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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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A relational database for sequence-specific protein NMR data

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Magic-Angle Spinning NMR of a Class I Filamentous Bacteriophage Virus

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High yield expression and NMR characterization of Arkadia E3 ubiquitin ligase RING-H2 finger domain

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Solution Structure of CCP Modules 10–12 Illuminates Functional Architecture of the Complement Regulator, Factor H

Makou, E., Mertens, H. D. T., Maciejewski, M., Soares, D. C., Matis, I., Schmidt, C. Q., Herbert, A. P., Svergun, D. I., & Barlow, P. N. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.09.013 · Cited by 26

Functional Insights from the Structure of the Multifunctional C345C Domain of C5 of Complement

Bramham, J., Thai, C.-T., Soares, D. C., Uhrı́n, D., Ogata, R. T., & Barlow, P. N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413126200 · Cited by 26

Solution structure of the C1‐subdomain of Bacillus stearothermophilus translation initiation factor IF2

Wienk, H., Tomaselli, S., Bernard, C., Spurio, R., Picone, D., Gualerzi, C. O., & Boelens, R. (2005) · Protein Science · doi:10.1110/ps.051531305 · Cited by 26

Differential conformational dynamics in the closely homologous FK506-binding domains of FKBP51 and FKBP52

Mustafi, S. M., LeMaster, D. M., & Hernández, G. (2014) · Biochemical Journal · doi:10.1042/bj20140232 · Cited by 25

Solution structure of the zinc finger HIT domain in protein FON

He, F., Umehara, T., Tsuda, K., Inoue, M., Kigawa, T., Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Terada, T., et al. (2007) · Protein Science · doi:10.1110/ps.062635107 · Cited by 25

A Tryptophan-Rich Hexapeptide Inhibits Nucleic Acid Destabilization Chaperoned by the HIV-1 Nucleocapsid Protein

Raja, C., Ferner, J., Dietrich, U., Avilov, S., Ficheux, D., Darlix, J., de ROCQUIGNY, H., Schwalbe, H., & Mély, Y. (2006) · Biochemistry · doi:10.1021/bi052560m · Cited by 25

Revisiting the NMR solution structure of the Cel48S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation

Chen, C., Cui, Z., Xiao, Y., Cui, Q., Smith, S. P., Lamed, R., Bayer, E. A., & Feng, Y. (2014) · Journal of Structural Biology · doi:10.1016/j.jsb.2014.09.006 · Cited by 24

Structural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation by ERK2

Piserchio, A., Ramakrishan, V., Wang, H., Kaoud, T. S., Arshava, B. M., Dutta, K., Dalby, K. N., & Ghose, R. (2015) · Scientific Reports · doi:10.1038/srep11127 · Cited by 27

Disulfide and amide-bridged cyclic peptide analogues of the VEGF81–91 fragment: Synthesis, conformational analysis and biological evaluation

García-Aranda, M. I., Mirassou, Y., Gautier, B., Martín‐Martinez, M., Inguimbert, N., Vidal, M., García-López, M. T., Jiménez, M. A., González‐Muñiz, R., & de Vega, M. J. P. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.10.032 · Cited by 26

NMR structure of the mengovirus Leader protein zinc‐finger domain

Cornilescu, C. C., Porter, F., Zhao, K. Q., Palmenberg, A. C., & Markley, J. L. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.02.023 · Cited by 24

A structural and mechanistic study of π-clamp-mediated cysteine perfluoroarylation

Dai, P., Williams, J. K., Zhang, C., Welborn, M., Shepherd, J. J., Zhu, T., Voorhis, T. V., Hong, M., & Pentelute, B. L. (2017) · Scientific Reports · doi:10.1038/s41598-017-08402-2 · Cited by 24

The Solution Structure and Dynamics of Cd-Metallothionein from Helix pomatia Reveal Optimization for Binding Cd over Zn

Beil, A., Jurt, S., Walser, R., Schönhut, T., Güntert, P., Palacios, Ò., Atrian, S., Capdevila, M., Dallinger, R., & Zerbe, O. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00830 · Cited by 26

Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A2-activating Protein

Fu, Q., Zhou, C.-J., Gao, H.-C., Jiang, Y., Zhou, Z., Hong, J., Yao, W., Song, A., Lin, D., & Hu, H.-Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.009126 · Cited by 24

COPS—Cis/transpeptide bond conformation prediction of amino acids on the basis of secondary structure information

