H. Roder

发表

Early events in protein folding explored by rapid mixing methods.

H. Roder, K. Maki, Hong Cheng, 2006, Chemical reviews.

Solution structure and dynamics of a de novo designed three-helix bundle protein.

W. DeGrado, H. Roder, S. Walsh, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Stability engineering of anti-EGFR scFv antibodies by rational design of a lambda-to-kappa swap of the VL framework using a structure-guided approach

Roland L. Dunbrack, M. Shapovalov, A. Lehmann, 2015, mAbs.

Kinetic role of early intermediates in protein folding.

H. Roder, W. Colón, 1997, Current opinion in structural biology.

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.

Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands.

A. Bhuyan, H. Roder, G. A. Elöve, 1994, Biochemistry.

Identification of the predominant non-native histidine ligand in unfolded cytochrome c.

H. Roder, F. Sherman, W. Colón, 1997, Biochemistry.

Evidence for barrier-limited protein folding kinetics on the microsecond time scale

H. Roder, M. Shastry, 1998, Nature Structural Biology.

Rapid mixing methods for exploring the kinetics of protein folding.

H. Roder, K. Maki, Hong Cheng, 2004, Methods.

NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106–126

H. Roder, Hong Cheng, T. James, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Design of a switchable eliminase

Daniel W. Kulp, W. DeGrado, H. Roder, 2011, Proceedings of the National Academy of Sciences.

Energetics and kinetics of substrate analog-coupled staphylococcal nuclease folding revealed by a statistical mechanical approach

H. Roder, K. Maki, T. Ikura, 2020, Proceedings of the National Academy of Sciences.

Squalamine: an aminosterol antibiotic from the shark.

J. Forrest, S. Wehrli, H. Roder, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing

Soon-Ho Park, H. Roder, M. Shastry, 1999, Nature Structural Biology.

Stepwise helix formation and chain compaction during protein folding

H. Roder, Heinrich Roder, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Isothermal Analysis of ThermoFluor Data can readily provide Quantitative Binding Affinities

J. Karanicolas, H. Roder, A. Dickson, 2019, Scientific Reports.

Folding mechanism of reduced Cytochrome c: equilibrium and kinetic properties in the presence of carbon monoxide.

H. Roder, K. Maki, Hong Cheng, 2008, Journal of molecular biology.

An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core.

H. Roder, K. O'Neil, S. Park, 1997, Biochemistry.

Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy.

A. Chaffotte, H. Roder, M. Goldberg, 1992, Biochemistry.

Direct evidence for the cooperative unfolding of cytochrome c in lipid membranes from H-(2)H exchange kinetics.

H. Roder, H. Cheng, T. Pinheiro, 2000, Journal of molecular biology.

Redox-dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome c.

H. Roder, S. Englander, Y. Feng, 1990, Biochemistry.

Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c.

H. Roder, S. Englander, Y. Feng, 1990, Biophysical journal.

Gene network transitions in embryos depend upon interactions between a pioneer transcription factor and core histones

H. Roder, M. Magnuson, P. Santisteban, 2020, Nature Genetics.

Structure of the novel steroidal antibiotic squalamine determined by two-dimensional NMR spectroscopy

S. Durell, S. Wehrli, H. Roder, 1993, Steroids.

Autoinhibitory interactions between the PDZ2 and C-terminal domains in the scaffolding protein NHERF1.

H. Roder, Hong Cheng, Z. Bu, 2009, Structure.

Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles.

H. Roder, A. Watts, T. Pinheiro, 1997, Biochemistry.

A cytochrome c mutant with high electron transfer and antioxidant activities but devoid of apoptogenic effect.

D. Newmeyer, A. Arseniev, H. Roder, 2002, The Biochemical journal.

Advances in Mixer Design and Detection Methods for Kinetics Studies of Macromolecular Folding and Binding on the Microsecond Time Scale

H. Roder, T. Mizukami, 2022, Molecules.

SQUID measurement of metalloprotein magnetization. New methods applied to the nitrogenase proteins.

H. Roder, Anisha Roy, W. Orme-Johnson, 1987, Biophysical journal.

Trans/13-cis isomerization is essential for both the photocycle and proton pumping of bacteriorhodopsin.

