Pure and Applied Chemistry

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• Mohammed Sadia, Phelan Marie M., Rasul Usman, Ramesh Vasudevan: NMR elucidation of the role of Mg2+ in the structure and stability of the conserved RNA motifs of the EMCV IRES element. Org. Biomol. Chem. 2014, 12, 1495. <http://dx.doi.org/10.1039/c3ob41840e>
• Santiveri Clara M., García-Mayoral M. Flor, Pérez-Cañadillas José M., Jiménez M. Ángeles: NMR structure note: PHD domain from death inducer obliterator protein and its interaction with H3K4me3. J Biomol NMR 2013, 56, 183. <http://dx.doi.org/10.1007/s10858-013-9726-x>
• Tejero Roberto, Snyder David, Mao Binchen, Aramini James M., Montelione Gaetano T.: PDBStat: a universal restraint converter and restraint analysis software package for protein NMR. J Biomol NMR 2013, 56, 337. <http://dx.doi.org/10.1007/s10858-013-9753-7>
• Serrano Soraya, Callís Mariona, Vilanova Maria, Benito Antoni, Laurents Douglas V., Ribó Marc, Bruix Marta: 1H, 13C and 15N resonance assignments of the Onconase FL-G zymogen. Biomol NMR Assign 2013, 7, 13. <http://dx.doi.org/10.1007/s12104-012-9367-0>
• Mirassou Yasmina, Elías-Arnanz Montserrat, Padmanabhan S., Jiménez M. Angeles: 1H, 13C and 15N assignments of CdnL, an essential protein in Myxococcus xanthus. Biomol NMR Assign 2013, 7, 51. <http://dx.doi.org/10.1007/s12104-012-9375-0>
• Cui Zhenling, Li Yifei, Xiao Yan, Feng Yingang, Cui Qui: Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824. Biomol NMR Assign 2013, 7, 73. <http://dx.doi.org/10.1007/s12104-012-9381-2>
• Cavini Ítalo Augusto, Oliveira-Silva Rodrigo, Almeida Marques Ivo, Kalbitzer Hans Robert, Munte Claudia Elisabeth: Chemical shift assignments of the canecystatin-1 from Saccharum officinarum. Biomol NMR Assign 2013, 7, 163. <http://dx.doi.org/10.1007/s12104-012-9401-2>
• Xie Tao, Feng Yingang, Shan Lu, Wang Jinfeng: Modeling of the [E43S]SNase-ssDNA–Cd2+ complex: Structural insight into the action of nuclease on ssDNA. Archives of Biochemistry and Biophysics 2013, 532, 103. <http://dx.doi.org/10.1016/j.abb.2013.02.003>
• Lakowski Ted M., Szeitz András, Pak Magnolia L., Thomas Dylan, Vhuiyan Mynol I., Kotthaus Joscha, Clement Bernd, Frankel Adam: MS3 fragmentation patterns of monomethylarginine species and the quantification of all methylarginine species in yeast using MRM3. Journal of Proteomics 2013, 80, 43. <http://dx.doi.org/10.1016/j.jprot.2013.01.003>
• Montelione Gaetano T., Nilges Michael, Bax Ad, Güntert Peter, Herrmann Torsten, Richardson Jane S., Schwieters Charles D., Vranken Wim F., Vuister Geerten W., Wishart David S., Berman Helen M., Kleywegt Gerard J., Markley John L.: Recommendations of the wwPDB NMR Validation Task Force. Structure 2013, 21, 1563. <http://dx.doi.org/10.1016/j.str.2013.07.021>
• Imada Kumiko, Sakai Eriko, Kato Hikaru, Kawabata Tetsuro, Yoshinaga Sosuke, Nehira Tatsuo, Terasawa Hiroaki, Tsukamoto Sachiko: Reticulatins A and B and hyrtioreticulin F from the marine sponge Hyrtios reticulatus. Tetrahedron 2013, 69, 7051. <http://dx.doi.org/10.1016/j.tet.2013.06.043>
• Lizak Christian, Gerber Sabina, Michaud Gaëlle, Schubert Mario, Fan Yao-Yun, Bucher Monika, Darbre Tamis, Aebi Markus, Reymond Jean-Louis, Locher Kaspar P.: Unexpected reactivity and mechanism of carboxamide activation in bacterial N-linked protein glycosylation. Nat Comms 2013, 4. <http://dx.doi.org/10.1038/ncomms3627>
