Research graph
References from Modern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life Scientists. Local targets link to admitted publications; unresolved targets remain external evidence.
Protein structure determination by X-ray crystallography
10.1007/978-1-60327-159-2_3 · 2008 · External reference
The way to NMR structures of proteins
10.1038/nsb1101-923 · 2001 · External reference
Atomic resolution cryo electron microscopy of macromolecular complexes
10.1016/b978-0-12-386507-6.00001-4 · 2011 · External reference
Protein dynamics from solution NMR: theory and applications
10.1385/cbb:37:3:187 · 2003 · External reference
10.1017/s0033583516000019
10.1017/s0033583516000019 · External reference
10.1016/j.str.2009.08.001
10.1016/j.str.2009.08.001 · External reference
Measurement and analysis of NMR residual dipolar couplings for the study of intrinsically disordered proteins
10.1007/978-1-61779-927-3_9 · 2012 · External reference
NMR spectroscopic studies of intrinsically disordered proteins at near-physiological conditions
10.1002/anie.201304272 · 2013 · External reference
10.1016/j.sbi.2013.02.007
10.1016/j.sbi.2013.02.007 · External reference
10.1021/cr400688u
10.1021/cr400688u · External reference
10.1021/jacs.6b02424
10.1021/jacs.6b02424 · External reference
10.1002/jps.21378
10.1002/jps.21378 · External reference
10.1007/s10858-013-9740-z
10.1007/s10858-013-9740-z · External reference
Transient protein-protein interactions visualized by solution NMR
10.1016/j.bbapap.2015.04.009 · 2016 · External reference
KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies
10.1007/s10858-007-9175-5 · 2007 · External reference
PONDEROSA, an automated 3D-NOESY peak picking program, enables automated protein structure determination
10.1093/bioinformatics/btr200 · 2011 · External reference
An automated system designed for large scale NMR data deposition and annotation: application to over 600 assigned chemical shift data entries to the BioMagResBank from the Riken Structural Genomics/Proteomics Initiative internal database
10.1007/s10858-012-9641-6 · 2012 · External reference
PONDEROSA-C/S: client-server based software package for automated protein 3D structure determination
10.1007/s10858-014-9855-x · 2014 · External reference
CASD-NMR 2: robust and accurate unsupervised analysis of raw NOESY spectra and protein structure determination with UNIO
10.1007/s10858-015-9934-7 · 2015 · External reference
10.1017/s0033583500004108
10.1017/s0033583500004108 · External reference
10.1016/s0021-9258(18)45665-7
10.1016/s0021-9258(18)45665-7 · External reference
10.1517/17460441.2013.779665
10.1517/17460441.2013.779665 · External reference
10.1517/17460441.2014.941801
10.1517/17460441.2014.941801 · External reference
A simplified recipe for assigning amide NMR signals using combinatorial 14N amino acid inverse-labeling
10.1007/s10969-011-9116-0 · 2011 · External reference
Selective isotopic unlabeling of proteins using metabolic precursors: application to NMR assignment of intrinsically disordered proteins
10.1002/cbic.201100678 · 2012 · External reference
10.1007/s10858-007-9158-6
10.1007/s10858-007-9158-6 · External reference
Alternate 13C–12C labeling for complete mainchain resonance assignments using C alpha direct-detection with applicability toward fast relaxing protein systems
10.1021/ja806956p · 2008 · External reference
Selectively dispersed isotope labeling for protein structure determination by magic angle spinning NMR
10.1007/s10858-013-9773-3 · 2013 · External reference
Improved labeling strategy for 13C relaxation measurements of methyl groups in proteins
10.1023/a:1018311013338 · 1997 · External reference
Selective backbone labeling of proteins using 1,2-13C2-pyruvate as carbon source
10.1007/s10858-009-9326-y · 2009 · External reference
CACA-TOCSY with alternate 13C–12C labeling: a 13Calpha direct detection experiment for mainchain resonance assignment, dihedral angle information, and amino acid type identification
10.1007/s10858-010-9410-3 · 2010 · External reference
Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production
10.1002/jmr.687 · 2005 · External reference
10.1007/s10858-008-9276-9
10.1007/s10858-008-9276-9 · External reference
