Published in Protein Sci on March 01, 1998
Multiple diverse ligands binding at a single protein site: a matter of pre-existing populations. Protein Sci (2002) 3.01
Hydrogen exchange and mass spectrometry: A historical perspective. J Am Soc Mass Spectrom (2006) 2.78
Protein folding: the stepwise assembly of foldon units. Proc Natl Acad Sci U S A (2005) 2.29
Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry. Proc Natl Acad Sci U S A (2003) 2.09
Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase. Proc Natl Acad Sci U S A (2004) 1.73
Protein folding and misfolding: mechanism and principles. Q Rev Biophys (2008) 1.68
Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. Proc Natl Acad Sci U S A (2005) 1.67
Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange. Proc Natl Acad Sci U S A (2001) 1.66
Protein hydrogen exchange mechanism: local fluctuations. Protein Sci (2003) 1.63
The hydration of amides in helices; a comprehensive picture from molecular dynamics, IR, and NMR. Protein Sci (2003) 1.62
Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry. Proc Natl Acad Sci U S A (2009) 1.50
An amino acid code for protein folding. Proc Natl Acad Sci U S A (2001) 1.45
Cytochrome c folding pathway: kinetic native-state hydrogen exchange. Proc Natl Acad Sci U S A (2002) 1.37
The chemistry and biochemistry of heme c: functional bases for covalent attachment. Nat Prod Rep (2008) 1.37
On the mechanisms of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor binding to glutamate and kainate. J Biol Chem (2010) 1.18
Mapping protein energy landscapes with amide hydrogen exchange and mass spectrometry: I. A generalized model for a two-state protein and comparison with experiment. Protein Sci (2005) 1.08
The role of backbone conformational heat capacity in protein stability: temperature dependent dynamics of the B1 domain of Streptococcal protein G. Protein Sci (2000) 1.04
Can allosteric regulation be predicted from structure? Proc Natl Acad Sci U S A (2000) 1.01
ETD in a traveling wave ion guide at tuned Z-spray ion source conditions allows for site-specific hydrogen/deuterium exchange measurements. J Am Soc Mass Spectrom (2011) 1.01
Hydrogen/deuterium exchange and mass spectrometric analysis of a protein containing multiple disulfide bonds: Solution structure of recombinant macrophage colony stimulating factor-beta (rhM-CSFbeta). Protein Sci (2002) 1.01
Heme attachment motif mobility tunes cytochrome c redox potential. Biochemistry (2007) 1.01
Effect of heavy water on protein flexibility. Biophys J (2002) 0.97
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra. Protein Sci (2000) 0.97
Hydrogen exchange and ligand binding: ligand-dependent and ligand-independent protection in the Src SH3 domain. Protein Sci (2004) 0.94
Hydration state of single cytochrome c monolayers on soft interfaces via neutron interferometry. Biophys J (2001) 0.93
Prediction of native-state hydrogen exchange from perfectly funneled energy landscapes. J Am Chem Soc (2011) 0.92
Flexible xxx-asp/asn and gly-xxx residues of equine cytochrome C in matrix-assisted laser desorption/ionization in-source decay mass spectrometry. Mass Spectrom (Tokyo) (2012) 0.87
Computing H/D-exchange rates of single residues from data of proteolytic fragments. BMC Bioinformatics (2010) 0.87
Residue-specific side-chain packing determines the backbone dynamics of transmembrane model helices. Biophys J (2010) 0.84
Insights into the role of the histidines in the structure and stability of cytochrome c. J Biol Inorg Chem (2005) 0.83
Fast structural dynamics in reduced and oxidized cytochrome c. Protein Sci (2009) 0.83
Folding mechanism of reduced Cytochrome c: equilibrium and kinetic properties in the presence of carbon monoxide. J Mol Biol (2008) 0.81
Stability and fluctuations of amide hydrogen bonds in a bacterial cytochrome c: a molecular dynamics study. J Biol Inorg Chem (2005) 0.81
How amide hydrogens exchange in native proteins. Proc Natl Acad Sci U S A (2015) 0.81
Ultrafast hydrogen exchange reveals specific structural events during the initial stages of folding of cytochrome c. J Am Chem Soc (2013) 0.79
Protein stability and mutations in the axial methionine loop of a minimal cytochrome c. J Biol Inorg Chem (2004) 0.79