• King John, Shammas Christos, Nareen Misbah, Lelli Moreno, Ramesh Vasudevan: NMR characterisation of a highly conserved secondary structural RNA motif of Halobacterium halobium 23S rRNA. Org. Biomol. Chem. 2013, 11, 3382. <http://dx.doi.org/10.1039/c3ob40295a>
• Valadares Napoleão F., de Oliveira-Silva Rodrigo, Cavini Italo A., de Almeida Marques Ivo, D'Muniz Pereira Humberto, Soares-Costa Andrea, Henrique-Silva Flavio, Kalbitzer Hans R., Munte Claudia E., Garratt Richard C.: X-ray crystallography and NMR studies of domain-swapped canecystatin-1. FEBS J 2013, 280, 1028. <http://dx.doi.org/10.1111/febs.12095>
• Gallego-García Aranzazu, Mirassou Yasmina, Elías-Arnanz Montserrat, Padmanabhan S., Jiménez M. Angeles: NMR structure note: N-terminal domain of Thermus thermophilus CdnL. J Biomol NMR 2012, 53, 355. <http://dx.doi.org/10.1007/s10858-012-9648-z>
• Lee Woonghee, Yu Wookyung, Kim Suhkmann, Chang Iksoo, Lee Weontae, Markley John L.: PACSY, a relational database management system for protein structure and chemical shift analysis. J Biomol NMR 2012, 54, 169. <http://dx.doi.org/10.1007/s10858-012-9660-3>
• Subedi Ganesh P., Satoh Tadashi, Hanashima Shinya, Ikeda Akemi, Nakada Hiroshi, Sato Reiko, Mizuno Mamoru, Yuasa Noriyuki, Fujita-Yamaguchi Yoko, Yamaguchi Yoshiki: Overproduction of anti-Tn antibody MLS128 single-chain Fv fragment in Escherichia coli cytoplasm using a novel pCold-PDI vector. Protein Exp Purif 2012, 82, 197. <http://dx.doi.org/10.1016/j.pep.2011.12.010>
• Horváth Gergő, Király Péter, Tárkányi Gábor, Toke Orsolya: Internal Motions and Exchange Processes in Human Ileal Bile Acid Binding Protein As Studied by Backbone ¹⁵N Nuclear Magnetic Resonance Spectroscopy. Biochemistry (Wash ) 2012, 51, 1848. <http://dx.doi.org/10.1021/bi201588q>
• Yao Hongwei, Feng Yingang, Zhou Tao, Wang Jinfeng, Wang Zhi-Xin: NMR Studies of the Interaction between Human Programmed Cell Death 5 and Human p53. Biochemistry (Wash ) 2012, 51, 2684. <http://dx.doi.org/10.1021/bi201822x>
• Au Ring Yan, Ng Kui Sang, Chi Lai Man, Lam Sik Lok: Effect of an Abasic Site on Strand Slippage in DNA Primer-Templates. J. Phys. Chem. B 2012, 116, 14781. <http://dx.doi.org/10.1021/jp308759k>
• Neudecker P., Robustelli P., Cavalli A., Walsh P., Lundstrom P., Zarrine-Afsar A., Sharpe S., Vendruscolo M., Kay L. E.: Structure of an Intermediate State in Protein Folding and Aggregation. Sceince 2012, 336, 362. <http://dx.doi.org/10.1126/science.1214203>
• Xuan Jinsong, Song Xiaxia, Wang Jinfeng, Feng Yingang: Resonance assignments of a putative PilT N-terminus domain protein SSO1118 from hyperthermophilic archaeon Sulfolobus solfataricus P2. Biomol NMR Assign 2011, 5, 161. <http://dx.doi.org/10.1007/s12104-010-9291-0>
• Dominguez Cyril, Schubert Mario, Duss Olivier, Ravindranathan Sapna, Allain Frédéric H.-T.: Structure determination and dynamics of protein–RNA complexes by NMR spectroscopy. Progr Nucl Magn Reson Spectrosc 2011, 58, 1. <http://dx.doi.org/10.1016/j.pnmrs.2010.10.001>
• Trevino M. A., Rodriguez-Rodriguez M., Laurents D. V., Arranz R., Valpuesta J. M., Rico M., Bruix M., Jimenez M. A.: Characterization of the structure and self-recognition of the human centrosomal protein NA14: implications for stability and function. Protein Engineer 2011, 24, 883. <http://dx.doi.org/10.1093/protein/gzr050>