Production of isotopically labeled heterologous proteins in non-E. coli prokaryotic and eukaryotic cells
10.1007/s10858-009-9377-0 · 2010 · External reference
Isotopic labeling of heterologous proteins in the yeast Pichia pastoris and Kluyveromyces lactis
10.1007/978-1-61779-480-3_2 · 2012 · External reference
10.1016/s0014-5793(98)01620-2
10.1016/s0014-5793(98)01620-2 · External reference
Cell-free protein synthesis in an autoinduction system for NMR studies of protein–protein interactions
10.1007/s10858-005-7946-4 · 2005 · External reference
10.1007/s10858-006-9127-5
10.1007/s10858-006-9127-5 · External reference
10.1038/nprot.2009.207
10.1038/nprot.2009.207 · External reference
10.1007/s10858-010-9455-3
10.1007/s10858-010-9455-3 · External reference
10.1038/nbt0202-177
10.1038/nbt0202-177 · External reference
10.1038/nature04525
10.1038/nature04525 · External reference
Incorporation of fluorescent non-natural amino acids into N-terminal tag of proteins in cell-free translation and its dependence on position and neighboring codons
10.1016/j.jbiosc.2010.01.003 · 2010 · External reference
10.1002/anie.201108275
10.1002/anie.201108275 · External reference
Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O
10.1007/s10858-011-9477-5 · 2011 · External reference
The PURE system for protein production
10.1007/978-1-62703-782-2_19 · 2014 · External reference
10.1016/j.bbamem.2010.04.010
10.1016/j.bbamem.2010.04.010 · External reference
Strategies for the cell-free expression of membrane proteins
10.1007/978-1-60327-331-2_16 · 2010 · External reference
10.1016/j.pep.2012.01.018
10.1016/j.pep.2012.01.018 · External reference
Evaluation of cell-free expression system for the production of soluble and functional human GPCR N-formyl peptide receptors
10.2174/09298665113209990043 · 2013 · External reference
Isotope labeling in mammalian cells
10.1007/978-1-61779-480-3_4 · 2012 · External reference
Mammalian expression of isotopically labeled proteins for NMR spectroscopy
10.1007/978-94-007-4954-2_11 · 2012 · External reference
10.1093/pcp/pch117
10.1093/pcp/pch117 · External reference
Automated protein NMR structure determination in crude cell-extract
10.1007/s10858-005-4519-5 · 2006 · External reference
10.1371/journal.pone.0003805
10.1371/journal.pone.0003805 · External reference
10.1371/journal.pone.0048226
10.1371/journal.pone.0048226 · External reference
A survey of metabolic changes in potato leaves by NMR-based metabolic profiling in relation to resistance to late blight disease under field conditions
10.1002/mrc.4506 · 2017 · External reference
Using “on/off” (19)F NMR/magnetic resonance imaging signals to sense tyrosine kinase/phosphatase activity in vitro and in cell lysates
10.1021/acs.analchem.6b00036 · 2016 · External reference
10.1002/pro.92
10.1002/pro.92 · External reference
Micro-scale NMR experiments for monitoring the optimization of membrane protein solutions for structural biology
10.21769/bioprotoc.1539 · 2015 · External reference
10.1007/s10858-016-0027-z
10.1007/s10858-016-0027-z · External reference
NMR-profiles of protein solutions
10.1002/bip.22348 · 2013 · External reference
10.1021/ja993743x
10.1021/ja993743x · External reference
10.1016/j.jmr.2005.08.014
10.1016/j.jmr.2005.08.014 · External reference
10.1021/bi00449a003
10.1021/bi00449a003 · External reference
Unresolved reference
1986 · External reference
CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions
10.1007/s10858-014-9815-5 · 2014 · External reference
Low-conductivity buffers for high-sensitivity NMR measurements
10.1021/ja026121b · 2002 · External reference
10.1021/bi00466a018
10.1021/bi00466a018 · External reference
Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy
10.1021/bi00487a027 · 1990 · External reference
Multidimensional NMR methods for protein structure determination
10.1080/152165401317291147 · 2001 · External reference
Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H–15N Hartmann–Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta
10.1021/bi00441a004 · 1989 · External reference
TROSY in NMR studies of the structure and function of large biological macromolecules
10.1016/j.sbi.2003.09.009 · 2003 · External reference