C. Chang, H. Roder, G. Dollinger, 1985, Biophysical journal.

Proton resonance assignments of horse ferrocytochrome c.

A. Wand, H. Roder, S. Englander, 1989, Biochemistry.

Comparison of the magnetic properties of deoxy- and photodissociated myoglobin.

S. F. Bowne, H. Frauenfelder, M. Weissman, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Kinetic mechanism of folding and unfolding of Rhodobacter capsulatus cytochrome c2.

J. M. Sauder, H. Roder, N. Mackenzie, 1996, Biochemistry.

Slow folding-unfolding kinetics of an octameric β-peptide bundle.

W. DeGrado, H. Roder, F. Gai, 2014, ACS chemical biology.

Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two‐dimensional NMR

H. Roder, Y. Paterson, Yu-Zhu Zhang, 1995, Protein science : a publication of the Protein Society.

Ultrafast folding of α3D: A de novo designed three-helix bundle protein

Valerie Daggett, Feng Gai, William F. DeGrado, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Ultrafast folding of alpha3D: a de novo designed three-helix bundle protein.

Valerie Daggett, Feng Gai, V. Daggett, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Nonuniform chain collapse during early stages of staphylococcal nuclease folding detected by fluorescence resonance energy transfer and ultrarapid mixing methods

H. Roder, K. Maki, Hong Cheng, 2013, Protein science : a publication of the Protein Society.

Protein structure refinement based on paramagnetic NMR shifts: Applications to wild‐type and mutant forms of cytochrome c

M. Gochin, H. Roder, 1995, Protein science : a publication of the Protein Society.

Structural characterization of an equilibrium unfolding intermediate in cytochrome c.

H. Roder, Hong Cheng, R. F. Latypov, 2006, Journal of molecular biology.

Internal friction controls the speed of protein folding from a compact configuration.

S. Hagen, H. Roder, S. Pabit, 2004, Biochemistry.

The Tyrosine Kinase c-Src Specifically Binds to the Active Integrin αIIbβ3 to Initiate Outside-in Signaling in Platelets*

W. DeGrado, H. Roder, Hong Cheng, 2015, The Journal of Biological Chemistry.

Retroviral Integrases Promote Fraying of Viral DNA Ends*

H. Roder, A. Skalka, M. Andrake, 2011, The Journal of Biological Chemistry.

PDLIM3 supports hedgehog signaling in medulloblastoma by facilitating cilia formation

H. Roder, Zeng-jie Yang, Yijun Yang, 2023, Cell Death & Differentiation.

novel branch of the thioredoxin fold superfamily The evolutionarily conserved Dim1 protein defines a

Roland L. Dunbrack, T. Léveillard, J. Sahel, 2015 .

The evolutionarily conserved Dim1 protein defines a novel branch of the thioredoxin fold superfamily.

K. Gould, E. Golemis, H. Roder, 1999, Physiological genomics.

H-ras Inhibits the Hippo Pathway by Promoting Mst1/Mst2 Heterodimerization

Luis E. Arias-Romero, H. Roder, Sonali Rawat, 2016, Current Biology.

Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate

Sheena E. Radford, Colin Kleanthous, S. Radford, 2001, Nature Structural Biology.

Mapping of POP1-binding Site on Pyrin Domain of ASC*

H. Roder, Hong Cheng, Y. Park, 2008, Journal of Biological Chemistry.

[Expression of mutant horse cytochrome c genes in Escherichia coli].

H. Roder, D. Dolgikh, M. Kirpichnikov, 1998, Bioorganicheskaia khimiia.

Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferrocytochrome C.

S. Hagen, H. Roder, R. F. Latypov, 2002, Biochemistry.

An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR.

H. Roder, S. Englander, Y. Paterson, 1990, Science.

A single mutation in a regulatory protein produces evolvable allosterically regulated catalyst of nonnatural reaction.

Yurii S. Moroz, H. Roder, Hong Cheng, 2013, Angewandte Chemie.

Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods.