• Watanabe Eiji, Yamakura Fumiyuki, Kan Hirosaki: A new assignment technique of 2D-NMR spectra by spin-lock sequence to a tripeptide containing tryptophan in water. Magn Reson Chem 2010, n/a. <http://dx.doi.org/10.1002/mrc.2567>
• Feng Yingang, Yao Hongwei, Wang Jinfeng: Solution structure and calcium binding of protein SSO6904 from the hyperthermophilic archaeon Sulfolobus solfataricus . Proteins 2010, 78, 474. <http://dx.doi.org/10.1002/prot.22580>
• Todokoro Yasuto, Kobayashi Masatoshi, Sato Takeshi, Kawakami Toru, Yumen Ikuko, Aimoto Saburo, Fujiwara Toshimichi, Akutsu Hideo: Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR. J Biomol NMR 2010, 48, 1. <http://dx.doi.org/10.1007/s10858-010-9432-x>
• Ayuso-Tejedor Sara, Angarica Vladimir Espinosa, Bueno Marta, Campos Luis A., Abián Olga, Bernadó Pau, Sancho Javier, Jiménez M. Angeles: Design and Structure of an Equilibrium Protein Folding Intermediate: A Hint into Dynamical Regions of Proteins. Journal of Molecular Biology 2010, 400, 922. <http://dx.doi.org/10.1016/j.jmb.2010.05.050>
• Walsh Patrick, Neudecker Philipp, Sharpe Simon: Structural Properties and Dynamic Behavior of Nonfibrillar Oligomers Formed by PrP(106−126). J Am Chem Soc 2010, 132, 7684. <http://dx.doi.org/10.1021/ja100431q>
• Gortari Itzam De, Portella Guillem, Salvatella Xavier, Bajaj Vikram S., van der Wel Patrick C. A., Yates Jonathan R., Segall Matthew D., Pickard Chris J., Payne Mike C., Vendruscolo Michele: Time Averaging of NMR Chemical Shifts in the MLF Peptide in the Solid State. J Am Chem Soc 2010, 132, 5993. <http://dx.doi.org/10.1021/ja9062629>
• López-Alonso Jorge Pedro, Bruix Marta, Font Josep, Ribó Marc, Vilanova Maria, Jiménez María Angeles, Santoro Jorge, González Carlos, Laurents Douglas V.: NMR Spectroscopy Reveals that RNase A is Chiefly Denatured in 40% Acetic Acid: Implications for Oligomer Formation by 3D Domain Swapping. J Am Chem Soc 2010, 132, 1621. <http://dx.doi.org/10.1021/ja9081638>
• Kutyshenko V. P., Gushchina L. V., Khristoforov V. S., Prokhorov D. A., Timchenko M. A., Kudrevatykh Yu. A., Fedyukina D. V., Filimonov V. V.: NMR structure and dynamics of the chimeric protein SH3-F2. Mol Biol 2010, 44, 948. <http://dx.doi.org/10.1134/S0026893310060129>
• Khristoforov V. S., Prokhorov D. A., Timchenko M. A., Kudrevatykh Yu. A., Gushchina L. V., Filimonov V. V., Kutyshenko V. P.: Chimeric SHA-D domain “SH3-Bergerac“: 3D structure and dynamics studies. Rus J Bioorg Chem 2010, 36, 468. <http://dx.doi.org/10.1134/S1068162010040059>
• Nasr Khaled A., Schubert Christian R., Török Marianna, Kennedy Robert J., Kemp Daniel S.: Helix-coil energetics for helix formers and breakers reflect context and temperature: Mutants of helically robust, guest-sensitive homopeptide hosts. Biopolymers (Biospectroscopy) 2009, 91, 311. <http://dx.doi.org/10.1002/bip.21129>
• Shen Yang, Vernon Robert, Baker David, Bax Ad: De novo protein structure generation from incomplete chemical shift assignments. J Biomol NMR 2009, 43, 63. <http://dx.doi.org/10.1007/s10858-008-9288-5>