NMR techniques used with very large biological macromolecules in solution
10.1016/s0076-6879(05)94015-9 · 2005 · External reference
10.1073/pnas.94.23.12366
10.1073/pnas.94.23.12366 · External reference
10.1002/anie.200461794
10.1002/anie.200461794 · External reference
Protonless NMR experiments for sequence-specific assignment of backbone nuclei in unfolded proteins
10.1021/ja0582206 · 2006 · External reference
A method for C(alpha) direct-detection in protonless NMR
10.1016/j.jmr.2007.07.004 · 2007 · External reference
10.1002/prot.21577
10.1002/prot.21577 · External reference
13C–13C NOESY spectra of a 480kDa protein: solution NMR of ferritin
10.1007/s10858-007-9163-9 · 2007 · External reference
10.1007/bf00211777
10.1007/bf00211777 · External reference
10.1023/a:1008290618449
10.1023/a:1008290618449 · External reference
10.1007/bf00197809
10.1007/bf00197809 · External reference
10.1007/s10858-009-9333-z
10.1007/s10858-009-9333-z · External reference
10.1007/s10858-013-9741-y
10.1007/s10858-013-9741-y · External reference
10.1006/jmbi.1997.1284
10.1006/jmbi.1997.1284 · External reference
10.1016/s0022-2836(02)00241-3
10.1016/s0022-2836(02)00241-3 · External reference
10.1023/a:1021614115432
10.1023/a:1021614115432 · External reference
10.1023/a:1026122726574
10.1023/a:1026122726574 · External reference
Automated NMR structure calculation with CYANA
2004 · External reference
10.1007/bf00404272
10.1007/bf00404272 · External reference
PINE-SPARKY: graphical interface for evaluating automated probabilistic peak assignments in protein NMR spectroscopy
10.1093/bioinformatics/btp345 · 2009 · External reference
10.1093/bioinformatics/btu830
10.1093/bioinformatics/btu830 · External reference
Mars — robust automatic backbone assignment of proteins
10.1023/b:jnmr.0000042954.99056.ad · 2004 · External reference
Automated sequence-specific protein NMR assignment using the memetic algorithm MATCH
10.1007/s10858-008-9243-5 · 2008 · External reference
Automated amino acid side-chain NMR assignment of proteins using (13)C- and (15)N-resolved 3D [(1)H, (1)H]-NOESY
10.1007/s10858-008-9259-x · 2008 · External reference
The J-UNIO protocol for automated protein structure determination by NMR in solution
10.1007/s10858-012-9645-2 · 2012 · External reference
10.1021/ja305091n
10.1021/ja305091n · External reference
10.1007/bf00202037
10.1007/bf00202037 · External reference
Revisiting the initial rate approximation in kinetic NOE measurements
10.1016/j.jmr.2006.06.009 · 2006 · External reference
10.1016/j.pnmrs.2013.11.001
10.1016/j.pnmrs.2013.11.001 · External reference
10.1016/j.jmr.2013.11.016
10.1016/j.jmr.2013.11.016 · External reference
10.1016/j.bpj.2015.11.031
10.1016/j.bpj.2015.11.031 · External reference
Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy
10.1006/jmbi.1993.1259 · 1993 · External reference
10.1007/s10858-014-9882-7
10.1007/s10858-014-9882-7 · External reference
Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect
10.1007/s10858-009-9325-z · 2009 · External reference
PCS-based structure determination of protein-protein complexes
10.1007/s10858-010-9401-4 · 2010 · External reference
10.1371/journal.pone.0068567
10.1371/journal.pone.0068567 · External reference
Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY
10.1006/jmre.1998.1570 · 1998 · External reference
The AUDANA algorithm for automated protein 3D structure determination from NMR NOE data
10.1007/s10858-016-0036-y · 2016 · External reference
Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK
10.1007/s10858-016-0084-3 · 2017 · External reference
10.1146/annurev.bb.21.060192.001331
10.1146/annurev.bb.21.060192.001331 · External reference
10.1023/a:1008276004875
10.1023/a:1008276004875 · External reference
Measurement of 3hJNC' connectivities across hydrogen bonds in a 30kDa protein
10.1023/a:1008346517302 · 1999 · External reference
Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR
10.1006/jmbi.2002.5446 · 2002 · External reference
Vicinal proton coupling in nuclear magnetic resonance
10.1021/ja00901a059 · 1963 · External reference
10.1021/ja00070a024
10.1021/ja00070a024 · External reference
ARTSY-J: convenient and precise measurement of (3)JHNHα couplings in medium-size proteins from TROSY-HSQC spectra