H. Roder, K. Maki, Hong Cheng, 2007, Journal of molecular biology.

Dimer dissociation and unfolding mechanism of coagulation factor XI apple 4 domain: spectroscopic and mutational analysis.

H. Roder, Hong Cheng, P. Walsh, 2007, Journal of molecular biology.

A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c.

H. Roder, J. Carey, L. Wu, 1993, Biochemistry.

Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.

S W Englander, A J Wand, A. Wand, 1990, Biochemistry.

Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR

S. Walter Englander, H. Roder, S. Englander, 1988, Nature.

Intrinsic disorder and oligomerization of the hepatitis delta virus antigen.

H. Roder, Hong Cheng, Johnm . Taylor, 2010, Virology.

Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state

H. Roder, A. Watts, T. Pinheiro, 2008, Protein science : a publication of the Protein Society.

A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein.

H. Roder, K. Kuwata, Ming Xu, 2015, Structure.

Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapie.

W. Wedemeyer, H. Roder, Ming Xu, 2011, Biophysical journal.

Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis.

K. Gould, E. Golemis, H. Roder, 2003, Biochemistry.

Proton resonance assignments of horse ferricytochrome c.

A. Wand, H. Roder, S. Englander, 1989, Biochemistry.

Folding and stability of a tryptophan-containing mutant of ubiquitin.

S. Khorasanizadeh, T. Butt, H. Roder, 1993, Biochemistry.

Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange.

H. Roder, 1989, Methods in enzymology.

Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature.

K. Wüthrich, G. Wagner, H. Roder, 1985, Biochemistry.

Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitor.

K. Wüthrich, G. Wagner, H. Roder, 1985, Biochemistry.

Early hydrogen-bonding events in the folding reaction of ubiquitin.

H. Roder, H Roder, M S Briggs, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2.

H. Roder, Hong Cheng, K. Campbell, 2019, Structure.

Determinants of protein hydrogen exchange studied in equine cytochrome c

L Mayne, S W Englander, J S Milne, 1998, Protein science : a publication of the Protein Society.

De novo design of a single-chain diphenylporphyrin metalloprotein.

Hong Cheng, Hongling Zou, W. DeGrado, 2007, Journal of the American Chemical Society.

Nanosecond flash photolysis study of carbon monoxide binding to the beta chain of hemoglobin Zürich [beta 63(E7)His leads to Arg].

H. Frauenfelder, H. Roder, D. Dlott, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Ligand binding to heme proteins: relevance of low-temperature data.

H. Frauenfelder, H. Roder, A. Ansari, 1986, Biochemistry.

Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation

J. Weisel, A. Canutescu, H. Roder, 2007, Proceedings of the National Academy of Sciences.

Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues

S. Khorasanizadeh, H. Roder, Heinrich Roder, 1996, Nature Structural Biology.

The effects of pK(a) tuning on the thermodynamics and kinetics of folding: design of a solvent-shielded carboxylate pair at the a-position of a coiled-coil.

W. DeGrado, H. Roder, W. L. Lau, 2010, Biophysical journal.

Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing

H. Roder, K. Maki, K. Teilum, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Two-dimensional 1H NMR studies of cytochrome c: hydrogen exchange in the N-terminal helix.

A. Wand, H. Roder, S. Englander, 1986, Biochemistry.

Ultrafast hydrogen exchange reveals specific structural events during the initial stages of folding of cytochrome c.

Ming Xu, Hong Cheng, Hossein Fazelinia, 2014, Journal of the American Chemical Society.

Kinetics of loop formation and breakage in the denatured state of iso-1-cytochrome c.

B. Bowler, H. Roder, Eydiejo Kurchan, 2005, Journal of molecular biology.

Ultrarapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A.

H. Scheraga, E. Welker, D. Juminaga, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Methods for exploring early events in protein folding.

H. Roder, M. Shastry, 1999, Current opinion in structural biology.

Kinetic and Structural Analysis of Submillisecond Folding Events in Cytochrome c

J. M. Sauder, H. Roder, M. Shastry, 1998 .

Amide protection in an early folding intermediate of cytochrome c.

J. M. Sauder, H. Roder, 1998, Folding & design.

Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy.

