Published in J Biomol NMR on November 01, 1991
Semisynthesis of a segmental isotopically labeled protein splicing precursor: NMR evidence for an unusual peptide bond at the N-extein-intein junction. Proc Natl Acad Sci U S A (2004) 1.51
Branched intermediate formation stimulates peptide bond cleavage in protein splicing. Nat Chem Biol (2010) 1.22
A set of HNCO-based experiments for measurement of residual dipolar couplings in 15N, 13C, (2H)-labeled proteins. J Biomol NMR (2000) 1.21
The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy. J Am Chem Soc (2010) 1.03
Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments. J Magn Reson (2009) 1.02
HA-detected experiments for the backbone assignment of intrinsically disordered proteins. J Biomol NMR (2010) 1.01
Angular dependence of 1J(Ni,Calphai) and 2J(Ni,Calpha(i-1)) coupling constants measured in J-modulated HSQCs. J Biomol NMR (2002) 0.99
Intraresidual HNCA: an experiment for correlating only intraresidual backbone resonances. J Biomol NMR (2002) 0.95
Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins. J Biomol NMR (2011) 0.93
A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein. Protein Sci (2014) 0.88
Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings. J Biomol NMR (2000) 0.88
Simultaneous detection and deconvolution of congested NMR spectra containing three isotopically labeled species. J Am Chem Soc (2008) 0.86
Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment. J Biomol NMR (2012) 0.84
A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR experiment and quantum chemical calculations. J Biomol NMR (2005) 0.82
Structural dependencies of protein backbone 2JNC' couplings. Protein Sci (2008) 0.82
HNCA+, HNCO+, and HNCACB+ experiments: improved performance by simultaneous detection of orthogonal coherence transfer pathways. J Biomol NMR (2014) 0.82
Pairwise NMR experiments for the determination of protein backbone dihedral angle Phi based on cross-correlated spin relaxation. J Biomol NMR (2007) 0.80
Bridge over troubled proline: assignment of intrinsically disordered proteins using (HCA)CON(CAN)H and (HCA)N(CA)CO(N)H experiments concomitantly with HNCO and i(HCA)CO(CA)NH. J Biomol NMR (2013) 0.80
A 4D TROSY-based pulse scheme for correlating 1HNi,15Ni,13Calphai,13C'i-1 chemical shifts in high molecular weight, 15N,13C, 2H labeled proteins. J Biomol NMR (1999) 0.80
H-bonding mediates polarization of peptide groups in folded proteins. Protein Sci (2003) 0.79
Alternative E.COSY techniques for the measurement of 3J(C (i) (') (-1),C (i) (beta) ) and (3) J(H (i) (N) ,C (i) (beta) ) coupling constants in proteins. J Biomol NMR (1999) 0.79
Pulse schemes for the measurement of 3JC'C gamma and 3JNC gamma scalar couplings in 15N,13C uniformly labeled proteins. J Biomol NMR (1997) 0.78
Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in solution. J Biomol NMR (1998) 0.78
Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [(15)N,(1)H]-TROSY-HNC experiment. J Biomol NMR (2003) 0.78
An intraresidual i(HCA)CO(CA)NH experiment for the assignment of main-chain resonances in 15N, 13C labeled proteins. J Biomol NMR (2009) 0.78
HNCAN pulse sequences for sequential backbone resonance assignment across proline residues in perdeuterated proteins. J Biomol NMR (2000) 0.76
Improved accuracy in measuring one-bond and two-bond (15)N, (13)C (α) coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy. J Biomol NMR (2011) 0.76
Time-shared experiments for efficient assignment of triple-selectively labeled proteins. J Magn Reson (2014) 0.75
A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP. J Biomol NMR (2016) 0.75
NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR (1995) 93.94
Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR (1999) 26.99
Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry (1989) 10.50
Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science (1997) 9.39
Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science (1992) 6.16
Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. J Biomol NMR (1993) 6.02
Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J Magn Reson (1998) 5.83
A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry (1990) 5.01
Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry (1992) 4.25
Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. Biochem Biophys Res Commun (2001) 3.46
The CD4 determinant for downregulation by HIV-1 Nef directly binds to Nef. Mapping of the Nef binding surface by NMR. Biochemistry (1996) 3.41
Solution structure of calcium-free calmodulin. Nat Struct Biol (1995) 3.36
Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains. Nat Struct Biol (2001) 3.18