• Salnikov Evgeniy, Bertani Philippe, Raap Jan, Bechinger Burkhard: Analysis of the amide 15N chemical shift tensor of the Cα tetrasubstituted constituent of membrane-active peptaibols, the α-aminoisobutyric acid residue, compared to those of di- and tri-substituted proteinogenic amino acid residues. J Biomol NMR 2009, 45, 373. <http://dx.doi.org/10.1007/s10858-009-9380-5>
• Mirassou Yasmina, García-Moreno Diana, Santiveri Clara M., Santoro Jorge, Elías-Arnanz Montserrat, Padmanabhan S., Jiménez M. Angeles: 1H, 13C and 15N backbone and side chain resonance assignments of the C-terminal domain of CdnL from Myxococcus xanthus . Biomol NMR Assign 2009, 3, 9. <http://dx.doi.org/10.1007/s12104-008-9128-2>
• León Esther, González Carlos, Elías-Arnanz Montserrat, Padmanabhan S., Jiménez M. Angeles: 1H, 13C and 15N backbone and side chain resonance assignments of a Myxococcus xanthus anti-repressor with no known sequence homologues. Biomol NMR Assign 2009, 3, 37. <http://dx.doi.org/10.1007/s12104-008-9136-2>
• Munte Claudia Elisabeth, Becker Katja, Schirmer Rolf Heiner, Kalbitzer Hans Robert: NMR assignments of oxidised thioredoxin from Plasmodium falciparum . Biomol NMR Assign 2009, 3, 159. <http://dx.doi.org/10.1007/s12104-009-9163-7>
• Yao Hongwei, Xu Lanjun, Feng Yingang, Liu Dongsheng, Chen Yingyu, Wang Jinfeng: Structure–function correlation of human programmed cell death 5 protein. Archives of Biochemistry and Biophysics 2009, 486, 141. <http://dx.doi.org/10.1016/j.abb.2009.03.018>
• Spichty Martin, Taly Antoine, Hagn Franz, Kessler Horst, Barluenga Sofia, Winssinger Nicolas, Karplus Martin: The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts. biophys chem 2009, 143, 111. <http://dx.doi.org/10.1016/j.bpc.2009.04.003>
• Keifer Paul A.: Chemical-shift referencing and resolution stability in gradient LC–NMR (acetonitrile:water). J  Magn Reson 2009, 199, 75. <http://dx.doi.org/10.1016/j.jmr.2009.04.010>
• Bajaj Vikram S., van der Wel Patrick C.A., Griffin Robert G.: Observation of a Low-Temperature, Dynamically Driven Structural Transition in a Polypeptide by Solid-State NMR Spectroscopy. J Am Chem Soc 2009, 131, 118. <http://dx.doi.org/10.1021/ja8045926>
• Dos Alexandra, Schimming Volkmar, Huot Monique Chan, Limbach Hans-Heinrich: Acid-Induced Amino Side-Chain Interactions and Secondary Structure of Solid Poly-l-lysine Probed by ¹⁵N and ¹³C Solid State NMR and ab Initio Model Calculations. J Am Chem Soc 2009, 131, 7641. <http://dx.doi.org/10.1021/ja901082a>
• Hong Mei, Mishanina Tatiana V., Cady Sarah D.: Accurate Measurement of Methyl ¹³C Chemical Shifts by Solid-State NMR for the Determination of Protein Side Chain Conformation: The Influenza A M2 Transmembrane Peptide as an Example. J Am Chem Soc 2009, 131, 7806. <http://dx.doi.org/10.1021/ja901550q>
• Moreau Robert J., Schubert Christian R., Nasr Khaled A., Török Marianna, Miller Justin S., Kennedy Robert J., Kemp Daniel S.: Context-Independent, Temperature-Dependent Helical Propensities for Amino Acid Residues. J Am Chem Soc 2009, 131, 13107. <http://dx.doi.org/10.1021/ja904271k>
• Goodfellow Brian J., Nunes Sofia G., Rusnak Frank, Moura Isabel, Ascenso Carla, Moura José J.G., Volkman Brian F., Markley John L.: Zinc-substituted Desulfovibrio gigas desulforedoxins: Resolving subunit degeneracy with nonsymmetric pseudocontact shifts. Protein Sci 2009, 11, 2464. <http://dx.doi.org/10.1110/ps.0208802>
