Articles citing this article

The Citing articles tool gives a list of articles citing the current article.
The citing articles come from EDP Sciences database, as well as other publishers participating in CrossRef Cited-by Linking Program. You can set up your personal account to receive an email alert each time this article is cited by a new article (see the menu on the right-hand side of the abstract page).

Cited article:

Bacterial expression and characterization of the CREB bZip module: Circular dichroism and 2D 1H‐NMR studies

Zulma I. Santiago‐Rivera, David G. Gorenstein, John S. Williams and Ourania M. Andrisani
Protein Science 2 (9) 1461 (1993)
https://doi.org/10.1002/pro.5560020910

Complete assignments of magnetic resonances of ribonuclease H from Escherichia coli by double- and triple-resonance 2D and 3D NMR spectroscopies

Toshio Yamazaki, Mayumi Yoshida and Kuniaki Nagayama
Biochemistry 32 (21) 5656 (1993)
https://doi.org/10.1021/bi00072a023

The Nonhelical Structure of Antifreeze Protein Type III

Frank D. Sönnichsen, Brian D. Sykes, Heman Chao and Peter L. Davies
Science 259 (5098) 1154 (1993)
https://doi.org/10.1126/science.8438165

Metal Ion-Dependent Modulation of the Dynamics of a Designed Protein

Tracy M. Handel, Scott A. Williams and William F. DeGrado
Science 261 (5123) 879 (1993)
https://doi.org/10.1126/science.8346440

Assessing the Quality of Solution Nuclear Magnetic Resonance Structures by Complete Cross-Validation

Axel T. Brünger, G. Marius Clore, Angela M. Gronenborn, Rainer Saffrich and Michael Nilges
Science 261 (5119) 328 (1993)
https://doi.org/10.1126/science.8332897

Sequential1H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins

Mark G. Hinds and Raymond S. Norton
Journal of Protein Chemistry 12 (3) 371 (1993)
https://doi.org/10.1007/BF01028199

Three‐dimensional structure of human insulin‐like growth factor‐I (IGF‐I) determined by 1H‐NMR and distance geometry

AKIHIRO SATO, SHIGENORI NISHIMURA, TADAYASU OHKUBO, YOSHIMASA KYOGOKU, SATOSHI KOYAMA, MASAKAZU KOBAYASHI, TSUTOMU YASUDA and YUJI KOBAYASHI
International Journal of Peptide and Protein Research 41 (5) 433 (1993)
https://doi.org/10.1111/j.1399-3011.1993.tb00462.x

Conformational analysis of the type II and type III collagen α‐1 chain N‐telopeptides by 1H‐NMR spectroscopy and restrained molecular mechanics calculations

Albin Otter, Paul G. Scott and George Kotovych
Biopolymers 33 (9) 1443 (1993)
https://doi.org/10.1002/bip.360330914

βVI Turns in peptides and proteins: A model peptide mimicry

Gerhard Müller, Marion Gurrath, Michael Kurz and Horst Kessler
Proteins: Structure, Function, and Bioinformatics 15 (3) 235 (1993)
https://doi.org/10.1002/prot.340150303

Unfolding of an α‐helix in peptide crystals by solvation: Conformational fragility in a heptapeptide

Isabella L. Karle, Judith L. Flippen‐Anderson, K. Uma and P. Balaram
Biopolymers 33 (5) 827 (1993)
https://doi.org/10.1002/bip.360330511

Probing protein structure by solvent perturbation of nmr spectra. II. Determination of surface and buried residues in homologous proteins

Gennaro Esposito, Arthur M. Lesk, Henriette Molinari, Andrea Motta, Neri Niccolai and Annalisa Pastore
Biopolymers 33 (5) 839 (1993)
https://doi.org/10.1002/bip.360330512

A proton magnetic resonance study of two synthetic agonist–antagonist pairs of bradykinin analogues

Albin Otter, Peter Bigler, John M. Stewart and George Kotovych
Biopolymers 33 (5) 769 (1993)
https://doi.org/10.1002/bip.360330506