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A Cyclic Peptidic Serine Protease Inhibitor: Increasing Affinity by Increasing Peptide Flexibility

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Structures of domains I and IV from YbbR are representative of a widely distributed protein family

Barb, A. W., Cort, J., Seetharaman, J., Lew, S., Lee, H., Acton, T., Xiao, R., Kennedy, M. A., Tong, L., Montelione, G. T., et al. (2010) · Protein Science · doi:10.1002/pro.571 · Cited by 23

Structural Difference between Group I and Group II Cobra Cardiotoxins: X-ray, NMR, and CD Analysis of the Effect of cis-Proline Conformation on Three-Fingered Toxins

Chen, T.-S., Chung, F.-Y., Tjong, S.-C., Goh, K.-S., Huang, W., Chien, K., Wu, P.-L., Lin, H.-C., Chen, C., & Wu, W. (2005) · Biochemistry · doi:10.1021/bi050172e · Cited by 23

Solution structure of the antifreeze‐like domain of human sialic acid synthase

Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., et al. (2006) · Protein Science · doi:10.1110/ps.051700406 · Cited by 23

A cis-Proline in α-Hemoglobin Stabilizing Protein Directs the Structural Reorganization of α-Hemoglobin

Gell, D. A., Feng, L., Zhou, S., Jeffrey, P. D., Bendak, K., Gow, A. J., Weiss, M. J., Shi, Y., & Mackay, J. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.027045 · Cited by 23

Solution Structure of the THAP Domain from Caenorhabditis elegans C-terminal Binding Protein (CtBP)

Liew, C. K., Crossley, M., Mackay, J. P., & Nicholas, H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.058 · Cited by 23

Bicyclic Peptide Inhibitor of Urokinase‐Type Plasminogen Activator: Mode of Action

Roodbeen, R., Paaske, B., Jiang, L., Jensen, J. K., Christensen, A., Nielsen, J. T., Huang, M., Mulder, F. A. A., Nielsen, N. C., Andreasen, P. A., et al. (2013) · ChemBioChem · doi:10.1002/cbic.201300335 · Cited by 22

Solution structure of the RNA binding domain in the human muscleblind‐like protein 2

He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T., Matsuda, T., Yabuki, T., et al. (2008) · Protein Science · doi:10.1002/pro.17 · Cited by 22

Domain Reorientation and Induced Fit upon RNA Binding: Solution Structure and Dynamics of Ribosomal Protein L11 from Thermotoga maritima

Il'in, S. G., Hoskins, A. A., Ohlenschläger, O., Jonker, H. R. A., Schwalbe, H., & Wöhnert, J. (2005) · ChemBioChem · doi:10.1002/cbic.200500091 · Cited by 24

Solution Structures and Backbone Dynamics of Arsenate Reductase from Bacillus subtilis

Guo, X., Li, Y., Peng, K., Hu, Y., Li, C., Xia, B., & Jin, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508132200 · Cited by 22

Asteropsins B–D, sponge-derived knottins with potential utility as a novel scaffold for oral peptide drugs

Li, H., Bowling, J. J., Su, M., Hong, J., Lee, B., Hamann, M. T., & Jung, J. H. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.11.001 · Cited by 21

Insight into the Binding Properties of MEKK3 PB1 to MEK5 PB1 from Its Solution Structure,

Hu, Q., Shen, W., Huang, H., Liu, J., Zhang, J., Huang, X., Wu, J., & Shi, Y. (2007) · Biochemistry · doi:10.1021/bi701341n · Cited by 21

Structural Basis of the Role of the NikA Ribbon-Helix-Helix Domain in Initiating Bacterial Conjugation

Yoshida, H., Furuya, N., Lin, Y., Güntert, P., Komano, T., & Kainosho, M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.09.067 · Cited by 21

Ligand- and pH-Induced Structural Transition of Gypsy Moth Lymantria dispar Pheromone-Binding Protein 1 (LdisPBP1)

Terrado, M., Okon, M., McIntosh, L. P., & Plettner, E. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00592 · Cited by 20

Anti-inflammatory marine cyclic peptide stylissatin A and its derivatives inhibit differentiation of murine preadipocytes

Zhang, M., Sunaba, T., Sun, Y., Sasaki, K., Isoda, H., Kigoshi, H., & Kita, M. (2019) · Chemical Communications · doi:10.1039/c9cc02517k · Cited by 21

