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Torsion angle dynamics for NMR structure calculation with the new program Dyana

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Protein NMR Structure Determination with Automated NOE Assignment Using the New Software CANDID and the Torsion Angle Dynamics Algorithm DYANA

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Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from β-spectrin 1 1Edited by P. E. Wright

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Stable and biocompatible cystine knot peptides from the marine sponge Asteropus sp.

Su, M., Li, H., Wang, H., Kim, E. L., Kim, H. S., Kim, E., Lee, J., & Jung, J. H. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.05.006 · Cited by 10

Novel Lysine-Rich Delivery Peptides of Plant Origin ERD and Human S100: The Effect of Carboxyfluorescein Conjugation, Influence of Aromatic and Proline Residues, Cellular Internalization, and Penetration Ability

Sebák, F., Horváth, L. B., Kovács, D., Szolomájer, J., Tóth, G. K., Babiczky, Á., Bősze, S. E., & Bodor, A. (2021) · ACS Omega · doi:10.1021/acsomega.1c04637 · Cited by 9

NMR structure of a phosphatidyl‐ethanolamine binding protein from Drosophila

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Expanding the MiniAp‐4 BBB‐shuttle family: Evaluation of proline cis‐trans ratio as tool to fine‐tune transport

Fuster, C., Varese, M., García, J., Giralt, E., Sánchez‐Navarro, M., & Teixidò, M. (2019) · Journal of Peptide Science · doi:10.1002/psc.3172 · Cited by 9

A Model for the Solution Structure of Human Fe(II)-Bound Acireductone Dioxygenase and Interactions with the Regulatory Domain of Matrix Metalloproteinase I (MMP-I)

Liu, X., Garber, A., Ryan, J., Deshpande, A. R., Ringe, D., & Pochapsky, T. C. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00724 · Cited by 9

NMR study of non-structural proteins—part II: 1H, 13C, 15N backbone and side-chain resonance assignment of macro domain from Venezuelan equine encephalitis virus (VEEV)

Makrynitsa, G. I., Ntonti, D., Marousis, K. D., Tsika, A. C., Lichière, J., Papageorgiou, N., Coutard, B., Bentrop, D., & Spyroulias, G. A. (2014) · Biomolecular NMR Assignments · doi:10.1007/s12104-014-9584-9 · Cited by 9

NMR assignments of juvenile hormone binding protein in complex with JH III

Suzuki, R., Tase, A., Fujimoto, Z., Shiotsuki, T., & Yamazaki, T. (2009) · Biomolecular NMR Assignments · doi:10.1007/s12104-009-9144-x · Cited by 9

NMR structure note: PHD domain from death inducer obliterator protein and its interaction with H3K4me3

Santiveri, C. M., García‐Mayoral, M. F., Pérez‐Cañadillas, J. M., & Jiménez, M. A. (2013) · Journal of Biomolecular NMR · doi:10.1007/s10858-013-9726-x · Cited by 9

Trp-Trp pairs as β-hairpin stabilisers: Hydrogen-bonded versus non-hydrogen-bonded sites

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The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil

de Opakua, A. I., Merino, N., Villate, M., Cordeiro, T. N., Ormaza, G., Sänchez‐Carbayo, M., Diercks, T., Bernadó, P., & Blanco, F. J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0172507 · Cited by 9

Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation

Zhang, N., Chang, Y., Tseng, R., Ovchinnikov, S., Schwarz, R., & LiWang, A. (2020) · Protein Science · doi:10.1002/pro.3952 · Cited by 9

The Ni(II)-Binding Activity of the Intrinsically Disordered Region of Human NDRG1, a Protein Involved in Cancer Development

Beniamino, Y., Cenni, V., Piccioli, M., Ciurli, S., & Zambelli, B. (2022) · Biomolecules · doi:10.3390/biom12091272 · Cited by 7

Recombinant Production, NMR Solution Structure, and Membrane Interaction of the Phα1β Toxin, a TRPA1 Modulator from the Brazilian Armed Spider Phoneutria nigriventer

Lyukmanova, E. N., Mironov, P. A., Kulbatskii, D. S., Shulepko, M. A., Paramonov, A. S., Chernaya, E. M., Logashina, Y. A., Andreev, Y. A., Kirpichnikov, M. P., & Shenkarev, Z. O. (2023) · Toxins · doi:10.3390/toxins15060378 · Cited by 8

