J. Hofrichter

发表

A statistical mechanical model for β-hairpin kinetics

V. Muñoz, E. Henry, J. Hofrichter, 1998 .

Folding dynamics and mechanism of β-hairpin formation

V. Muñoz, J. Hofrichter, W. Eaton, 1997, Nature.

Submillisecond kinetics of protein folding.

V. Muñoz, J. Hofrichter, W. Eaton, 1997, Current opinion in structural biology.

Speed of intersubunit communication in proteins.

C. M. Jones, E. Henry, J. Hofrichter, 1992, Biochemistry.

Is cooperative oxygen binding by hemoglobin really understood?

Andrea Mozzarelli, William A. Eaton, E. Henry, 1999, Nature Structural Biology.

High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.

Regine Herbst-Irmer, Jan Kubelka, William A Eaton, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Fast kinetics and mechanisms in protein folding.

Lisa J. Lapidus, V. Muñoz, E. Henry, 2000, Annual review of biophysics and biomolecular structure.

Quasi-elastic laser light scattering from solutions and gels of hemoglobin S.

J. Hofrichter, Z. Kam, 1986, Biophysical journal.

The protein folding 'speed limit'.

J. Hofrichter, W. Eaton, J. Kubelka, 2004, Current opinion in structural biology.

Experimental tests of villin subdomain folding simulations.

J. Hofrichter, W. Eaton, J. Kubelka, 2003, Journal of molecular biology.

Chemical, physical, and theoretical kinetics of an ultrafast folding protein

E. Henry, J. Hofrichter, W. Eaton, 2008, Proceedings of the National Academy of Sciences.

Kinetics and Dynamics of Loops, α-Helices, β-Hairpins, and Fast-Folding Proteins

V. Muñoz, E. Henry, J. Hofrichter, 1998 .

Sub-microsecond protein folding.

J. Hofrichter, W. Eaton, D. Davies, 2006, Journal of molecular biology.

Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding.

J. Hofrichter, W. Eaton, S. Hagen, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Rate of Intrachain Diffusion of Unfolded Cytochrome c

J. Hofrichter, W. Eaton, S. Hagen, 1997 .

Measuring the rate of intramolecular contact formation in polypeptides.

Lisa J. Lapidus, J. Hofrichter, W. Eaton, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Fast events in protein folding initiated by nanosecond laser photolysis.

C. M. Jones, E. Henry, J. Hofrichter, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Submillisecond protein folding kinetics studied by ultrarapid mixing.

J. Hofrichter, W. Eaton, S. Takahashi, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease.

J. Hofrichter, W. Eaton, P. Ross, 1974, Proceedings of the National Academy of Sciences of the United States of America.

Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model.

J. Hofrichter, W. Eaton, P. A. Thompson, 1997, Biochemistry.

Kinetics and Dynamics of Loops, α-Helices, β-Hairpins, and Fast-Folding Proteins

V. Muñoz, E. Henry, J. Hofrichter, 1999 .

[8] Singular value decomposition: Application to analysis of experimental data

E. Henry, J. Hofrichter, E. R. Henry, 1992 .

Requirements for therapeutic inhibition of sickle haemoglobin gelation

J. Hofrichter, W. Eaton, H. Sunshine, 1978, Nature.

Kinetics of sickle haemoglobin polymerization in single red cells

Massimo Coletta, Frank A. Ferrone, William A. Eaton, 1982, Nature.

A multiparameter analysis of sickle erythrocytes in patients undergoing hydroxyurea therapy.

J. Hofrichter, W. Eaton, C. Guttmann, 1996, Blood.

Understanding the shape of sickled red cells.

William A Eaton, J. Hofrichter, W. Eaton, 2005, Biophysical journal.

Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity.

E. Henry, J. Hofrichter, W. Eaton, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Folding dynamics and mechanism of beta-hairpin formation.

V Muñoz, V. Muñoz, J. Hofrichter, 1997, Nature.

Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism.

J. Hofrichter, W. Eaton, F. Ferrone, 1980, Biophysical journal.

Hemoglobin S gelation and sickle cell disease.

J. Hofrichter, W. Eaton, 1987, Blood.

Geminate recombination of n-butyl isocyanide to myoglobin.

E. Henry, J. Hofrichter, J. Sommer, 1985, Biochemistry.

Folding and Aggregation Kinetics of a β-Hairpin†

V. Muñoz, J. Hofrichter, W. Eaton, 2006 .

ABSORPTION OF METHYLBACTERIOPHEOPHORBIDE a SINGLE CRYSTALS: SPECTRAL SHIFTS DUE TO π‐π INTERACTIONS

L. K. Hanson, J. Hofrichter, 1985 .

A second generation transgenic mouse model expressing both hemoglobin S (HbS) and HbS-Antilles results in increased phenotypic severity.

J. Hofrichter, E. Rubin, R. Nagel, 1995, Blood.

Supersaturation in sickle cell hemoglobin solutions.

J. Hofrichter, W. Eaton, P. Ross, 1976, Proceedings of the National Academy of Sciences of the United States of America.

Health monitoring in Austria - statistical models based on somatic cell count at cow level for early detection of udder health problems developed.