• Osborne Michael J., Siddiqui Nadeem, Landgraf Dirk, Pomposiello Pablo J., Gehring Kalle: The solution structure of the oxidative stress-related protein YggX from Escherichia coli. Protein Sci 2009, 14, 1673. <http://dx.doi.org/10.1110/ps.051358105>
• Harris R. K.: Editorial. Magn Reson Chem 2008, 46, 507. <http://dx.doi.org/10.1002/mrc.2218>
• Harris Robin K., Becker Edwin D., De Menezes Sonia M. Cabral, Granger Pierre, Hoffman Roy E., Zilm Kurt W.: Further Conventions for NMR Shielding and Chemical Shifts (IUPAC Recommendations 2008). Magn Reson Chem 2008, 46, 582. <http://dx.doi.org/10.1002/mrc.2225>
• Markley John L., Ulrich Eldon L., Berman Helen M., Henrick Kim, Nakamura Haruki, Akutsu Hideo: BioMagResBank (BMRB) as a partner in the Worldwide Protein Data Bank (wwPDB): new policies affecting biomolecular NMR depositions. J Biomol NMR 2008, 40, 153. <http://dx.doi.org/10.1007/s10858-008-9221-y>
• Geng Yong, Feng Yingang, Xie Tao, Dai Yuanyuan, Wang Jinfeng, Lu Shih-Hsin: Mapping the putative binding site for uPA protein in Esophageal Cancer-Related Gene 2 by heteronuclear NMR method. Archives of Biochemistry and Biophysics 2008, 479, 153. <http://dx.doi.org/10.1016/j.abb.2008.08.023>
• Yang Hao, Zhan Yingqian, Fenn Dickson, Chi Lai Man, Lam Sik Lok: Effect of 1-methyladenine on double-helical DNA structures. FEBS Letters 2008, 582, 1629. <http://dx.doi.org/10.1016/j.febslet.2008.04.013>
• Fenn Dickson, Chi Lai Man, Lam Sik Lok: Effect of hyperoxidized guanine on DNA primer–template structures: Spiroiminodihydantoin leads to strand slippage. FEBS Letters 2008, 582, 4169. <http://dx.doi.org/10.1016/j.febslet.2008.11.021>
• Bodner Michele L., Gabrys Charles M., Struppe Jochem O., Weliky David P.: [sup 13]C–[sup 13]C and [sup 15]N–[sup 13]C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations. J Chem Phys 2008, 128, 052319. <http://dx.doi.org/10.1063/1.2829984>
• Prokhorov D. A., Timchenko M. A., Kudrevatykh Yu. A., Fedyukina D. V., Gushchina L. V., Khristoforov V. S., Filimonov V. V., Kutyshenko V. P.: Study of the structure and dynamics of a chimeric variant of the SH3 domain (SHA-Bergerac) by NMR spectroscopy. Rus J Bioorg Chem 2008, 34, 578. <http://dx.doi.org/10.1134/S1068162008050075>
• Masternak Anna, Skalski Bogdan, Milecki Jan: NMR spectra of the tautomeric mixture of two forms of 6-azidopurine ribonucleoside labeled with15N. J Labelled Cpd Radiopharm 2007, 50, 43. <http://dx.doi.org/10.1002/jlcr.1155>
• Franks W. Trent, Kloepper Kathryn D., Wylie Benjamin J., Rienstra Chad M.: Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins. J Biomol NMR 2007, 39, 107. <http://dx.doi.org/10.1007/s10858-007-9179-1>
• Feng Yingang, Liu Dongsheng, Yao Hongwei, Wang Jinfeng: Solution structure and mapping of a very weak calcium-binding site of human translationally controlled tumor protein by NMR. Archives of Biochemistry and Biophysics 2007, 467, 48. <http://dx.doi.org/10.1016/j.abb.2007.08.021>
• Ulrich E. L., Akutsu H., Doreleijers J. F., Harano Y., Ioannidis Y. E., Lin J., Livny M., Mading S., Maziuk D., Miller Z.: BioMagResBank. Nucleic Acids Res 2007, 36, D402. <http://dx.doi.org/10.1093/nar/gkm957>