Further Evidence for 2-Alkyl-2-carboxyazetidines as γ-Turn Inducers

Baeza, J. L., Gerona‐Navarro, G., Thompson, K., de Vega, M. J. P., Infantes, L., López, M. G., González‐Muñiz, R., & Martín‐Martinez, M. (2009) · The Journal of Organic Chemistry · doi:10.1021/jo901712x · Cited by 20

The TβR-I Pre-Helix Extension Is Structurally Ordered in the Unbound Form and Its Flanking Prolines Are Essential for Binding

Zúñiga, J. E., Ilangovan, U., Mahlawat, P., Hinck, C. S., Huang, T., Groppe, J. C., McEwen, D. G., & Hinck, A. P. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.07.046 · Cited by 20

Insight into Disulfide Bond Catalysis in Chlamydia from the Structure and Function of DsbH, a Novel Oxidoreductase

Mac, T.-T., von Hacht, A., Hung, K.-C., Dutton, R. J., Boyd, D. H., Bardwell, J. C. A., & Ulmer, T. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707863200 · Cited by 20

Solution Structure of the Mouse Enhancer of Rudimentary Protein Reveals a Novel Fold

Li, H. L., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., et al. (2005) · Journal of Biomolecular NMR · doi:10.1007/s10858-005-7959-z · Cited by 20

The High-Precision Solution Structure of Yersinia Modulating Protein YmoA Provides Insight into Interaction with H-NS

McFeeters, R. L., Altieri, A. S., Cherry, S., Tropea, J. E., Waugh, D. S., & Byrd, R. A. (2007) · Biochemistry · doi:10.1021/bi701210j · Cited by 20

The NMR Structure and Dynamics of the Two-Domain Tick Carboxypeptidase Inhibitor Reveal Flexibility in Its Free Form and Stiffness upon Binding to Human Carboxypeptidase B

Pantoja‐Uceda, D., Arolas, J. L., García, P., López‐Hernández, E., Padró, D., Avilés, F. X., & Blanco, F. J. (2008) · Biochemistry · doi:10.1021/bi800403m · Cited by 20

Analysing the visible conformational substates of the FK506 binding protein FKBP12

Mustafi, S. M., Chen, H., Li, H., LeMaster, D. M., & Hernández, G. (2013) · Biochemical Journal · doi:10.1042/bj20130276 · Cited by 19

Structure, Dynamics, Lipid Binding, and Physiological Relevance of the Putative GTPase-binding Domain of Dictyostelium Formin C

Dames, S. A., Junemann, A., Sass, H. J., Schönichen, A., Stopschinski, B. E., Grzesiek, S., Faix, J., & Geyer, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225052 · Cited by 20

3D Structure Elucidation Using NMR Chemical Shifts

Sternberg, U., Witter, R., & Ulrich, A. S. (2004) · Annual reports on NMR spectroscopy · doi:10.1016/s0066-4103(04)52002-1 · Cited by 19

Consequences of Depsipeptide Substitution on the ClpP Activation Activity of Antibacterial Acyldepsipeptides

Li, Y., Lavey, N. P., Coker, J. A., Knobbe, J. E., Truong, D., Yu, H., Lin, Y., Nimmo, S. L., & Duerfeldt, A. S. (2017) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00320 · Cited by 18

Structural and functional characterisation of a novel peptide from the Australian sea anemone Actinia tenebrosa

Elnahriry, K. A., Wai, D. C. C., Krishnarjuna, B., Badawy, N. N., Chittoor, B., MacRaild, C. A., Williams‐Noonan, B. J., Surm, J. M., Chalmers, D. K., Zhang, A. H., et al. (2019) · Toxicon · doi:10.1016/j.toxicon.2019.07.002 · Cited by 20

Double Monoubiquitination Modifies the Molecular Recognition Properties of p15PAF Promoting Binding to the Reader Module of Dnmt1

Magaña, A. G., de Opakua, A. I., Merino, N., Monteiro, H. P., Diercks, T., Murciano‐Calles, J., Luque, I., Bernadó, P., Cordeiro, T. N., Biasio, A. D., et al. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00679 · Cited by 18

Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature

Nordyke, C. T., Ahmed, Y. M., Puterbaugh, R. Z., Bowman, G. R., & Varga, K. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.09.020 · Cited by 16

The C-Terminal V5 Domain of Protein Kinase Cα Is Intrinsically Disordered, with Propensity to Associate with a Membrane Mimetic