The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nat Struct Biol (1996) 2.94
Spectral density function mapping using 15N relaxation data exclusively. J Biomol NMR (1995) 2.77
A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles. J Biomol NMR (2001) 2.64
Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Protein Sci (1993) 2.61
Protein dynamics from NMR. Nat Struct Biol (2000) 2.52
Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution. Nat Struct Biol (1997) 2.51
Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J Biomol NMR (1994) 2.50
Flexibility and function in HIV-1 protease. Nat Struct Biol (1995) 2.49
Recommendations for the presentation of NMR structures of proteins and nucleic acids. J Mol Biol (1998) 2.42
A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J Magn Reson (1998) 2.38
Assignment of the 31P and 1H resonances in oligonucleotides by two-dimensional NMR spectroscopy. FEBS Lett (1986) 2.28
Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution. Science (1990) 2.28
Solution structure of cyanovirin-N, a potent HIV-inactivating protein. Nat Struct Biol (1998) 2.19
Refined solution structure and backbone dynamics of HIV-1 Nef. Protein Sci (1997) 2.09
Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function. Structure (1999) 1.98
Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxation measurements at two magnetic fields. J Biomol NMR (1996) 1.94
Use of 31P nuclear magnetic resonance spectroscopy and 14C fluorography in studies of glycolysis and regulation of pyruvate kinase in Streptococcus lactis. J Bacteriol (1984) 1.87
Preparation of intact monomeric collagen from rat tail tendon and skin and the structure of the nonhelical ends in solution. J Biol Chem (1976) 1.85
Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements. Eur J Biochem (1995) 1.81
Climate change and the integrity of science. Science (2010) 1.80
Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor. Nat Struct Biol (1994) 1.80
Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules. J Biomol NMR (1998) 1.78
Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C-labeled protein using constant-time evolution. J Biomol NMR (1991) 1.74
Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times. J Magn Reson (2000) 1.73
Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat Struct Biol (1997) 1.70
A two-dimensional NMR study of the antimicrobial peptide magainin 2. FEBS Lett (1988) 1.69
1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma. Biochemistry (1992) 1.66
Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy. Biochemistry (1990) 1.65
2H NMR study of molecular motion in collagen fibrils. Nature (1980) 1.64
Solution structure of DinI provides insight into its mode of RecA inactivation. Protein Sci (2000) 1.61
Measurement of amide proton exchange rates and NOEs with water in 13C/15N-enriched calcineurin B. J Biomol NMR (1993) 1.60
A simple and sensitive experiment for measurement of JCC couplings between backbone carbonyl and methyl carbons in isotopically enriched proteins. J Biomol NMR (1993) 1.59
Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease. Biochemistry (1992) 1.56
Solution structure and dynamics of linked cell attachment modules of mouse fibronectin containing the RGD and synergy regions: comparison with the human fibronectin crystal structure. J Mol Biol (1998) 1.53
Investigation of labeled amino acid side-chain motion in collagen using 13C nuclear magnetic resonance. J Mol Biol (1980) 1.52
Morphology of three lyotropic liquid crystalline biological NMR media studied by translational diffusion anisotropy. J Am Chem Soc (2001) 1.52
Sequential backbone assignment of isotopically enriched proteins in D2O by deuterium-decoupled HA(CA)N and HA(CACO)N. J Biomol NMR (1995) 1.51
Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values. J Biomol NMR (1999) 1.50
Four-dimensional 13C/13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1 beta. Biochemistry (1991) 1.42
Quantitative measurement of small through-hydrogen-bond and 'through-space' 1H-113Cd and 1H-199Hg J couplings in metal-substituted rubredoxin from Pyrococcus furiosus. J Biomol NMR (1992) 1.40
Characterization of molecular alignment in aqueous suspensions of Pf1 bacteriophage. J Biomol NMR (2001) 1.39
Recommendations for the presentation of NMR structures of proteins and nucleic acids--IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy. Eur J Biochem (1998) 1.37
Characterization of leucine side-chain reorientation in collagen-fibrils by solid-state 2H NMR. Proc Natl Acad Sci U S A (1982) 1.36
NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors. Biochemistry (1994) 1.35
13C/1H high power double magnetic resonance investigation of collagen backbone motion in fibrils and in solution. J Mol Biol (1979) 1.34
Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272. Biochemistry (1996) 1.32
Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings. J Biomol NMR (2000) 1.30
Spin-locked multiple quantum coherence for signal enhancement in heteronuclear multidimensional NMR experiments. J Biomol NMR (1995) 1.30
Measurement of the exchange rates of rapidly exchanging amide protons: application to the study of calmodulin and its complex with a myosin light chain kinase fragment. J Biomol NMR (1991) 1.29
Intracellular polymerization of sickle hemoglobin. Effects of cell heterogeneity. J Clin Invest (1983) 1.28
15N-labeled Escherichia coli tRNAfMet, tRNAGlu, tRNATyr, and tRNAPhe. Double resonance and two-dimensional NMR of N1-labeled pseudouridine. J Biol Chem (1985) 1.27
Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy. Biochemistry (1991) 1.24
Investigation of molecular motion of proteoglycans in cartilage by 13C magnetic resonance. J Biol Chem (1977) 1.24
Measurement of dipolar couplings for methylene and methyl sites in weakly oriented macromolecules and their use in structure determination. J Magn Reson (1998) 1.22
Two-dimensional nuclear magnetic resonance spectroscopy. Science (1986) 1.21
Escherichia coli K51 and K93 capsular polysaccharides are crossreactive with the group A capsular polysaccharide of Neisseria meningitidis. Immunochemical, biological, and epidemiological studies. J Exp Med (1985) 1.18
Measurement of homonuclear proton couplings from regular 2D COSY spectra. J Magn Reson (2001) 1.18
Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution. J Biomol NMR (1999) 1.18
Measurement of 3hJNC' connectivities across hydrogen bonds in a 30 kDa protein. J Biomol NMR (1999) 1.17
Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix. Biochemistry (1991) 1.17
13C Magnetic resonance evidence for anisotropic molecular motion in collagen fibrils. J Mol Biol (1976) 1.17
Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy. Protein Sci (1996) 1.16
Determination of deoxyhemoglobin S polymer in sickle erythrocytes upon deoxygenation. Proc Natl Acad Sci U S A (1980) 1.16
A powerful method of sequential proton resonance assignment in proteins using relayed 15N-1H multiple quantum coherence spectroscopy. FEBS Lett (1989) 1.15
Chi 1 angle information from a simple two-dimensional NMR experiment that identifies trans 3JNC gamma couplings in isotopically enriched proteins. J Biomol NMR (1997) 1.15
The solution structure of ribosomal protein S4 delta41 reveals two subdomains and a positively charged surface that may interact with RNA. EMBO J (1998) 1.14
A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA. Genes Dev (2001) 1.14
Folded monomer of HIV-1 protease. J Biol Chem (2001) 1.12
High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA. Nat Struct Biol (1997) 1.11
Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy. Biochemistry (2000) 1.11
Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS. J Biomol NMR (1993) 1.11
Identification and localization of bound internal water in the solution structure of interleukin 1 beta by heteronuclear three-dimensional 1H rotating-frame Overhauser 15N-1H multiple quantum coherence NMR spectroscopy. Biochemistry (1990) 1.09
Three-dimensional solution structure of Acanthamoeba profilin-I. J Cell Biol (1993) 1.06
Absorption mode two-dimensional NOE spectroscopy of exchangeable protons in oligonucleotides. FEBS Lett (1987) 1.06
Detection of cis and trans X-Pro peptide bonds in proteins by 13C NMR: application to collagen. Proc Natl Acad Sci U S A (1984) 1.05
Solid state NMR studies of protein internal dynamics. Annu Rev Biophys Bioeng (1984) 1.05
Measurement of one-bond 15N-13C' dipolar couplings in medium sized proteins. J Biomol NMR (2000) 1.05
1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques. Biochemistry (1991) 1.04
Multiple quantum two-dimensional 1H--15N nuclear magnetic resonance spectroscopy: chemical shift correlation maps for exchangeable imino protons of Escherichia coli tRNAMetf in water. Proc Natl Acad Sci U S A (1983) 1.03
Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2. Biochemistry (1996) 1.03
Characterization of native and recombinant bone sialoprotein: delineation of the mineral-binding and cell adhesion domains and structural analysis of the RGD domain. J Bone Miner Res (1997) 1.02
Solid state 13C NMR study of collagen molecular dynamics in hard and soft tissues. J Biol Chem (1983) 1.02