Functional dynamics of hexameric helicase probed by hydrogen exchange and simulation. Biophys J (2014) 0.79
Defining the Apoptotic Trigger: THE INTERACTION OF CYTOCHROME c AND CARDIOLIPIN. J Biol Chem (2015) 0.78
Access of hydrogen-radicals to the peptide-backbone as a measure for estimating the flexibility of proteins using matrix-assisted laser desorption/ionization mass spectrometry. Int J Mol Sci (2014) 0.77
Prediction of Residue Status to Be Protected or Not Protected From Hy-drogen Exchange Using Amino Acid Sequence Only. Open Biochem J (2008) 0.77
Estimation of Hydrogen-Exchange Protection Factors from MD Simulation Based on Amide Hydrogen Bonding Analysis. J Chem Inf Model (2015) 0.76
Increased dynamics in the 40-57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation. Sci Rep (2016) 0.76
Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution. Sci Rep (2017) 0.75
Analysis of Flexibility of Proteins by means of Positive and Negative Ion MALDI In-Source Decay Mass Spectrometry. Mass Spectrom (Tokyo) (2014) 0.75
Non-equilibrium hydrogen exchange for determination of H-bond strength and water accessibility in solid proteins. J Biomol NMR (2017) 0.75
Conformational preludes to the latency transition in PAI-1 as determined by atomistic computer simulations and hydrogen/deuterium-exchange mass spectrometry. Sci Rep (2017) 0.75
Solvent-accessible surfaces of proteins and nucleic acids. Science (1983) 11.29
Hydrogen exchange in proteins. Adv Protein Chem (1966) 7.02
Primary structure effects on peptide group hydrogen exchange. Biochemistry (1972) 4.08
Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nat Struct Biol (1996) 2.96
Hydrogen exchange and the dynamic structure of proteins. Mol Cell Biochem (1982) 2.74
Stable submolecular folding units in a non-compact form of cytochrome c. J Mol Biol (1991) 2.67
Protein stability parameters measured by hydrogen exchange. Proteins (1994) 2.55
Mechanisms and uses of hydrogen exchange. Curr Opin Struct Biol (1996) 2.48
Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. J Mol Biol (1996) 2.29
Free energy balance in protein folding. Adv Protein Chem (1995) 2.10
Hydrogen exchange in native and denatured states of hen egg-white lysozyme. Proteins (1992) 1.79
Future directions in folding: the multi-state nature of protein structure. Proteins (1996) 1.70
Hydrogen exchange kinetics and internal motions in proteins and nucleic acids. Annu Rev Biophys Bioeng (1979) 1.50
Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide. Biochemistry (1991) 1.46
Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C. Proc Natl Acad Sci U S A (1997) 1.42
Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange. Proc Natl Acad Sci U S A (1995) 1.29
Proton resonance assignments of horse ferrocytochrome c. Biochemistry (1989) 1.25
Assessment of stability differences in the protein G B1 and B2 domains from hydrogen-deuterium exchange: comparison with calorimetric data. Biochemistry (1995) 1.16
Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase. Biochemistry (1995) 1.13
Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing. Biochemistry (1994) 1.10
Determination of the rate constants k1 and k2 of the Linderström-Lang model for protein amide hydrogen exchange. A study of the individual amides in hen egg-white lysozyme. J Mol Biol (1993) 1.09
Solution structure of horse heart ferricytochrome c and detection of redox-related structural changes by high-resolution 1H NMR. Biochemistry (1996) 1.08
Protein hydrogen exchange in denaturant: quantitative analysis by a two-process model. Biochemistry (1994) 1.05
The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c. J Mol Biol (1994) 1.05
Studies of hydrogen exchange in proteins. I. The exchange kinetics of bovine carbonic anhydrase. J Biol Chem (1968) 1.03
A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions. Proc Natl Acad Sci U S A (1996) 0.99
Local perturbations by ligand binding of hydrogen deuterium exchange kinetics in a four-helix bundle protein, acyl coenzyme A binding protein (ACBP). J Mol Biol (1995) 0.97
Hydrogen exchange in Pseudomonas cytochrome c-551. Biochim Biophys Acta (1992) 0.97
Amide proton exchange rates of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochrome c. Protein Sci (1993) 0.96
Protein complexes studied by NMR spectroscopy. Curr Opin Biotechnol (1996) 0.95
Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study. J Biomol NMR (1991) 0.94
Disulfide mutants of barnase. II: Changes in structure and local stability identified by hydrogen exchange. J Mol Biol (1995) 0.88
Studies of hydrogen exchange in proteins. II. The reversible thermal unfolding of chymotrypsinogen A as studied by exchange kinetics. J Biol Chem (1969) 0.84
Mutations Pro----Ala-35 and Tyr----Phe-75 of Rhodobacter capsulatus ferrocytochrome c2 affect protein backbone dynamics: measurements of individual amide proton exchange rate constants by 1H-15N HMQC spectroscopy. Biochemistry (1992) 0.82
Primary structure effects on peptide group hydrogen exchange. Proteins (1993) 10.79
Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q Rev Biophys (1983) 9.14
Protein folding intermediates: native-state hydrogen exchange. Science (1995) 5.91
Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature (1988) 4.57
Primary structure effects on peptide group hydrogen exchange. Biochemistry (1972) 4.08
Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex. Nat Struct Biol (2000) 3.49
Fast events in protein folding initiated by nanosecond laser photolysis. Proc Natl Acad Sci U S A (1993) 3.45
Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu Rev Biophys Biomol Struct (1992) 3.34
Hydrogen exchange. Annu Rev Biochem (1972) 3.31
Isotope effects in peptide group hydrogen exchange. Proteins (1993) 3.21
The barriers in protein folding. Nat Struct Biol (1994) 2.79
Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy. Proc Natl Acad Sci U S A (2000) 2.75
Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nat Struct Biol (1996) 2.71
Stable submolecular folding units in a non-compact form of cytochrome c. J Mol Biol (1991) 2.67
Design and synthesis of multi-haem proteins. Nature (1994) 2.59
Protein stability parameters measured by hydrogen exchange. Proteins (1994) 2.55
Mechanisms and uses of hydrogen exchange. Curr Opin Struct Biol (1996) 2.48
Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands. Biochemistry (1994) 2.23
Protein hydrogen exchange studied by the fragment separation method. Anal Biochem (1985) 2.12
Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nat Struct Biol (1998) 2.12
Nature of the open state in long polynucleotide double helices: possibility of soliton excitations. Proc Natl Acad Sci U S A (1980) 2.10
Microscopic origins of entropy, heat capacity and the glass transition in proteins. Nature (2001) 2.09
Water magnetic relaxation dispersion in biological systems: the contribution of proton exchange and implications for the noninvasive detection of cartilage degradation. Proc Natl Acad Sci U S A (2001) 2.07
Hydrogen exchange: the modern legacy of Linderstrøm-Lang. Protein Sci (1997) 2.06
Measurement of structural and free energy changes in hemoglobin by hydrogen exchange methods. Ann N Y Acad Sci (1975) 2.04
Insights into the local residual entropy of proteins provided by NMR relaxation. Protein Sci (1996) 2.03
Measurement and calibration of peptide group hydrogen-deuterium exchange by ultraviolet spectrophotometry. Anal Biochem (1979) 2.01
Structural and kinetic characterization of early folding events in beta-lactoglobulin. Nat Struct Biol (2001) 1.97
Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry (1993) 1.96
Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins (1996) 1.95
Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR. Biochemistry (1990) 1.94
Base-pair opening and closing reactions in the double helix. A stopped-flow hydrogen exchange study in poly(rA).poly(rU). J Mol Biol (1979) 1.91
Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry (1992) 1.90
Open states in native polynucleotides. I. Hydrogen-exchange study of adenine-containing double helices. J Mol Biol (1975) 1.88
A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale. Biophys J (1998) 1.87
An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR. Science (1990) 1.86
Fast internal main-chain dynamics of human ubiquitin. Biochemistry (1992) 1.84
Open states in native polynucleotides. II. Hydrogen-exchange study of cytosine-containing double helices. J Mol Biol (1975) 1.84
Chaperonin function: folding by forced unfolding. Science (1999) 1.83