J. Hofrichter, C. Mosconi, W. Obritzhauser, 2010 .

Dynamics of Structural Changes in Hemoglobin

E. Henry, J. Hofrichter, W. Eaton, 1987 .

Comparison of sickle cell hemoglobin gelation kinetics measured by NMR and optical methods.

J. Hofrichter, W. Eaton, E. Becker, 1976, Biochemical and biophysical research communications.

Linear dichroism of biological chromophores.

J. Hofrichter, W. Eaton, 1976, Annual review of biophysics and bioengineering.

Dynamics of intramolecular contact formation in polypeptides: distance dependence of quenching rates in a room-temperature glass.

J. Hofrichter, W. Eaton, L. Lapidus, 2001, Physical review letters.

Dynamics of Intramolecular Contact Formation in Polypeptides

J. Hofrichter, W. Eaton, L. Lapidus, 2001 .

Protein Structure: Nanosecond Crystallographic Snapshots of Protein Structural Changes

E. Henry, J. Hofrichter, W. Eaton, 1996, Science.

Optical spectra and electronic structure of flavine mononucleotide in flavodoxin crystals.

J. Hofrichter, W. Eaton, M. Ludwig, 1975, Biochemistry.

Fast events in protein folding.

J. Hofrichter, W. Eaton, P. A. Thompson, 1996, Structure.

Geminate recombination of carbon monoxide to myoglobin.

E. Henry, J. Hofrichter, W. Eaton, 1983, Journal of molecular biology.

Polarized absorption and linear dichroism spectroscopy of hemoglobin.

J. Hofrichter, W. Eaton, 1981, Methods in enzymology.

Protein reaction kinetics in a room-temperature glass

J. Hofrichter, SJ Hagen, Warren D Eaton, 1995, Science.

A tertiary two-state allosteric model for hemoglobin.

E. Henry, J. Hofrichter, W. Eaton, 2002, Biophysical chemistry.

Can a two-state MWC allosteric model explain hemoglobin kinetics?

C. M. Jones, E. Henry, J. Hofrichter, 1997, Biochemistry.

Photocycles of bacteriorhodopsin in light- and dark-adapted purple membrane studied by time-resolved absorption spectroscopy.

E. Henry, J. Hofrichter, R. Lozier, 1989, Biophysical journal.

Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication.

E. Henry, J. Hofrichter, W. Eaton, 1985, Biochemistry.

The biophysics of sickle cell hydroxyurea therapy.

J. Hofrichter, W. Eaton, William A. Eaton, 1995, Science.

Sickle cell hemoglobin polymerization.

J. Hofrichter, W. Eaton, W A Eaton, 1990, Advances in protein chemistry.

Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism.

J. Hofrichter, W. Eaton, F. Ferrone, 1985, Journal of molecular biology.

Editorial: Delay time of gelation: a possible determinant of clinical severity in sickle cell disease

William A. Eaton, J. Hofrichter, W. Eaton, 1976 .

Calorimetric and optical characterization of sickle cell hemoglobin gelation.

J. Hofrichter, W. Eaton, P. Ross, 1975, Journal of molecular biology.

Gelation of sickle cell hemoglobin in mixtures with normal adult and fetal hemoglobins.

J. Hofrichter, W. Eaton, H. Sunshine, 1979, Journal of molecular biology.

Molecular and cellular pathogenesis of hemoglobin SC disease.

A. Schechter, J. Hofrichter, W. Eaton, 1982, Proceedings of the National Academy of Sciences of the United States of America.

Delay time of hemoglobin S polymerization prevents most cells from sickling in vivo.

J. Hofrichter, W. Eaton, A. Mozzarelli, 1987, Science.

Oxygen binding by sickle cell hemoglobin polymers.

J. Hofrichter, W. Eaton, F. Ferrone, 1982, Journal of molecular biology.

Thermodynamics of gelation of sickle cell deoxyhemoglobin.

J. Hofrichter, W. Eaton, P. Ross, 1977, Journal of molecular biology.

Phenotypic screening of the ReFRAME drug repurposing library to discover new drugs for treating sickle cell disease

E. Henry, J. Hofrichter, W. Eaton, 2022, bioRxiv.

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.

Kinetic assay shows that increasing red cell volume could be a treatment for sickle cell disease

E. Henry, J. Hofrichter, W. Eaton, 2017, Proceedings of the National Academy of Sciences.

Ligand binding and the gelation of sickle cell hemoglobin.

J. Hofrichter, 1979, Journal of molecular biology.

Current Perspectives on the Kinetics of Hemoglobin S Gelation

E. Henry, J. Hofrichter, W. Eaton, 1989, Annals of the New York Academy of Sciences.

Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques.

J. Hofrichter, W. Eaton, F. Ferrone, 1985, Journal of molecular biology.

LIGAND BINDING AND THE GELATION OF SICKLE CELL HEMOGLOBIN

J. Hofrichter, 1978 .

Small angle neutron scattering studies of HbA in concentrated solutions.

S. H. Chen, J. Hofrichter, R. Nossal, 1990, Biophysical journal.

Kinetics of sickle hemoglobin polymerization. III. Nucleation rates determined from stochastic fluctuations in polymerization progress curves.

