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Overcoming the overlap problem in the assignment of proton NMR spectra of larger proteins by use of three-dimensional heteronuclear proton-nitrogen-15 Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1.beta.
Dominique Marion, Paul C. Driscoll, Lewis E. Kay, Paul T. Wingfield, Ad Bax, Angela M. Gronenborn and G. Marius Clore Biochemistry 28(15) 6150 (1989) https://doi.org/10.1021/bi00441a004
Electrostatic interactions in wild-type and mutant recombinant human myoglobins
Two‐dimensional 1H‐nmr study of synthetic peptides containing the main immunogenic region of the Torpedo acetylcholine receptor
M. T. Cung, M. Marraud, I. Hadjidakis, E. Bairaktari, C. Sakarellos, A. Kokla and S. Tzartos Biopolymers 28(1) 465 (1989) https://doi.org/10.1002/bip.360280141
Conformational analysis of cyclic peptides in solution
Proton NMR studies of bovine and porcine phospholipase A2: assignment of aromatic resonances and evidence for a conformational equilibrium in solution
J. Fisher, W. U. Primrose, G. C. K. Roberts, N. Dekker, R. Boelens, R. Kaptein and A. J. Slotboom Biochemistry 28(14) 5939 (1989) https://doi.org/10.1021/bi00440a034
Multinuclear NMR studies of DNA hairpins. 1. Structure and dynamics of d(CGCGTTGTTCGCG)
A structural study of phosphate‐methylated d(CpG)n and d(GpC)n DNA oligomers. Implications of phosphate shielding for the isomerisation of B‐DNA into Z‐DNA
Peter J. L. M. Quaedflieg, Leo H. Koole, Marcel H. P. van Genderen and Henk M. Buck Recueil des Travaux Chimiques des Pays-Bas 108(11) 421 (1989) https://doi.org/10.1002/recl.19891081107
1H‐n.m.r. studies of squash seed trypsin inhibitor
High-resolution NMR studies of fibrinogen-like peptides in solution: structure of a thrombin-bound peptide corresponding to residues 7-16 of the A.alpha. chain of human fibrinogen
Preliminary assignments of the aromatic and some methyl group resonances of the 1H‐NMR spectrum of the oxidized form of uteroglobin
Nadège JAMIN, Pierre ROY, Françoise FRIDLANSKY, Muriel DELEPIERRE, Edwin MILGROM, Bernard P. ROQUES and Jean‐Paul MORNON European Journal of Biochemistry 183(1) 219 (1989) https://doi.org/10.1111/j.1432-1033.1989.tb14916.x
Improved resolution in 1H‐detected 1H‐15N correlation experiments
1H n.m.r. conformational studies on the C‐terminal octapeptide of oxyntomodulin, a β‐turn locked by a salt bridge
ANDRÉ AUMELAS, MARIE‐PASCALE AUDOUSSET‐PUECH, ANNIE HEITZ, DOMINIQUE BATAILLE and JEAN MARTINEZ International Journal of Peptide and Protein Research 34(4) 268 (1989) https://doi.org/10.1111/j.1399-3011.1989.tb01574.x
Magnetization‐transfer n.m.r. investigation of the hydrogen exchang in H20 of the peptide fragment B23‐B29 of insulin
Peptidkonformationen, 50. Synthese und Konformationsanalyse von cyclischen Alanin‐Analogen des Thymopoietins durch NMR‐Spektroskopie und Molecular‐Dynamics‐Rechnungen im Vakuum und in Lösung
Intrauterine fetal brain NMR spectroscopy: 1H and 31P studies in rats
Tsutomu Nakada, Ingrid L. Kwee, Nobuyuki Suzuki and Kiyohiro Houkin Magnetic Resonance in Medicine 12(2) 172 (1989) https://doi.org/10.1002/mrm.1910120204
Conformations of dehydrophenylalanine containing peptides: nmr studies of an acyclic hexapeptide with two Δz‐Phe residues
Optimising selective deuteration of proteins for 2D 1H NMR detection and assignment studies Application to the Phe residues of Lactobacillus casei dihydrofolate reductase
J. Feeney, B. Birdsall, J. Akiboye, S.J.B. Tendler, J.Jiménez Barbero, G. Ostler, J.R.P. Arnold, G.C.K. Roberts, A. Kühn and K. Roth FEBS Letters 248(1-2) 57 (1989) https://doi.org/10.1016/0014-5793(89)80431-4