1H, 13C, and 15N assignments and secondary structure of the FK506 binding protein when bound to ascomycin

Robert X. Xu, David Nettesheim, Edward T. Olejniczak, Robert Meadows, Gerd Gemmecker and Stephen W. Fesik
Biopolymers 33 (4) 535 (1993)
https://doi.org/10.1002/bip.360330404

Recombinant human IL-6 expressed inE. coli undergoes selective N-terminal degradation: Evidence that the protein consists of a stable core and a nonessential flexible N-terminal

Amanda E. I. Proudfoot, Steven C. Brown, Alain R. Bernard, Jean-Yves Bonnefoy and Eric H. Kawashima
Journal of Protein Chemistry 12 (4) 489 (1993)
https://doi.org/10.1007/BF01025050

Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti‐MIR antibody: A two‐dimensional nuclear magnetic resonance and molecular dynamics approach

Vassilios Tsikaris, Evangelos Detsikas, Maria Sakarellos‐Daitsiotis, Constantinos Sakarellos, Efstratia Vatzaki, Socrates J. Tzartos, Michel Marraud and Manh Thong Cung
Biopolymers 33 (7) 1123 (1993)
https://doi.org/10.1002/bip.360330714

Conformation of thymosin β4 in water determined by NMR spectroscopy

Michael CZISCH, Michael SCHLEICHER, Susanne HÖRGER, Wolfgang VOELTER and Tad A. HOLAK
European Journal of Biochemistry 218 (2) 335 (1993)
https://doi.org/10.1111/j.1432-1033.1993.tb18382.x

Sequential assignment of proton resonances in the NMR spectrum of Zn‐substituted α chains from human hemoglobin.

Laure MARTINEAU and Constantin T. CRAESCU
European Journal of Biochemistry 214 (2) 383 (1993)
https://doi.org/10.1111/j.1432-1033.1993.tb17934.x

1H‐NMR analysis of turkey egg‐white lysozyme and comparison with hen egg‐white lysozyme

Kristin BARTIK, Christopher M. DOBSON and Christina REDFIELD
European Journal of Biochemistry 215 (2) 255 (1993)
https://doi.org/10.1111/j.1432-1033.1993.tb18030.x

Two‐dimensional NMR assignment of hyperfine‐shifted resonances of very fast relaxing metal binding sites of proteins by NOE spectroscopy

Marco SETTE, Maurizio PACI, Alessandro DESIDERI and Giuseppe ROTILIO
European Journal of Biochemistry 213 (1) 391 (1993)
https://doi.org/10.1111/j.1432-1033.1993.tb17773.x

Zinc‐ and sequence‐dependent binding to nucleic acids by the N‐terminal zinc finger of the HIV‐1 nucleocapsid protein: NMR structure of the complex with the Psi‐site analog, dACGCC

Terri L. South and Michael F. Summers
Protein Science 2 (1) 3 (1993)
https://doi.org/10.1002/pro.5560020102

Structures of DNA‐binding mutant zinc finger domains: Implications for DNA binding

Ross C. Hoffman, Rachel E. Klevit and Suzanna J. Horvath
Protein Science 2 (6) 951 (1993)
https://doi.org/10.1002/pro.5560020609

Solution structure of the calcium channel antagonist ω‐conotoxin GVIA

Jack J. Skalicky, D. Joseph Ciesla, Arthur Pardi, William J. Metzler and Alphonse Galdes
Protein Science 2 (10) 1591 (1993)
https://doi.org/10.1002/pro.5560021005

Structural studies of Desulfovibrio vulgaris ferrocytochrome c3 by two‐dimensional NMR

David L. TURNER, Carlos A. SALGUEIRO, Jean LeGALL and António V. XAVIER
European Journal of Biochemistry 210 (3) 931 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17497.x

NMR studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1

Xiao Lu Zhang, Michael E. Selsted and Arthur Pardi
Biochemistry 31 (46) 11348 (1992)
https://doi.org/10.1021/bi00161a012

Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

Axel T. Brünger
Nature 355 (6359) 472 (1992)
https://doi.org/10.1038/355472a0

Three-Dimensional Solution Structure of Human Interleukin-4 by Multidimensional Heteronuclear Magnetic Resonance Spectroscopy

Robert Powers, Daniel S. Garrett, Carl J. March, Eric A. Frieden, Angela M. Gronenborn and G. Marius Clore
Science 256 (5064) 1673 (1992)
https://doi.org/10.1126/science.256.5064.1673

The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

D. S. Wishart, B. D. Sykes and F. M. Richards
Biochemistry 31 (6) 1647 (1992)
https://doi.org/10.1021/bi00121a010

Conformation and dynamics of an Fab'-bound peptide by isotope-edited NMR spectroscopy

P. Tsang, M. Rance, T. M. Fieser, J. M. Ostresh, R. A. Houghten, R. A. Lerner and P. E. Wright
Biochemistry 31 (15) 3862 (1992)
https://doi.org/10.1021/bi00130a018

Identification by 1H NMR spectroscopy of flexible C‐terminal extensions in bovine lens α‐crystallin

John A. Carver, J.Andrew Aquilina, Roger J.W. Truscott and Gregory B. Ralston
FEBS Letters 311 (2) 143 (1992)
https://doi.org/10.1016/0014-5793(92)81386-Z

Proton NMR studies of Cucurbita maxima trypsin inhibitors: evidence for pH-dependent conformational change and His25-Tyr27 interaction

Ramaswamy Krishnamoorthi, Chan Lan Sun Lin, Yu Xi Gong, David VanderVelde and Karl Hahn
Biochemistry 31 (3) 905 (1992)
https://doi.org/10.1021/bi00118a037

Proton NMR-based determination of the secondary structure of porcine pancreatic spasmolytic polypeptide: one of a new family of "trefoil" motif containing cell growth factors

Mark D. Carr
Biochemistry 31 (7) 1998 (1992)
https://doi.org/10.1021/bi00122a015

Three-dimensional homonuclear NOESY-TOCSY of an intramolecular pyrimidine.cntdot.purine.cntdot.pyrimidine DNA triplex containing a central G.cntdot.TA triple: nonexchangeable proton assignments and structural implications

Ishwar Radhakrishnan, Dinshaw J. Patel and Xiaolian Gao
Biochemistry 31 (9) 2514 (1992)
https://doi.org/10.1021/bi00124a011

1H‐NMR assignments and local environments of aromatic residues in bovine, human and guinea pig variants of α‐lactalbumin

Andrei T. ALEXANDRESCU, R. William BROADHURST, Claire WORMALD, Chia‐Lin CHYAN, Jean BAUM and Christopher M. DOBSON
European Journal of Biochemistry 210 (3) 699 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17471.x

Membrane-bound conformation of mastoparan-X, a G-protein-activating peptide

Kaori Wakamatsu, Akihiko Okada, Tatsuo Miyazawa, Masanao Ohya and Tsutomu Higashijima
Biochemistry 31 (24) 5654 (1992)
https://doi.org/10.1021/bi00139a032

Improved strategy for sequence‐specific 13C NMR assignments in [d(CGTACGTACG)]2

Ke Yu Wang, Gregory J. Heffron, Karl D. Bishop, George C. Levy, Anna M. Garbesi, Luisa Tondelli, James H. Medley and Philip N. Borer
Magnetic Resonance in Chemistry 30 (5) 377 (1992)
https://doi.org/10.1002/mrc.1260300504

Determination of the solution structure of a platelet-adhesion peptide of von Willebrand factor

Heather M. Knott, Michael C. Berndt, Andrew V. Kralicek, Sean I. O'Donoghue and Glenn F. King
Biochemistry 31 (45) 11152 (1992)
https://doi.org/10.1021/bi00160a028

Heteronuclear proton-nitrogen-15 nuclear magnetic resonance studies of the c subunit of the Escherichia coli F1F0 ATP synthase: assignment and secondary structure

Timothy J. Norwood, D. Arthur Crawford, Mary E. Steventon, Paul C. Driscoll and Iain D. Campbell
Biochemistry 31 (27) 6285 (1992)
https://doi.org/10.1021/bi00142a017