J. Hofrichter, 1986, Journal of molecular biology.

The role of solvent viscosity in the dynamics of protein conformational changes.

C. M. Jones, E. Henry, J. Hofrichter, 1992, Science.

Conformational relaxation and ligand binding in myoglobin.

C. M. Jones, E. Henry, J. Hofrichter, 1994, Biochemistry.

Editorial: Delay time of gelation: a possible determinant of clinical severity in sickle cell disease.

J. Hofrichter, W. Eaton, P. Ross, 1976, Blood.

Evolution of allosteric models for hemoglobin

E. Henry, J. Hofrichter, W. Eaton, 2007, IUBMB life.

Effects of chain stiffness on the dynamics of loop formation in polypeptides. Appendix: Testing a 1-dimensional diffusion model for peptide dynamics

J. Hofrichter, W. Eaton, P. J. Steinbach, 2002 .

Effects of denaturants on the dynamics of loop formation in polypeptides.

Lisa J. Lapidus, J. Hofrichter, W. Eaton, 2006, Biophysical journal.

SUCCESSES AND FAILURES OF A SIMPLE NUCLEATION THEORY FOR SICKLE CELL HEMOGLOBIN GELATION

J. Hofrichter, W. Eaton, 1978 .

The Helix-Coil Kinetics of a Heteropeptide

V. Muñoz, E. Henry, J. Hofrichter, 2000 .

A statistical mechanical model for beta-hairpin kinetics.

V Muñoz, V. Muñoz, E. Henry, 1998, Proceedings of the National Academy of Sciences of the United States of America.

The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.

L. P. Murray, E. Henry, J. Hofrichter, 1988, Proceedings of the National Academy of Sciences of the United States of America.

Time-resolved optical spectroscopy and structural dynamics following photodissociation of carbonmonoxyhemoglobin.

L. P. Murray, E. Henry, J. Hofrichter, 1988, Biophysical chemistry.

Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

E. Henry, J. Hofrichter, W. Eaton, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Effect of Viscosity on the Kinetics of α-Helix and β-Hairpin Formation

J. Hofrichter, G. Jas, A. W. Eaton, 2001 .

Mixing Nanoliters in Microseconds

J. Hofrichter, W. Eaton, R. Austin, 1998 .

Photoselection in polarized photolysis experiments on heme proteins.

C. M. Jones, E. Henry, J. Hofrichter, 1993, Biophysical journal.

Ligand binding and conformational changes measured by time-resolved absorption spectroscopy.

C. M. Jones, E. Henry, J. Hofrichter, 1994, Methods in enzymology.

Dynamics of the quaternary conformational change in trout hemoglobin.

M Brunori, C. M. Jones, L. P. Murray, 1991, Biochemistry.

Determination of ultrafast protein folding rates from loop formation dynamics.

J. Hofrichter, W. Eaton, J. Kubelka, 2005, Journal of molecular biology.

Oxygen Binding and the Gelation of Sickle Cell Hemoglobin

J. Hofrichter, W. Eaton, F. Ferrone, 1981 .

Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering.

S Doniach, K. Hodgson, J. Hofrichter, 1999, Journal of molecular biology.

Reversible steps in the bacteriorhodopsin photocycle.

J. Hofrichter, G. Clore, R. Lozier, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Measuring internal friction of an ultrafast-folding protein

William A Eaton, Troy Cellmer, E. Henry, 2008, Proceedings of the National Academy of Sciences.

Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data.

Jan Kubelka, William A Eaton, Victor Muñoz, 2008, The journal of physical chemistry. B.

Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers.

J. Hofrichter, W. Eaton, R. Ghirlando, 2008, Biophysical journal.

Optical Triggers of Protein Folding

W. A. Eaton, H. B. Gray, J. Hofrichter, 1996, Science.

Making connections between ultrafast protein folding kinetics and molecular dynamics simulations

Marco Buscaglia, William A Eaton, Troy Cellmer, 2011, Proceedings of the National Academy of Sciences.

Evidence for a partially structured state of the amylin monomer.

J. Hofrichter, W. Eaton, R. Best, 2009, Biophysical journal.

Kinetics of intramolecular contact formation in a denatured protein.

Lisa J. Lapidus, J. Hofrichter, W. Eaton, 2003, Journal of molecular biology.

Measuring dynamic flexibility of the coil state of a helix-forming peptide.

Lisa J. Lapidus, J. Hofrichter, W. Eaton, 2002, Journal of molecular biology.

Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration.

E. Henry, J. Hofrichter, W. Eaton, 2007, Journal of the American Chemical Society.

Making connections between ultrafast protein folding kinetics and molecular dynamics simulations

E. Henry, J. Hofrichter, W. Eaton, 2011, Proceedings of the National Academy of Sciences.

Sickle Cell Hemoglobin Polymers Bind Oxygen Noncooperatively

J. Hofrichter, W. Eaton, F. Ferrone, 1982 .

Contributory presentations/posters

Diederichs, Bosco K. Ho, Hironori K. Nakamura, 1999, Journal of Biosciences.