NMR structure note: N-terminal domain of Thermus thermophilus CdnL

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Synthesis, Structural Characterization, and Bioactivity of the Stable Peptide RCB-1 from Ricinus communis

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Solution Structure of the Conserved Hypothetical Protein Rv2302 from Mycobacterium tuberculosis

Buchko, G. W., Kim, C., Terwilliger, T. C., & Kennedy, M. A. (2006) · Journal of Bacteriology · doi:10.1128/jb.00460-06 · Cited by 8

Identification of Polyproline II Regions Derived From the Proline‐Rich Nuclear Receptor Coactivators PNRC and PNRC2: New Insights for ERα Coactivator Interactions

Byrne, C., Miclet, E., Broutin, I., Gallo, D., Pelekanou, V., Kampa, M., Castanas, E., Leclercq, G., & Jacquot, Y. (2013) · Chirality · doi:10.1002/chir.22188 · Cited by 8

Crystallomycin revisited after 60 years: aspartocins B and C

Tyurin, A. P., Alferova, V. A., Paramonov, A. S., Shuvalov, M. V., Алексеевна, М. И., Grammatikova, N. E., Solyev, P. N., Liu, S., Sun, C., Prokhorenko, I. A., et al. (2018) · MedChemComm · doi:10.1039/c8md00002f · Cited by 8

A Trade between Similar but Nonequivalent Intrasubunit and Intersubunit Contacts in Cro Dimer Evolution,

Newlove, T., Atkinson, K. R., Dorn, L. O. V., & Cordes, M. H. J. (2006) · Biochemistry · doi:10.1021/bi052541c · Cited by 8

Acetylation and hydration treatment of recombinant spider silk fiber, and their characterization using 13C NMR spectroscopy

Asakura, T., Matsuda, H., Aoki, A., & Naito, A. (2022) · Polymer · doi:10.1016/j.polymer.2022.124605 · Cited by 7

Insight into polyproline II helical bundle stability in an antifreeze protein denatured state

Treviño, M. Á., López‐Sánchez, R., Moya, M. R., Pantoja‐Uceda, D., Mompeán, M., & Laurents, D. V. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.10.034 · Cited by 7

Electron Transfer Mechanism of the Rieske Protein from Thermus thermophilus from Solution Nuclear Magnetic Resonance Investigations

Hsueh, K.-L., Tonelli, M., Cai, K., Westler, W. M., & Markley, J. L. (2013) · Biochemistry · doi:10.1021/bi400296c · Cited by 7

Letter to the Editor: Complete 1H, 15N and 13C Assignment of the Soluble Domain of the ba 3 Oxidase Subunit II of Thermus Thermophilus in the Reduced State

Mukrasch, M. D., Lücke, C., Löhr, F., Maneg, O., Ludwig, B., & Rüterjans, H. (2004) · Journal of Biomolecular NMR · doi:10.1023/b:jnmr.0000013687.83263.b5 · Cited by 7

Complete sequential assignment and secondary structure prediction of the cannulae forming protein CanA from the hyperthermophilic archaeon Pyrodictium abyssi

Kreitner, R., Munte, C. E., Singer, K., STETTER, K. O., Horn, G., Kremer, W., & Kalbitzer, H. R. (2020) · Biomolecular NMR Assignments · doi:10.1007/s12104-020-09934-x · Cited by 6

Structural Plasticity as a Driver of the Maturation of Pro-Interleukin-18

Bonin, J. P., Aramini, J. M., & Kay, L. E. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c09805 · Cited by 5

Backbone and nearly complete side-chain chemical shift assignments of the human death-associated protein 1 (DAP1)

Wiedemann, C., Voigt, J., Jirschitzka, J., Häfner, S., Ohlenschläger, O., & Bordusa, F. (2020) · Biomolecular NMR Assignments · doi:10.1007/s12104-020-09988-x · Cited by 6

Total synthesis of a reversed cyclopurpuracin using a combination of solid and solution phase methods

Yayat, H. N. A., Maharani, R., Hidayat, A. T., Wiani, I., Zainuddin, A., Mayanti, T., Nurlelasari, N., Harneti, D., & Supratman, U. (2022) · Journal of Heterocyclic Chemistry · doi:10.1002/jhet.4532 · Cited by 6

Solution structure of an arsenate reductase-related protein, YffB, fromBrucella melitensis, the etiological agent responsible for brucellosis

Buchko, G. W., Hewitt, S. N., Napuli, A. J., A, W. C. V. V., & Myler, P. J. (2011) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309111006336 · Cited by 6