Proton and nitrogen-15 NMR characterization of free and bound states of an amphiphilic peptide interacting with calmodulin

Benedict Precheur, Helene Munier, Joel Mispelter, Octavian Barzu and Constantin T. Craescu
Biochemistry 31 (1) 229 (1992)
https://doi.org/10.1021/bi00116a032

Sequential proton NMR assignments and secondary structure of the kringle domain from urokinase

Xiang Li, Richard A. G. Smith and Christopher M. Dobson
Biochemistry 31 (40) 9562 (1992)
https://doi.org/10.1021/bi00155a008

Peptide secondary structure induced by a micellar phospholipidic interface: proton NMR conformational study of a lipopeptide

Francois Macquaire, Francoise Baleux, Emmanuelle Giaccobi, Huynh Dinh Tam, Jean Michel Neumann and Alain Sanson
Biochemistry 31 (9) 2576 (1992)
https://doi.org/10.1021/bi00124a018

Sequential proton and nitrogen-15 NMR assignments and secondary structure of a recombinant anti-digoxin antibody VL domain

Keith L. Constantine, Valentina Goldfarb, Michael Wittekind, James Anthony, Shi Chung Ng and Luciano Mueller
Biochemistry 31 (21) 5033 (1992)
https://doi.org/10.1021/bi00136a017

NMR study of parallel-stranded tetraplex formation by the hexadeoxynucleotide d(TG4T)

Fareed Aboul-ela, Alastair I. H. Murchie and David M. J. Lilley
Nature 360 (6401) 280 (1992)
https://doi.org/10.1038/360280a0

Proton NMR assignments and secondary structure of human .beta.2-microglobulin in solution

Mark Okon, Paul Bray and Dusan Vucelic
Biochemistry 31 (37) 8906 (1992)
https://doi.org/10.1021/bi00152a030

Nucleic acid interactive properties of a peptide corresponding to the N-terminal zinc finger domain of HIV-1 nucleocapsid protein

Martha D. Delahunty, Terri L. South, Michael F. Summers and Richard L. Karpel
Biochemistry 31 (28) 6461 (1992)
https://doi.org/10.1021/bi00143a015

Proton NMR assignments of systemin

David J. Russell, Gregory Pearce, Clarence A. Ryan and James D. Satterlee
Journal of Protein Chemistry 11 (3) 265 (1992)
https://doi.org/10.1007/BF01024865

High-level expression of recombinant human FK-binding protein from a fusion precursor

Rohinton Edalji, Tami J. Pilot-Matias, Steven D. Pratt, David A. Egan, Jean M. Severin, Earl G. Gubbins, Andrew M. Petros, Stephen W. Fesik, Neal S. Burres and Thomas F. Holzman
Journal of Protein Chemistry 11 (3) 213 (1992)
https://doi.org/10.1007/BF01024859

Two-dimensional NMR, circular dichroism, and fluorescence studies of PP-50, a synthetic ATP-binding peptide from the .beta.-subunit of mitochondrial ATP synthase

Woei Jer Chuang, Chitrananda Abeygunawardana, Peter L. Pedersen and Albert S. Mildvan
Biochemistry 31 (34) 7915 (1992)
https://doi.org/10.1021/bi00149a024

Solution structure of a synthetic peptide corresponding to a receptor binding region of FSH (hFSH-β 33–53)

Paul F. Agris, Richard H. Guenther, Hanna Sierzputowska-Gracz, Laura Easter, Wanda Smith, Charles C. Hardin, Tomás A. Santa-Coloma, John W. Crabb and Leo E. Reichert
Journal of Protein Chemistry 11 (5) 495 (1992)
https://doi.org/10.1007/BF01025027

The solution structure of a cyclic endothelin antagonist, BQ‐123, based on 1H–1H and 13H–1H three bond oupling constants

Michael D. Reily, Venkataraman Thanabal, Diana O. Omecinsky, James B. Dunbar, Annette M. Doherty and Patricia L. DePue
FEBS Letters 300 (2) 136 (1992)
https://doi.org/10.1016/0014-5793(92)80181-F

