1 Proteinase Specificity*

Irene T. Weber, John M. Louis, J. Louis, 1997, The Journal of Biological Chemistry.

Modulation of Human Immunodeﬁciency Virus Type 1 Protease Autoprocessing by Charge Properties of Surface Residue 69 (cid:1)

J. Louis, J. M. Sayer, Chaoping Chen, 2009 .

Structural basis for specificity of retroviral proteases.

J. Louis, I. Weber, R. Harrison, 1998, Biochemistry.

Effect of the Active Site D25N Mutation on the Structure, Stability, and Ligand Binding of the Mature HIV-1 Protease*

J. Louis, I. Weber, R. Ishima, 2008, Journal of Biological Chemistry.

HIV-1 protease: maturation, enzyme specificity, and drug resistance.

A. Gronenborn, G. Clore, J. Louis, 2000, Advances in pharmacology.

Structures of Darunavir-Resistant HIV-1 Protease Mutant Reveal Atypical Binding of Darunavir to Wide Open Flaps

J. Louis, I. Weber, R. Harrison, 2014, ACS chemical biology.

Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles

A. Bax, J. Louis, J. Lorieau, 2013, Journal of biomolecular NMR.

Influence of flanking sequences on the dimer stability of human immunodeficiency virus type 1 protease.

J. Louis, E. Wondrak, 1996, Biochemistry.

Mechanism of drug resistance revealed by the crystal structure of the unliganded HIV-1 protease with F53L mutation.

Irene T Weber, Robert W Harrison, Yuan-Fang Wang, 2006, Journal of molecular biology.

Highly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV‐1 protease

Irene T Weber, Rieko Ishima, J. Louis, 2010, Proteins.

Molecular charecterization of multidrug resistance in acinetobacter species

J. Louis, V. Balasubramanian, Bosco Dhanaseeli, 2014 .

Fast three-color single-molecule FRET using statistical inference

J. Louis, Jae-Yeol Kim, Janghyun Yoo, 2020, Nature Communications.

Probing the structure and stability of a hybrid protein: the human-E. coli thioredoxin chimera.

M. L. Tasayco, A. Gronenborn, J. Louis, 2001, Biochemistry.

Inside Back Cover: Co‐Evolutionary Fitness Landscapes for Sequence Design (Angew. Chem. Int. Ed. 20/2018)

Pengfei Tian, Robert B. Best, John M. Louis, 2018 .

Is human thioredoxin monomeric or dimeric?

A. Gronenborn, J. Louis, P. Wingfield, 2008, Protein science : a publication of the Protein Society.

Dysregulation of HSP27 oligomerization and interactions by a neuropathy-causing mutation in the IPV motif

J. Louis, B. Asselbergh, T. Alderson, 2019 .

Binding of clinical inhibitors to a model precursor of a rationally selected multidrug resistant HIV-1 protease is significantly weaker than to the released mature enzyme

J. Louis, I. Weber, Xiaxia Yu, 2016 .

Mixed-time parallel evolution in multiple quantum NMR experiments: sensitivity and resolution enhancement in heteronuclear NMR

A. Bax, J. Louis, Jinfa Ying, 2007, Journal of biomolecular NMR.

Dissociation of the trimeric gp41 ectodomain at the lipid–water interface suggests an active role in HIV-1 Env-mediated membrane fusion

A. Bax, J. Louis, A. Grishaev, 2014, Proceedings of the National Academy of Sciences.

Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding

A. Bax, J. Louis, R. Ghirlando, 2015, Journal of Biomolecular NMR.

The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures.

A. Gronenborn, M. Boyd, J. Louis, 2002, Structure.

Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles

A. Bax, J. Louis, J. Lorieau, 2013, Journal of Biomolecular NMR.

Analysis of Fluorescence Lifetime and Energy Transfer Efficiency in Single-Molecule Photon Trajectories of Fast-Folding Proteins.

J. Louis, H. Chung, I. Gopich, 2016, The journal of physical chemistry. B.

Two transmembrane signaling mechanisms control expression of the cAMP receptor gene CAR1 during Dictyostelium development.

J. Louis, C. Saxe, A. Kimmel, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Construction and characterization of a fully active PXR/SRC-1 tethered protein with increased stability W.Wang, W.W.Prosise, J.Chen, S.Shane Taremi, H.V.Le, V.Madison, X.Cui, A.Thomas, K.-C.Cheng and C.A.Lesburg 425 Directed evolution of a biterminal bacterial display scaffold enhances the display o

J. Louis, P. Daugherty, R. Ishima, 2008 .

Revisiting Monomeric HIV-1 Protease CHARACTERIZATION AND REDESIGN FOR IMPROVED PROPERTIES*

L. Pannell, A. Gronenborn, J. Louis, 2003 .

Proton transfer and drug binding details revealed in neutron diffraction studies of wild-type and drug resistant HIV-1 protease.

J. Louis, I. Weber, K. Weiss, 2020, Methods in enzymology.