R. Hochstrasser, W. DeGrado, D. Talaga, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Arginyltransferase ATE1 catalyzes midchain arginylation of proteins at side chain carboxylates in vivo.

J. Yates, Catherine C L Wong, L. Hedstrom, 2014, Chemistry & biology.

Structural and kinetic characterization of early folding events in β-lactoglobulin

C. Batt, H. Roder, Hong Cheng, 2001, Nature Structural Biology.

Structural and kinetic characterization of early folding events in beta-lactoglobulin.

C. Batt, H. Roder, K. Kuwata, 2001, Nature structural biology.

Conformational equilibration time of unfolded protein chains and the folding speed limit.

R. A. Goldbeck, H. Roder, R. F. Latypov, 2007, Biochemistry.

Definition of amide protection factors for early kinetic intermediates in protein folding.

H. Scheraga, W. Houry, H. Roder, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Structure and Stability of Cytochrome c Folding Intermediates

H. Roder, G. A. Elove, Gulnur A. Elove, 1991 .

Parallel pathways in cytochrome c(551) folding.

M. Brunori, H. Roder, S. Gianni, 2003, Journal of molecular biology.

Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562.

A. Fersht, H. Roder, L. Banci, 2005, Journal of molecular biology.

Early events during folding of wild-type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing.

H. Roder, K. Maki, Hong Cheng, 2004, Journal of molecular biology.

Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons

K Wüthrich, K. Wüthrich, H. Roder, 1986, Proteins.

Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding.

F Sherman, H. Roder, F. Sherman, 1996, Biochemistry.

Kinetic intermediates in the formation of the cytochrome c molten globule

H. Roder, W. Colón, 1996, Nature Structural Biology.

Gene network transitions in embryos depend upon interactions between a pioneer transcription factor and core histones

Anna B. Osipovich, H. Roder, M. Magnuson, 2020, Nature Genetics.

Complex Folding Landscape of Apomyoglobin at Acidic pH Revealed by Ultrafast Kinetic Analysis of Core Mutants.

H. Roder, V. Bychkova, Ming Xu, 2018, The journal of physical chemistry. B.

Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments.

H. Roder, K. Maki, W. Surewicz, 2006, Journal of the American Chemical Society.

Microsecond folding dynamics of apomyoglobin at acidic pH.

H. Roder, O. Beresneva, Ming Xu, 2012, The journal of physical chemistry. B.

Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease.

H. Roder, S. Green, W. F. Walkenhorst, 1997, Biochemistry.

Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange

John L Markley, J. Markley, H. Roder, 2002, Protein science : a publication of the Protein Society.

A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein.

H. Roder, K. Kuwata, Ming Xu, 2015, Structure.

Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons

K. Wüthrich, H. Roder, 1986, Proteins.

A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale.

H. Roder, S. Luck, H Roder, 1998, Biophysical journal.

Localized solution structure refinement of an F45W variant of ubiquitin using stochastic boundary molecular dynamics and NMR distance restraints

S. Khorasanizadeh, H. Roder, P. B. Laub, 1995, Protein science : a publication of the Protein Society.

Nanosecond flash photolysis study of carbon monoxide binding to the 18 chain of hemoglobin Zurich [ , 863 ( E 7 ) His-- ArgI ( heme protein / ligand binding / protein dynamics / conformational relaxation / sequential-barrier model )

H. Frauenfelder, H. Roder, P. Langer, 1999 .

Folding of Staphylococcal Nuclease Induced by Binding of Chemically Modified Substrate Analogues Sheds Light on Mechanisms of Coupled Folding/Binding Reactions.

H. Roder, K. Maki, Saho Segawa, 2023, Biochemistry.

Design of a switchable eliminase

Daniel W. Kulp, W. DeGrado, H. Roder, 2011, Proceedings of the National Academy of Sciences.

Characterizing protein folding intermediates

R. L. Baldwin, H. Roder, 1991, Current Biology.

Template-constrained somatostatin analogues: a biphenyl linker induces a type-V' turn.

W. DeGrado, R. P. Cheng, H. Roder, 2001, Journal of the American Chemical Society.