• León Esther, Yee Adelinda, Ortíz Angel R., Santoro Jorge, Rico Manuel, Jiménez M. Angeles: Solution structure of the hypothetical protein TA0095 from Thermoplasma acidophilum: A novel superfamily with a two-layer sandwich architecture. Protein Sci 2007, 16, 2278. <http://dx.doi.org/10.1110/ps.072869607>
• Rovnyak David, Thompson Laura E.: An accessible two-dimensional solution nuclear magnetic resonance experiment on human ubiquitin*. Biochem Mol Biol Educ 2006, 33, 117. <http://dx.doi.org/10.1002/bmb.2005.494033022423>
• Hoffman Roy E.: Standardization of chemical shifts of TMS and solvent signals in NMR solvents. Magn Reson Chem 2006, 44, 606. <http://dx.doi.org/10.1002/mrc.1801>
• Kim Yong-Ick, Manalo Marlon N., Peréz Lisa M., LiWang Andy: Computational and Empirical Trans-hydrogen Bond Deuterium Isotope Shifts Suggest that N1–N3 A:U Hydrogen Bonds of RNA are Shorter than those of A:T Hydrogen Bonds of DNA. J Biomol NMR 2006, 34, 229. <http://dx.doi.org/10.1007/s10858-006-0021-y>
• Kobayashi Masatoshi, Matsuki Yoh, Yumen Ikuko, Fujiwara Toshimichi, Akutsu Hideo: Signal assignment and secondary structure analysis of a uniformly [13C, 15N]-labeled membrane protein, H+-ATP synthase subunit c, by magic-angle spinning solid-state NMR. J Biomol NMR 2006, 36, 279. <http://dx.doi.org/10.1007/s10858-006-9094-x>
• Neudecker Philipp, Zarrine-Afsar Arash, Choy Wing-Yiu, Muhandiram D. Ranjith, Davidson Alan R., Kay Lewis E.: Identification of a Collapsed Intermediate with Non-native Long-range Interactions on the Folding Pathway of a Pair of Fyn SH3 Domain Mutants by NMR Relaxation Dispersion Spectroscopy. Journal of Molecular Biology 2006, 363, 958. <http://dx.doi.org/10.1016/j.jmb.2006.08.047>
• Ivleva N. B., Gao T., LiWang A. C., Golden S. S.: Quinone sensing by the circadian input kinase of the cyanobacterial circadian clock. Proceedings of the National Academy of Sciences 2006, 103, 17468. <http://dx.doi.org/10.1073/pnas.0606639103>
• Banerjee Amit: Novel targets in drug design: enzymes in the protein ubiquitylation pathway. Expert Opin Drug Discov 2006, 1, 151. <http://dx.doi.org/10.1517/17460441.1.2.151>
• Sicinska Wanda, Westler William M., DeLuca Hector F.: NMR assignments of tryptophan residue in apo and holo LBD-rVDR. Proteins 2005, 61, 461. <http://dx.doi.org/10.1002/prot.20625>
• Morcombe Corey R., Paulson Eric K., Gaponenko Vadim, Byrd R. Andrew, Zilm Kurt W.: 1H–15N correlation spectroscopy of nanocrystalline proteins. J Biomol NMR 2005, 31, 217. <http://dx.doi.org/10.1007/s10858-005-0527-8>
• Hoffman Roy E., Becker Edwin D.: Temperature dependence of the 1H chemical shift of tetramethylsilane in chloroform, methanol, and dimethylsulfoxide. J  Magn Reson 2005, 176, 87. <http://dx.doi.org/10.1016/j.jmr.2005.05.015>
• Duarte Iola F., Goodfellow Brian J., Gil Ana M., Delgadillo Ivonne: Characterization of Mango Juice by High‐Resolution NMR, Hyphenated NMR, and Diffusion‐Ordered Spectroscopy. Spec Lett 2005, 38, 319. <http://dx.doi.org/10.1081/SL-200058713>
• Neudecker Philipp, Nerkamp Jörg, Eisenmann Anke, Nourse Amanda, Lauber Thomas, Schweimer Kristian, Lehmann Katrin, Schwarzinger Stephan, Ferreira Fátima, Rösch Paul: Solution Structure, Dynamics, and Hydrodynamics of the Calcium-bound Cross-reactive Birch Pollen Allergen Bet v 4 Reveal a Canonical Monomeric Two EF-Hand Assembly with a Regulatory Function. Journal of Molecular Biology 2004, 336, 1141. <http://dx.doi.org/10.1016/j.jmb.2003.12.070>