NMR studies of amyloid .beta.-peptides: proton assignments, secondary structure, and mechanism of an .alpha.-helix .fwdarw. .beta.-sheet conversion for a homologous, 28-residue, N-terminal fragment

Michael G. Zagorski and Colin J. Barrow
Biochemistry 31 (24) 5621 (1992)
https://doi.org/10.1021/bi00139a028

Solution structure of the DNA-binding domain of Cd2-GAL4 from S. cerevisiae

James D. Baleja, Ronen Marmorstein, Stephen C. Harrison and Gerhard Wagner
Nature 356 (6368) 450 (1992)
https://doi.org/10.1038/356450a0

Determination of the three‐dimensional solution structure of the histidine‐containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy

Nico A. J. van NULAND, Joachim GRÖTZINGER, Klaas DIJKSTRA, Ruud M. SCHEEK and George T. ROBILLARD
European Journal of Biochemistry 210 (3) 881 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17492.x

Sequential resonance assignments of oxidized high-potential iron-sulfur protein from Chromatium vinosum

David G. Nettesheim, Scott R. Harder, Benjamin A. Feinberg and James D. Otvos
Biochemistry 31 (4) 1234 (1992)
https://doi.org/10.1021/bi00119a037

Solution conformation of human neuropeptide Y by 1H nuclear magnetic resonance and restrained molecular dynamics

Hervé DARBON, Jean‐Marie BERNASSAU, Colette DELEUZE, Jacques CHENU, Alain ROUSSEL and Christian CAMBILLAU
European Journal of Biochemistry 209 (2) 765 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17346.x

Three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution

Milton H. Werner and David E. Wemmer
Biochemistry 31 (4) 999 (1992)
https://doi.org/10.1021/bi00119a008

Cyclosporin A—cyclophilin complex formation A model based on X‐ray and NMR data

Claus Spitzfaden, Hans-Peter Weber, Werner Braun, Joerg Kallen, Gerhard Wider, Hans Widmer, Malcolm D. Walkinshaw and Kurt Wüthrich
FEBS Letters 300 (3) 291 (1992)
https://doi.org/10.1016/0014-5793(92)80866-F

Sequence-specific assignments of the proton nuclear magnetic resonance spectra of reduced high-potential ferredoxin (HiPIP) from Chromatium vinosum

Jacques Gaillard, Jean Pierre Albrand, Jean Marc Moulis and David E. Wemmer
Biochemistry 31 (24) 5632 (1992)
https://doi.org/10.1021/bi00139a029

Solution structure of a platelet receptor peptide bound to bovine .alpha.-thrombin

Feng Ni, Daniel R. Ripoll, Philip D. Martin and Brian F. P. Edwards
Biochemistry 31 (46) 11551 (1992)
https://doi.org/10.1021/bi00161a037

Sequence‐specific 1H‐NMR assignment and determination of the secondary structure of bovine heart fatty‐acid‐binding protein

Christian LÜCKE, Dirck LASSEN, Hans‐Jürgen KREIENKAMP, Friedrich SPENER and Heinz RÜTERJANS
European Journal of Biochemistry 210 (3) 901 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17494.x

Sequence specific 1H‐NMR assignments and secondary structure of a carboxy‐terminal functional fragment of apolipoprotein CII

Per‐Olof LYCKSELL, Anders ÖHMAN, Gunilla BENGTSSON‐OLIVECRONA, Lennart B.‐Å. JOHANSSON, Sybren S. WIJMENGA, Dominik WERNIC and Astrid GRÄSLUND
European Journal of Biochemistry 205 (1) 223 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb16772.x

The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton‐NMR

David SIPOS, Mats ANDERSSON and Anders EHRENBERG
European Journal of Biochemistry 209 (1) 163 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17273.x

NMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins

Tai‐He Xia, John H. Bushweller, Patrick Sodano, Martin Billeter, Olof Björnberg, Arne Holmgren and Kurt Wüthrich
Protein Science 1 (3) 310 (1992)
https://doi.org/10.1002/pro.5560010302