1H, 13C, 15N backbone and side-chain resonance assignment of Nostoc sp. C139A variant of the heme–nitric oxide/oxygen binding (H-NOX) domain

Alexandropoulos, I. I., Argyriou, A. I., Marousis, K. D., Topouzis, S., Papapetropoulos, A., & Spyroulias, G. A. (2016) · Biomolecular NMR Assignments · doi:10.1007/s12104-016-9707-6 · Cited by 6

Peptide Toxin Structure and Function by NMR

Norton, R. S. (2018) · Springer eBooks · doi:10.1007/978-3-319-28388-3_120 · Cited by 6

NMR resonance assignments for the GSPII-C domain of the PilF ATPase from Thermus thermophilus in complex with c-di-GMP

Keller, H., Kruse, K., Averhoff, B., Duchardt, E., & Wöhnert, J. (2019) · Biomolecular NMR Assignments · doi:10.1007/s12104-019-09906-w · Cited by 6

NMR spectroscopic studies of a TAT-derived model peptide in imidazolium-based ILs: influence on chemical shifts and the cis/trans equilibrium state

Wiedemann, C., Ohlenschläger, O., Mrestani‐Klaus, C., & Bordusa, F. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp03295a · Cited by 6

Recombinant production and structural studies of the human Lypd6 and Lypd6b proteins

Paramonov, A. S., Kulbatskii, D. S., Loktyushov, E. V., Tsarev, A. V., Dolgikh, D. A., Shenkarev, Z. O., Kirpichnikov, M. P., & Lyukmanova, E. N. (2017) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162017060127 · Cited by 6

Amyloid Oligomers: Expediting Crystal Growth and Revisiting the Corkscrew Structures

Hirschbeck, S. S., Sawaya, M. R., Lindberg, E. T., Limbach, M. N., Jang, J. H., Cantrell, K. L., Eisenberg, D. S., & Do, T. D. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c00656 · Cited by 5

P450 cyptide synthase MpoB catalyzes the cross-linking of the YPW motif on the precursor peptide

Khan, A. H., Haedar, J. R., Kiselov, V., Romaņuks, V., Šmits, G., Donadio, S., & Phan, C. (2025) · RSC Chemical Biology · doi:10.1039/d5cb00153f · Cited by 5

2-Alkyl-2-carboxyazetidines as γ-turn inducers: incorporation into neurotrophin fragments

Baeza, J. L., Bonache, M. Á., López, M. G., González‐Muñiz, R., & Martín‐Martinez, M. (2010) · Amino Acids · doi:10.1007/s00726-010-0569-4 · Cited by 5

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Napolitano, S., Pokharna, A., Glockshuber, R., & Gossert, A. D. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.10.040 · Cited by 5

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Wiedemann, C., Goretzki, B., Merz, Z. N., Tebbe, F., Schmitt, P., & Hellmich, U. A. (2022) · Biomolecular NMR Assignments · doi:10.1007/s12104-022-10093-4 · Cited by 5

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Huang, B., Fu, J., Guo, C., Wu, X., Lin, D., & Liao, X. (2016) · Biomolecular NMR Assignments · doi:10.1007/s12104-016-9692-9 · Cited by 5

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Adler, A., Kjaer, L. F., Beugelink, J. W., Baldus, M., & van Ingen, H. (2023) · Biomolecular NMR Assignments · doi:10.1007/s12104-023-10124-8 · Cited by 5

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Miyamoto, K., Nakatani, A., & Saito, K. (2017) · Protein Science · doi:10.1002/pro.3301 · Cited by 5

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Galera‐Prat, A., Pantoja‐Uceda, D., Laurents, D. V., & Carrión‐Vázquez, M. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.02.016 · Cited by 5

NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii

Watzel, J., Sarawi, S., Duchardt, E., Bode, H. B., & Wöhnert, J. (2021) · Biomolecular NMR Assignments · doi:10.1007/s12104-021-10010-1 · Cited by 5

1H, 15N, 13C assignment and secondary structure determination of two domains of La protein from D. discoideum

Apostolidi, M., Vourtsis, D. J., Chasapis, C. T., Stathopoulos, C., Bentrop, D., & Spyroulias, G. A. (2012) · Biomolecular NMR Assignments · doi:10.1007/s12104-012-9450-6 · Cited by 5