Climate change and the integrity of science. Science (2010) 1.80
The burst phase in ribonuclease A folding and solvent dependence of the unfolded state. Nat Struct Biol (1998) 1.78
Biochemistry without oxygen. Anal Biochem (1987) 1.77
Early hydrogen-bonding events in the folding reaction of ubiquitin. Proc Natl Acad Sci U S A (1992) 1.76
Oligomerization of the integrin alphaIIbbeta3: roles of the transmembrane and cytoplasmic domains. Proc Natl Acad Sci U S A (2001) 1.74
Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate. Nat Struct Biol (2001) 1.72
Future directions in folding: the multi-state nature of protein structure. Proteins (1996) 1.70
Solution structure and dynamics of a de novo designed three-helix bundle protein. Proc Natl Acad Sci U S A (1999) 1.69
Two-dimensional 1H NMR studies of cytochrome c: hydrogen exchange in the N-terminal helix. Biochemistry (1986) 1.69
Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing. Nat Struct Biol (1999) 1.69
Squalamine: an aminosterol antibiotic from the shark. Proc Natl Acad Sci U S A (1993) 1.67
Thermodynamic parameters from hydrogen exchange measurements. Methods Enzymol (1995) 1.63
Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. Methods Enzymol (1989) 1.63
Experimental study of the protein folding landscape: unfolding reactions in cytochrome c. J Mol Biol (1999) 1.59
The role of helix formation in the folding of a fully alpha-helical coiled coil. Proteins (1996) 1.58
Two-dimensional 1H NMR study of human ubiquitin: a main chain directed assignment and structure analysis. Biochemistry (1987) 1.52
Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry (1998) 1.51
De novo proteins as models of radical enzymes. Biochemistry (1999) 1.51
Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation. Neuroreport (1999) 1.49
Hydrogen-tritium exchange. Methods Enzymol (1972) 1.48
An amino acid code for protein folding. Proc Natl Acad Sci U S A (2001) 1.45
Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C. Proc Natl Acad Sci U S A (1997) 1.42
Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitor. Biochemistry (1985) 1.39
Main-chain-directed strategy for the assignment of 1H NMR spectra of proteins. Biochemistry (1987) 1.38
Evidence for an unfolding and refolding pathway in cytochrome c. Nat Struct Biol (1998) 1.38
Ultrafast signals in protein folding and the polypeptide contracted state. Proc Natl Acad Sci U S A (1997) 1.35
Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry (1996) 1.34
Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease. Biochemistry (1997) 1.34
Xeroderma pigmentosum, Cockayne syndrome and trichothiodystrophy: do the genes explain the diseases? Trends Genet (1996) 1.31
Fourth rank immobile nucleic acid junctions. J Biomol Struct Dyn (1983) 1.30
NMR analysis of DNA junctions: imino proton NMR studies of individual arms and intact junction. Biochemistry (1985) 1.29
An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core. Biochemistry (1997) 1.28
Comparison of the magnetic properties of deoxy- and photodissociated myoglobin. Proc Natl Acad Sci U S A (1984) 1.28
Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature. Biochemistry (1985) 1.28
Abnormal kinetics of DNA synthesis in ultraviolet light-irradiated cells from patients with Cockayne's syndrome. Cancer Res (1979) 1.27
Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence. Biochemistry (1983) 1.27
Quenching of room temperature protein phosphorescence by added small molecules. Biochemistry (1988) 1.27
Hydrogen exchange study of some polynucleotides and transfer RNA. J Mol Biol (1972) 1.27
Lay health advisors: a strategy for getting the word out about breast cancer. Health Educ Behav (1997) 1.26
Proton resonance assignments of horse ferrocytochrome c. Biochemistry (1989) 1.25
A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c. Biochemistry (1993) 1.24
Solution structure of apocytochrome b562. Nat Struct Biol (1994) 1.24
Nanosecond flash photolysis study of carbon monoxide binding to the beta chain of hemoglobin Zürich [beta 63(E7)His leads to Arg]. Proc Natl Acad Sci U S A (1983) 1.23
Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles. Biochemistry (1997) 1.23
Individual breathing reactions measured in hemoglobin by hydrogen exchange methods. Biophys J (1980) 1.22