NMR study of nitrogen-15-labeled Escherichia coli valine transfer RNA

Byong Seok Choi and Alfred G. Redfield
Biochemistry 31 (51) 12799 (1992)
https://doi.org/10.1021/bi00166a013

Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy

Brian J. Stockman, Terrence A. Scahill, Melinda Roy, Eldon L. Ulrich, Nancy A. Strakalaitis, David P. Brunner, Anthony W. Yem and Martin R. Deibel
Biochemistry 31 (23) 5237 (1992)
https://doi.org/10.1021/bi00138a001

A .beta.-turn is present in the 392-411 segment of the human fibrinogen .gamma.-chain. Effects of structural changes in this segment on affinity to antibody 4A5

Michael Blumenstein, Gary R. Matsueda, Sheila Timmons and Jacek Hawiger
Biochemistry 31 (44) 10692 (1992)
https://doi.org/10.1021/bi00159a008

Proton NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas

Xiao Mei Ye, Thomas C. Pochapsky and Susan Sondej Pochapsky
Biochemistry 31 (7) 1961 (1992)
https://doi.org/10.1021/bi00122a009

Homo- and heteronuclear NMR studies of the human retinoic acid receptor .beta. DNA-binding domain: sequential assignments and identification of secondary structure elements

M. Katahira, R. M. A. Knegtel, R. Boelens, D. Eib, J. G. Schilthuis, P. T. Van der Saag and R. Kaptein
Biochemistry 31 (28) 6474 (1992)
https://doi.org/10.1021/bi00143a017

NMR analysis of helix I from the 5S RNA of Escherichia coli

S. A. White, M. Nilges, A. Huang, A. T. Brunger and P. B. Moore
Biochemistry 31 (6) 1610 (1992)
https://doi.org/10.1021/bi00121a005

High-resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1

James G. Omichinski, G. Marius Clore, Mark Robien, Kazuyasu Sakaguchi, Ettore Appella and Angela M. Gronenborn
Biochemistry 31 (16) 3907 (1992)
https://doi.org/10.1021/bi00131a004

NMR and molecular modeling characterization of RGD containing peptides

M.J. BOGUSKY, A.M. NAYLOR, S.M. PITZENBERGER, R.F. NUTT, S.F. BRADY, C.D. COLTON, J.T. SISKO, P.S. ANDERSON and D.F. VEBER
International Journal of Peptide and Protein Research 39 (1) 63 (1992)
https://doi.org/10.1111/j.1399-3011.1992.tb01557.x

Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding

Magnus Ullner, Maria Selander, Egon Persson, Johan Stenflo, Torbjoern Drakenberg and Olle Teleman
Biochemistry 31 (26) 5974 (1992)
https://doi.org/10.1021/bi00141a004

Warum Pentose‐ und nicht Hexose‐Nucleinsäuren??. Teil II. Oligonucleotide aus 2′,3′‐Dideoxy‐β‐D‐glucopyranosyl‐Bausteinen (‘Homo‐DNS’): Herstellung.

Markus Böhringer, Hans‐JÖRg Roth, Jürg Hunziker, Michael Göbel, Ravichandran Krishnan, Alfred Giger, Bernd Schweizer, Jakob Schreiber, Christian Leumann and Albert Eschenmoser
Helvetica Chimica Acta 75 (5) 1416 (1992)
https://doi.org/10.1002/hlca.19920750503

The three‐dimensional structure of guanine‐specific ribonuclease F1 in solution determined by NMR spectroscopy and distance geometry

Takahisa NAKAI, Wataru YOSHIKAWA, Haruki NAKAMURA and Hiroshi YOSHIDA
European Journal of Biochemistry 208 (1) 41 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb17157.x

Three-dimensional solution structure of the B domain of staphylococcal protein A: comparisons of the solution and crystal structures

Hiroaki Gouda, Hidetaka Torigoe, Akiko Saito, Moriyuki Sato, Yoji Arata and Ichio Shimada
Biochemistry 31 (40) 9665 (1992)
https://doi.org/10.1021/bi00155a020