NMR study of Met-1 human Angiogenin: 1H, 13C, 15N backbone and side-chain resonance assignment

Tsika, A. C., Chatzileontiadou, D. S. M., Leonidas, D. D., & Spyroulias, G. A. (2016) · Biomolecular NMR Assignments · doi:10.1007/s12104-016-9704-9 · Cited by 5

Structural basis of interdomain communication in PPARγPreprint

Mosure, S. A., Munoz‐Tello, P., Kuo, K.-T., MacTavish, B. S., Yu, X., Scholl, D., Williams, C. C., Strutzenberg, T. S., Li, J., Bass, J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.13.499031 · Cited by 6

Sea Anemone Kunitz Peptide HCIQ2c1: Structure, Modulation of TRPA1 Channel, and Suppression of Nociceptive Reaction In Vivo

Николаевна, К. А., Oreshkov, S. D., Mironov, P. A., Zaigraev, M. M., Климович, А. А., Deriavko, Y. V., Menshov, A. S., Kulbatskii, D. S., Logashina, Y. A., Andreev, Y. A., et al. (2024) · Marine Drugs · doi:10.3390/md22120542 · Cited by 4

Comprehensive Analysis of Coupled Proline Cis–Trans States in Bradykinin Using ωBP-REMD Simulations

Kienlein, M., Zacharias, M., & Reif, M. (2024) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.3c01356 · Cited by 4

Structure and functional studies of Avt1, a novel peptide from the sea anemone Aulactinia veratra

Albar, R. A. A., Smith, H. L., Sanches, K., Wai, D. C. C., Naseem, M. U., Szanto, T. G., Panyi, G., Prentis, P. J., & Norton, R. S. (2024) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2024.141050 · Cited by 4

Conformational Consequences of Regio‐ and Stereoselective Disulfide Bridge Oxidation in a Cyclic Peptide

Malešević, M., Jahreis, G., Wawra, S., Fischer, G., & Lücke, C. (2007) · ChemBioChem · doi:10.1002/cbic.200700529 · Cited by 4

Solution structural study of a proline-rich decapeptide

Miclet, E., Jacquot, Y., Goasdoué, N., & Lavielle, S. (2007) · Comptes Rendus Chimie · doi:10.1016/j.crci.2007.06.016 · Cited by 4

1H, 13C, and 15N resonance assignments for the pro-inflammatory cytokine interleukin-36α

Goradia, N., Wißbrock, A., Wiedemann, C., Bordusa, F., Ramachandran, R., Imhof, D., & Ohlenschläger, O. (2016) · Biomolecular NMR Assignments · doi:10.1007/s12104-016-9694-7 · Cited by 4

Automatic 13C chemical shift reference correction for unassigned protein NMR spectra

Chen, X., Smelter, A., & Moseley, H. (2018) · Journal of Biomolecular NMR · doi:10.1007/s10858-018-0202-5 · Cited by 4

1H, 13C and 15N resonance assignments for the microtubule-binding domain of the kinetoplastid kinetochore protein KKT4 from Trypanosoma brucei

Ludzia, P., Akiyoshi, B., & Redfield, C. (2020) · Biomolecular NMR Assignments · doi:10.1007/s12104-020-09968-1 · Cited by 4

Lingaoamide, a cyclic heptapeptide from a Chinese freshwater cyanobacterium Oscillatoria sp.

Iwasaki, A., Kurisawa, N., Wang, T., Li, X., Luo, H., Zhu, C.-C., Patial, G., Yan, X., He, S., Luzzatto‐Knaan, T., et al. (2021) · Tetrahedron Letters · doi:10.1016/j.tetlet.2021.153214 · Cited by 4

Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein

Wiedemann, C., Obika, K. B., Liebscher, S., Jirschitzka, J., Ohlenschläger, O., & Bordusa, F. (2022) · Biomolecular NMR Assignments · doi:10.1007/s12104-022-10086-3 · Cited by 4

Assignment of the disordered, proline-rich N-terminal domain of the tumour suppressor p53 protein using 1HN and 1Hα-detected NMR measurements

Sebák, F., Ecsédi, P., Nyitray, L., & Bodor, A. (2023) · Biomolecular NMR Assignments · doi:10.1007/s12104-023-10160-4 · Cited by 4

Backbone and side chain NMR assignment, along with the secondary structure prediction of RRM2 domain of La protein from a lower eukaryote exhibiting identical structural organization with its human homolog