• Gronwald Wolfram, Kalbitzer Hans Robert: Automated structure determination of proteins by NMR spectroscopy. Progr Nucl Magn Reson Spectrosc 2004, 44, 33. <http://dx.doi.org/10.1016/j.pnmrs.2003.12.002>
• Preece Nicholas E, Nguyen Minh, Mahata Manjula, Mahata Sushil K, Mahapatra Nitish R, Tsigelny Igor, O'Connor Daniel T: Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A. REGUL PEPT 2004, 118, 75. <http://dx.doi.org/10.1016/j.regpep.2003.10.035>
• Vermeulen Wim, Vanhaesebrouck Peter, Van Troys Marleen, Verschueren Mieke, Fant Franky, Goethals Marc, Ampe Christophe, Martins José C., Borremans Frans A.M.: Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements. Protein Sci 2004, 13, 1276. <http://dx.doi.org/10.1110/ps.03518104>
• Ruchala P., Picur B., Lisowski M., Cierpicki T., Wieczorek Z., Siemion I.Z.: Synthesis, conformation, and immunosuppressive activity of CLX and its analogues. Biopolymers (Biospectroscopy) 2003, 70, 497. <http://dx.doi.org/10.1002/bip.10422>
• Petkova Aneta T, Baldus Marc, Belenky Marina, Hong Mei, Griffin Robert G, Herzfeld Judith: Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state. J  Magn Reson 2003, 160, 1. <http://dx.doi.org/10.1016/S1090-7807(02)00137-4>
• Morcombe Corey R, Zilm Kurt W: Chemical shift referencing in MAS solid state NMR. J  Magn Reson 2003, 162, 479. <http://dx.doi.org/10.1016/S1090-7807(03)00082-X>
• Nowick James S., Khakshoor Omid, Hashemzadeh Mehrnoosh, Brower Justin O.: DSA:  A New Internal Standard for NMR Studies in Aqueous Solution. Org Lett 2003, 5, 3511. <http://dx.doi.org/10.1021/ol035347w>
• Heitmann Bjorn, Maurer Till, Weitzel Joachim M., Stratling Wolf H., Kalbitzer Hans Robert, Brunner Eike: Solution structure of the matrix attachment region-binding domain of chicken MeCP2. Eur J Biochem 2003, 270, 3263. <http://dx.doi.org/10.1046/j.1432-1033.2003.03714.x>
• Harris Robin K., Becker Edwin D., Cabral de Menezes Sonia M., Goodfellow Robin, Granger Pierre: NMR nomenclature: nuclear spin properties and conventions for chemical shifts. IUPAC Recommendations 2001. International Union of Pure and Applied Chemistry. Physical Chemistry Division. Commission on Molecular Structure and Spectroscopy. Magn Reson Chem 2002, 40, 489. <http://dx.doi.org/10.1002/mrc.1042>
• Harris Robin K.: Editorial. Magn Reson Chem 2002, 40, 431. <http://dx.doi.org/10.1002/mrc.1045>
• Vranken Wim F., James Susan, Bennett Hugh P.J., Ni Feng: Solution structures of a 30-residue amino-terminal domain of the carp granulin-1 protein and its amino-terminally truncated 3-30 subfragment: Implications for the conformational stability of the stack of two β-hairpins. Proteins 2002, 47, 14. <http://dx.doi.org/10.1002/prot.10077>
• Harris Robin K., Becker Edwin D.: NMR Nomenclature: Nuclear Spin Properties and Conventions for Chemical Shifts—IUPAC Recommendations. J  Magn Reson 2002, 156, 323. <http://dx.doi.org/10.1006/jmre.2002.2554>
• Surmacz Tatiana Anna, Bayer Elena, Rahfeld Jens-Ulrich, Fischer Gunter, Bayer Peter: The N-terminal Basic Domain of Human Parvulin hPar14 is Responsible for the Entry to the Nucleus and High-affinity DNA-binding. Journal of Molecular Biology 2002, 321, 235. <http://dx.doi.org/10.1016/S0022-2836(02)00615-0>
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