Toward a Dynamical Structure of DNA: Comparison of Theoretical and Experimental NOE Intensities

Jane M. Withka, S. Swaminathan, Jayashree Srinivasan, David L. Beveridge and Philip H. Bolton
Science 255 (5044) 597 (1992)
https://doi.org/10.1126/science.1736362

NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor

Dario Neri, Martin Billeter, Gerhard Wider and Kurt Wüthrich
Science 257 (5076) 1559 (1992)
https://doi.org/10.1126/science.1523410

Solution structure of a calmodulin-target peptide complex by multidimensional NMR

Mitsuhiko Ikura, G. Marius Clore, Angela M. Gronenborn, Guang Zhu, Claude B. Klee and Ad Bax
Science 256 (5057) 632 (1992)
https://doi.org/10.1126/science.1585175

Conformation of the TAR RNA-Arginine Complex by NMR Spectroscopy

Joseph D. Puglisi, Ruoying Tan, Barbara J. Calnan, Alan D. Frankel and James R. Williamson
Science 257 (5066) 76 (1992)
https://doi.org/10.1126/science.1621097

Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions

Daisuke Kohda and Fuyuhiko Inagaki
Biochemistry 31 (47) 11928 (1992)
https://doi.org/10.1021/bi00162a036

Effects of the presence of an aldehydic abasic site on the thermal stability and rates of helix opening and closing of duplex DNA

Igor Goljer, Jane M. Withka, Jung Yie Kao and Philip H. Bolton
Biochemistry 31 (46) 11614 (1992)
https://doi.org/10.1021/bi00161a047

NMR structural characterization of the reaction product between d(GpG) and the octahedral antitumor complex trans-RuCl2(DMSO)4

Gennaro Esposito, Sabina Cauci, Federico Fogolari, Enzo Alessio, Marco Scocchi, Franco Quadrifoglio and Paolo Viglino
Biochemistry 31 (31) 7094 (1992)
https://doi.org/10.1021/bi00146a010

Linear and cyclic peptide analogues of the polypeptide cardiac stimulant, anthopleurin‐A

Alison R. GOULD, Bridget C. MABBUTT, Lyndon E. LLEWELLYN, Neil H. GOSS and Raymond S. NORTON
European Journal of Biochemistry 206 (3) 641 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb16969.x

Solution structures of cyclic and dicyclic analogues of growth hormone releasing factor as determined by two‐dimensional NMR and CD spectroscopies and constrained molecular dynamics

David C. Fry, Vincent S. Madison, David N. Greeley, Arthur M. Felix, Edgar P. Heimer, Lawrence Frohman, Robert M. Campbell, Thomas F. Mowles, Voldemar Toome and Bogda B. Wegrzynski
Biopolymers 32 (6) 649 (1992)
https://doi.org/10.1002/bip.360320608

The three‐dimensional structure of the first EGF‐like module of human factor IX: Comparison with EGF and TGF‐α

M. Baron, D.G. Norman, T.S. Harvey, I.D. Campbell, P.A. Handford, M. Mayhew, G.G. Brownlee and A.G.D. Tse
Protein Science 1 (1) 81 (1992)
https://doi.org/10.1002/pro.5560010109

Sequence‐specific NMR assignments of the trp repressor from Escherichia coli using three‐dimensional 15N/1H heteronuclear techniques

Katherine L. B. BORDEN, Christopher J. BAUER, Thomas A. FRENKIEL, Pamela BECKMANN and Andrew N. LANE
European Journal of Biochemistry 204 (1) 137 (1992)
https://doi.org/10.1111/j.1432-1033.1992.tb16616.x

Folding topology of the disulfide-bonded dimeric DNA-binding domain of the myogenic determination factor MyoD

Melissa A. Starovasnik, T. Keith Blackwell, Thomas M. Laue, Harold Weintraub and Rachel E. Klevit
Biochemistry 31 (41) 9891 (1992)
https://doi.org/10.1021/bi00156a006