10.1016/j.jmr.2016.05.001 · 2016 · External reference
An alternative 3D-NMR technique for correlating backbone N-15 with side-chain H-beta-resonances in larger proteins
1991 · External reference
10.1021/ja903772t
10.1021/ja903772t · External reference
10.1007/s10858-011-9478-4
10.1007/s10858-011-9478-4 · External reference
10.1007/s10858-015-9924-9
10.1007/s10858-015-9924-9 · External reference
10.1016/j.pnmrs.2005.10.001
10.1016/j.pnmrs.2005.10.001 · External reference
CASD-NMR: critical assessment of automated structure determination by NMR
10.1038/nmeth0909-625 · 2009 · External reference
The second round of critical assessment of automated structure determination of proteins by NMR: CASD-NMR-2013
10.1007/s10858-015-9953-4 · 2015 · External reference
Integrative NMR for biomolecular research
10.1007/s10858-016-0029-x · 2016 · External reference
10.1016/s0079-6565(97)00025-3
10.1016/s0079-6565(97)00025-3 · External reference
Automated assignment of simulated and experimental NOESY spectra of proteins by feedback filtering and self-correcting distance geometry
10.1006/jmbi.1995.0631 · 1995 · External reference
10.1023/a:1018383106236
10.1023/a:1018383106236 · External reference
10.1002/prot.20820
10.1002/prot.20820 · External reference
Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin
10.1006/jmbi.1997.1044 · 1997 · External reference
10.1093/bioinformatics/btl589
10.1093/bioinformatics/btl589 · External reference
10.1023/a:1020279503261
10.1023/a:1020279503261 · External reference
Robust and highly accurate automatic NOESY assignment and structure determination with Rosetta
10.1007/s10858-014-9832-4 · 2014 · External reference
10.1021/ja049786h
10.1021/ja049786h · External reference
10.1016/s1090-7807(02)00014-9
10.1016/s1090-7807(02)00014-9 · External reference
Crystallography & NMR system: a new software suite for macromolecular structure determination
1998 · External reference
10.1002/wcms.1121
10.1002/wcms.1121 · External reference
10.1021/acs.jctc.5b00356
10.1021/acs.jctc.5b00356 · External reference
10.1002/jcc.20945
10.1002/jcc.20945 · External reference
An automated approach for defining core atoms and domains in an ensemble of NMR-derived protein structures
10.1093/protein/10.6.737 · 1997 · External reference
10.1002/prot.24490
10.1002/prot.24490 · External reference
10.1186/1471-2105-12-170
10.1186/1471-2105-12-170 · External reference
A robust method for quantitative identification of ordered cores in an ensemble of biomolecular structures by non-linear multi-dimensional scaling using inter-atomic distance variance matrix
10.1007/s10858-013-9805-z · 2014 · External reference
10.1002/jcc.20084
10.1002/jcc.20084 · External reference
10.1107/s0907444911007281
10.1107/s0907444911007281 · External reference
10.1006/jmre.2001.2300
10.1006/jmre.2001.2300 · External reference
10.1016/0263-7855(96)00009-4
10.1016/0263-7855(96)00009-4 · External reference
Concepts and tools for NMR restraint analysis and validation
10.1002/cmr.a.20016 · 2004 · External reference
10.1016/j.pnmrs.2004.08.003
10.1016/j.pnmrs.2004.08.003 · External reference
Evaluation of the utility of NMR structures determined from minimal NOE-based restraints for structure-based drug design, using MMP-1 as an example
10.1021/bi001658s · 2000 · External reference
10.1016/j.sbi.2013.08.005
10.1016/j.sbi.2013.08.005 · External reference
PROCHECK — a program to check the stereochemical quality of protein structures
10.1107/s0021889892009944 · 1993 · External reference
10.1007/bf00228148
10.1007/bf00228148 · External reference
10.1093/nar/gkm216
10.1093/nar/gkm216 · External reference
High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium
10.1023/a:1018308717741 · 1997 · External reference
10.1038/4176
10.1038/4176 · External reference
10.1023/a:1011263920003
10.1023/a:1011263920003 · External reference
10.1146/annurev.biophys.33.110502.140306
10.1146/annurev.biophys.33.110502.140306 · External reference
10.1038/nprot.2008.36
10.1038/nprot.2008.36 · External reference
Advances in the REDCAT software package
10.1186/1471-2105-14-302 · 2013 · External reference
10.1007/s10858-005-2601-7
10.1007/s10858-005-2601-7 · External reference