Three‐dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy
The influence of stereospecific assignments on the determination of three‐dimensional structures of proteins by nuclear magnetic resonance spectroscopy
Concerted two-dimensional NMR approaches to hydrogen-1, carbon-13, and nitrogen-15 resonance assignments in proteins
Brian J. Stockman, Michael D. Reily, William M. Westler, Eldon L. Ulrich and John L. Markley Biochemistry 28(1) 230 (1989) https://doi.org/10.1021/bi00427a032
Two-dimensional proton and phosphorus-31 NMR spectra and restrained molecular dynamics structure of an extrahelical adenosine tridecamer oligodeoxyribonucleotide duplex
Edward Nikonowicz, Vikram Roongta, Claude R. Jones and David G. Gorenstein Biochemistry 28(22) 8714 (1989) https://doi.org/10.1021/bi00448a007
Mobility of secondary structure units of horse‐muscle acylphosphatase
Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution
Andrew D. Robertson, Enrico O. Purisima, Margaret A. Eastman and Harold A. Scheraga Biochemistry 28(14) 5930 (1989) https://doi.org/10.1021/bi00440a033
Conformational Analysis of Didemnins. A multidisciplinary approach by means of X‐Ray, NMR, molecular‐dynamics, and molecular‐mechanics techniques
A proton nuclear magnetic resonance study on the solution structure of crotamine
Toshiya Endo, Masanao Oya, Hiroshi Ozawa, Yoshio Kawano, José R. Giglio and Tatsuo Miyazawa Journal of Protein Chemistry 8(6) 807 (1989) https://doi.org/10.1007/BF01024904
1H‐NMR study of endothelin, sequence‐specific assignment of the spectrum and a solution structure
Proton and Phosphorus NMR Study of RNA Self-Complementary Hexamers: Influence of the 5-Methylcytidine on the Conformational Transitions and the Molecular Motions
G. Bloch, F. Ceolin, F. Macquaire, J. M. Neumann, F. Babin and T. Huynh-Dinh Journal of Biomolecular Structure and Dynamics 6(6) 1151 (1989) https://doi.org/10.1080/07391102.1989.10506542
Solution conformation of endothelin determined by nuclear magnetic resonance and distance geometry
Proton‐detected C,H correlation NMR techniques for the complete assignment of all proton and carbon resonances of a cyclic peptide
Mechtild Hofmann, Matthias Gehrke, Wolfgang Bermel and Horst Kessler Magnetic Resonance in Chemistry 27(9) 877 (1989) https://doi.org/10.1002/mrc.1260270911
Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a
Solution conformation of a synthetic fragment of human pituitary growth hormone. Two-dimensional NMR of an .alpha.-helical dimer
Vikram Roongta, Robert Powers, Claude Jones, Michael J. Beakage, James E. Shields and David G. Gorenstein Biochemistry 28(3) 1048 (1989) https://doi.org/10.1021/bi00429a019
Static and transient hydrogen-bonding interactions in recombinant desulfatohirudin studied by proton nuclear magnetic resonance measurements of amide proton exchange rates and pH-dependent chemical shifts
A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin
Julie D. Forman-Kay, G. Marius Clore, Paul C. Driscoll, Paul Wingfield, Frederic M. Richards and Angela M. Gronenborn Biochemistry 28(17) 7088 (1989) https://doi.org/10.1021/bi00443a045
NMR studies of the influence of dodecyl sulfate on the amide hydrogen exchange kinetics of a micelle-solubilized hydrophobic tripeptide
Analysis of the relative contributions of the nuclear Overhauser interproton distance restraints and the empirical energy function in the calculation of oligonucleotide structures using restrained molecular dynamics
Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
Per J. Kraulis, G. Marius Clore, Michael Nilges, T. Alwyn Jones, Goeran Pettersson, Jonathan Knowles and Angela M. Gronenborn Biochemistry 28(18) 7241 (1989) https://doi.org/10.1021/bi00444a016