Argyriou, A. I., Chasapis, C. T., Apostolidi, M., Κωνσταντινίδου, Π., Stathopoulos, C., Bentrop, D., & Spyroulias, G. A. (2014) · Biomolecular NMR Assignments · doi:10.1007/s12104-014-9578-7 · Cited by 4

Oligopeptide cyclophilin inhibitors: A reassessment

Schümann, M., Jahreis, G., Kahlert, V., Lücke, C., & Fischer, G. S. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.09.019 · Cited by 4

1H, 13C and 15N resonance assignments of human parvulin 17

Lin, Y.-J., Schmidt, A., Burgardt, N. I., Thiele, A., Weiwad, M., & Lücke, C. (2012) · Biomolecular NMR Assignments · doi:10.1007/s12104-012-9438-2 · Cited by 4

NMR evidence of charge‐dependent interaction between various PND V3 and CCR5 N‐terminal peptides

Galanakis, P., Kandias, N. G., Rizos, A. K., Morikis, D., Krambovitis, E., & Spyroulias, G. A. (2008) · Biopolymers · doi:10.1002/bip.21127 · Cited by 4

Conformationally constrained cyclic grafted peptidomimetics targeting protein–protein interactions

Dahal, A., Vivekanandan, S., Shrestha, P., Liu, D., Gauthier, T. J., & Jois, S. D. S. (2023) · Peptide Science · doi:10.1002/pep2.24328 · Cited by 3

Conformational dynamics in specialized C2H2 zinc finger domains enable zinc‐responsive gene repression in S. pombe

Wadhwa, V., Jamshidi, C., Stachowski, K., Bird, A. J., & Foster, M. P. (2025) · Protein Science · doi:10.1002/pro.70044 · Cited by 3

1H, 13C, 15N backbone and side-chain resonance assignment of the native form of UbcH7 (UBE2L3) through solution NMR spectroscopy

Marousis, K. D., Birkou, M., Asimakopoulou, A., & Spyroulias, G. A. (2019) · Biomolecular NMR Assignments · doi:10.1007/s12104-019-09923-9 · Cited by 3

Backbone and side chain NMR assignments of the H-NOX domain from Nostoc sp. in complex with BAY58-2667 (cinaciguat)

Makrynitsa, G. I., Argyriou, A. I., Dalkas, G. A., Georgopoulou, D. A., Bantzi, M., Giannis, A., Papapetropoulos, A., & Spyroulias, G. A. (2020) · Biomolecular NMR Assignments · doi:10.1007/s12104-020-09982-3 · Cited by 3

A scorpion toxin affecting sodium channels shows double cis – trans isomerism

Mineev, K. S., Chernykh, M. A., Motov, V. V., Prudnikova, D. A., Pavlenko, D. M., Kuzmenkov, A. I., Peigneur, S., Tytgat, J., & Vassilevski, A. A. (2023) · FEBS Letters · doi:10.1002/1873-3468.14705 · Cited by 4

Dual FGFR-targeting and pH-activatable ruthenium–peptide conjugates for targeted therapy of breast cancer

Machado, J. F., de Sá, M., Pires, I. D. S., Silva, M., Marques, F., Coelho, J. A. S., Mendes, F., Piedade, M. F. M., Machuqueiro, M., Jiménez, M. A., et al. (2024) · Dalton Transactions · doi:10.1039/d4dt00497c · Cited by 3

Characterization of the two conformations adopted by the T3SS inner‐membrane protein PrgK

Bergeron, J. R. C., Brockerman, J., Vuckovic, M., Deng, W., Okon, M., Finlay, B. B., McIntosh, L. P., & Strynadka, N. C. J. (2018) · Protein Science · doi:10.1002/pro.3447 · Cited by 3

1H, 13C and 15N resonance assignments and secondary structure of the human PHF6-ePHD1 domain

Bao, Y., Liu, Z., Zhang, J., Wu, J., & Shi, Y. (2015) · Biomolecular NMR Assignments · doi:10.1007/s12104-015-9627-x · Cited by 3

1H, 13C and 15N backbone and side chain resonance assignments of a Myxococcus xanthus anti-repressor with no known sequence homologues

León, E., González, C., Arnanz, M. E., Padmanabhan, S., & Jiménez, M. A. (2009) · Biomolecular NMR Assignments · doi:10.1007/s12104-008-9136-2 · Cited by 3

1H, 13C and 15N resonance assignments of the N-terminal domain of Vta1–Vps60 peptide complex

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