10.1007/s10858-007-9215-1
10.1007/s10858-007-9215-1 · External reference
Domain orientation and dynamics in multidomain proteins from residual dipolar couplings
10.1021/bi9905213 · 1999 · External reference
10.1006/jmbi.1999.3133
10.1006/jmbi.1999.3133 · External reference
10.1007/s00249-011-0720-5
10.1007/s00249-011-0720-5 · External reference
10.1016/j.pnmrs.2014.05.003
10.1016/j.pnmrs.2014.05.003 · External reference
Solution NMR in structural genomics
10.1016/j.sbi.2006.08.002 · 2006 · External reference
10.1586/14789450.5.4.589
10.1586/14789450.5.4.589 · External reference
10.1007/s00249-008-0367-z
10.1007/s00249-008-0367-z · External reference
10.1017/s0033583510000326
10.1017/s0033583510000326 · External reference
10.1073/pnas.0800256105
10.1073/pnas.0800256105 · External reference
De novo protein structure generation from incomplete chemical shift assignments
10.1007/s10858-008-9288-5 · 2009 · External reference
Automated structure determination of proteins with the SAIL-FLYA NMR method
10.1038/nprot.2007.423 · 2007 · External reference
10.1007/s10858-009-9339-6
10.1007/s10858-009-9339-6 · External reference
Differential isotope-labeling for Leu and Val residues in a protein by E. coli cellular expression using stereo-specifically methyl labeled amino acids
10.1007/s10858-013-9784-0 · 2013 · External reference
Highly efficient residue-selective labeling with isotope-labeled Ile, Leu, and Val using a new auxotrophic E. coli strain
10.1007/s10858-016-0042-0 · 2016 · External reference
10.1006/jmbi.1996.0603
10.1006/jmbi.1996.0603 · External reference
Production and incorporation of N-15, C-13, H-2 (H-1-delta 1 methyl) isoleucine into proteins for multidimensional NMR studies
10.1021/ja9706514 · 1997 · External reference
A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteins
10.1023/a:1008393201236 · 1999 · External reference
10.1021/ja030345s
10.1021/ja030345s · External reference
An isotope labeling strategy for methyl TROSY spectroscopy
10.1023/b:jnmr.0000013824.93994.1f · 2004 · External reference
Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins
10.1002/anie.200905660 · 2010 · External reference
10.1007/s10858-005-4425-x
10.1007/s10858-005-4425-x · External reference
Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein NMR
10.1016/j.jmr.2005.10.007 · 2006 · External reference
Rapid heteronuclear single quantum correlation NMR spectra at natural abundance
10.1021/ja411588d · 2014 · External reference
10.1021/ja044032o
10.1021/ja044032o · External reference
10.1021/ja902012x
10.1021/ja902012x · External reference
10.1007/s10858-016-0074-5
10.1007/s10858-016-0074-5 · External reference
Detecting the “afterglow” of 13C NMR in proteins using multiple receivers
10.1021/ja1080025 · 2010 · External reference
Parallel acquisition of 3D-HA(CA)NH and 3D-HACACO spectra
10.1007/s10858-013-9735-9 · 2013 · External reference
10.1016/j.jmr.2013.12.002
10.1016/j.jmr.2013.12.002 · External reference
Improving resolution in multidimensional NMR using random quadrature detection with compressed sensing reconstruction
10.1007/s10858-016-0062-9 · 2017 · External reference
Sparse multidimensional iterative lineshape-enhanced (SMILE) reconstruction of both non-uniformly sampled and conventional NMR data
2016 · External reference
A non-uniform sampling approach enables studies of dilute and unstable proteins
2017 · External reference
10.1002/0471721204.ch5
10.1002/0471721204.ch5 · External reference
10.1126/science.1183649
10.1126/science.1183649 · External reference
Building macromolecular assemblies by information-driven docking: introducing the HADDOCK multibody docking server
10.1074/mcp.m000051-mcp201 · 2010 · External reference
Accelerated NMR spectroscopy by using compressed sensing
10.1002/anie.201100370 · 2011 · External reference
10.1371/journal.pbio.1001244
10.1371/journal.pbio.1001244 · External reference
10.1021/ar700132n
10.1021/ar700132n · External reference
10.1017/s0033583514000122
10.1017/s0033583514000122 · External reference
10.1021/ja026939x
10.1021/ja026939x · External reference
10.1016/j.jmb.2015.09.014
10.1016/j.jmb.2015.09.014 · External reference
10.1016/j.str.2015.05.013
10.1016/j.str.2015.05.013 · External reference