Sequential 1H‐NMR assignment and solution structure of bovine pancreatic ribonuclease A
Manuel RICO, Marta BRUIX, Jorge SANTORO, Carlos GONZALEZ, José Luis NEIRA, José Luis NIETO and José HERRANZ European Journal of Biochemistry 183(3) 623 (1989) https://doi.org/10.1111/j.1432-1033.1989.tb21092.x
Conformational studies of d(AAAAATTTTT)2 using constraints from nuclear Overhauser effects and from quantitative analysis of the cross-peak fine structures in two-dimensional proton nuclear magnetic resonance spectra
Bernardo Celda, Hans Widmer, Werner Leupin, Walter J. Chazin, William A. Denny and Kurt Wuethrich Biochemistry 28(4) 1462 (1989) https://doi.org/10.1021/bi00430a006
19F NMR detection of a fluorine‐labelled enzyme in vivo
A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure
Paul C. Driscoll, G. Marius Clore, Laszlo Beress and Angela M. Gronenborn Biochemistry 28(5) 2178 (1989) https://doi.org/10.1021/bi00431a032
Investigation of the solution structures and mobility of oxidised and reduced cytochrome b5 by 2D NMR spectroscopy
High-Field NMR and Circular Dichroism Solvent-Dependent Conformational Studies of the Bradykinin C-Terminal Tetrapeptide Ser-Pro-Phe-Arg
Albin Otter, Paul G. Scott, John R. Cann, Raymond J. Vavrek, John M. Stewart and George Kotovych Journal of Biomolecular Structure and Dynamics 6(3) 609 (1988) https://doi.org/10.1080/07391102.1988.10506511
2D NMR investigation of the binding of the anticancer drug actinomycin D to duplexed dATGCGCAT: conformational features of the unique 2:1 adduct
Type I collagen .alpha.-1 chain C-telopeptide: solution structure determined by 600-MHz proton NMR spectroscopy and implications for its role in collagen fibrillogenesis
Atomic Motions in Molecular Crystals from Diffraction Measurements
Jack D. Dunitz, Emily F. Maverick and Kenneth N. Trueblood Angewandte Chemie International Edition in English 27(7) 880 (1988) https://doi.org/10.1002/anie.198808801
Long‐range 15N‐1H correlation as an aid to sequential proton resonance assignment of proteins Application to the DNA‐binding protein ner from phage Mu
Determination of three‐dimensional structures of proteins from interproton distance data by hybrid distance geometry‐dynamical simulated annealing calculations
Selective reversible deuteriation of oligodeoxynucleotides: simplification of two-dimensional nuclear Overhauser effect NMR spectral assignment of a non-self-complementary dodecamer duplex
Two‐dimensional 1H‐NMR study of bacterioopsin‐(34–65)‐polypeptide conformation
Alexander S. Arseniev, Innokenti V. Maslennikov, Vladimir F. Bystrov, Alexander T. Kozhich, Vadim T. Ivanov and Yuri A. Ovchinnikov FEBS Letters 231(1) 81 (1988) https://doi.org/10.1016/0014-5793(88)80707-5
Structure and Reactivity of Lithium Enolates. From Pinacolone to Selective C‐Alkylations of Peptides. Difficulties and Opportunities Afforded by Complex Structures
High-resolution NMR studies of fibrinogen-like peptides in solution: resonance assignments and conformational analysis of residues 1-23 of the A.alpha. chain of human fibrinogen
Mobile sequences in the pyruvate dehydrogenase complex, the E2 component, the catalytic domain and the 2‐oxoglutarate dehydrogenase complex of Azotobacter vinelandii, as detected by 600 MHz 1H‐NMR spectroscopy
One‐ and two‐dimensional NMR investigations of the heme pocket in free α(CO) chains from human hemoglobin
Corinne SCHAEFFER, Constantin T. CRAESCU, Joël MISPELTER, Marie‐Claude GAREL, Jean ROSA and Jean‐Marc LHOSTE European Journal of Biochemistry 173(2) 317 (1988) https://doi.org/10.1111/j.1432-1033.1988.tb14001.x