Yang, Y., & Igumenova, T. I. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065699 · Cited by 18

Solution Structure of an Antifreeze Protein CfAFP-501 from Choristoneura fumiferana

Li, C., Guo, X., Jia, Z., Xia, B., & Jin, C. (2005) · Journal of Biomolecular NMR · doi:10.1007/s10858-005-8206-3 · Cited by 18

Cooperation between a T Domain and a Minimal C‐Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS

Watzel, J., Duchardt, E., Sarawi, S., Bode, H. B., & Wöhnert, J. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202103498 · Cited by 17

Nearest-neighbor effects on backbone alpha and beta carbon chemical shifts in proteins

Wang, L., Eghbalnia, H. R., & Markley, J. L. (2007) · Journal of Biomolecular NMR · doi:10.1007/s10858-007-9193-3 · Cited by 17

Structural studies of the SET domain from RIZ1 tumor suppressor

Briknarová, K., Zhou, X., Satterthwait, A. C., Hoyt, D. W., Ely, K. R., & Huang, S. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.12.034 · Cited by 17

Basic Folded and Low-Populated Locally Disordered Conformers of SUMO-2 Characterized by NMR Spectroscopy at Varying Pressures

Kitahara, R., Zhao, C., Saito, K., Koshiba, S., Ioune, M., Kigawa, T., Yokoyama, S., & Akasaka, K. (2007) · Biochemistry · doi:10.1021/bi7014458 · Cited by 17

Unraveling Molecular Recognition of Glycan Ligands by Siglec-9 via NMR Spectroscopy and Molecular Dynamics Modeling

Atxabal, U., Nycholat, C. M., Pröpster, J. M., Fernández, A., Oyenarte, I., Lenza, M. P., Franconetti, A., Soares, C. O., Coelho, H., Marcelo, F., et al. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.3c00664 · Cited by 17

The Complex Energy Landscape of the Protein IscU

Bothe, J. R., Tonelli, M., Ali, I. K., Dai, Z., Frederick, R. O., Westler, W. M., & Markley, J. L. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.07.045 · Cited by 16

NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa

Oeemig, J. S., Ollila, O. H. S., & Iwaï, H. (2018) · PeerJ · doi:10.7717/peerj.5412 · Cited by 16

Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues

Felli, I. C., Bermel, W., & Pierattelli, R. (2021) · Magnetic Resonance · doi:10.5194/mr-2-511-2021 · Cited by 15

Interaction between ghrelin and the ghrelin receptor (GHS-R1a), a NMR study using living cells

Martín‐Pastor, M., Capua, A. D., Álvarez, C. J. P., Díaz, D., Jiménez‐Barbero, J., Casanueva, F. F., & Pazos, Y. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.01.004 · Cited by 16

Solution structure of the Src homology 2 domain from␣the human feline sarcoma oncogene Fes

Scott, A., Pantoja‐Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S., et al. (2005) · Journal of Biomolecular NMR · doi:10.1007/s10858-005-0946-6 · Cited by 16

Phosphorylation-dependent structure of ATF4 peptides derived from a human ATF4 protein, a member of the family of transcription factors

Pons, J., Evrard‐Todeschi, N., Bertho, G., Gharbi‐Benarous, J., Bénarous, R., & Girault, J. (2007) · Peptides · doi:10.1016/j.peptides.2007.09.016 · Cited by 16

Structural and dynamic studies of the human RNA binding protein RBM3 reveals the molecular basis of its oligomerization and RNA recognition

Roy, S., Boral, S., Maiti, S., Kushwaha, T., Basak, A. J., Lee, W., Basak, A., Gholap, S. L., Inampudi, K. K., & De, S. (2021) · FEBS Journal · doi:10.1111/febs.16301 · Cited by 15

4,4-Difluoroproline as a Unique 19 F NMR Probe of Proline Conformation

Ganguly, H. K., Ludwig, B. A., Tressler, C. M., Bhatt, M. R., Pandey, A. K., Quinn, C. M., Bai, S., Yap, G. P. A., & Zondlo, N. J. (2024) · Biochemistry · doi:10.1021/acs.biochem.3c00697 · Cited by 14

Effect of Phosphorylation on the Structural Behaviour of Peptides Derived from the Intrinsically Disordered C‐Terminal Domain of Histone H1.0

Chaves‐Arquero, B., Pérez‐Cañadillas, J. M., & Jiménez, M. A. (2020) · Chemistry - A European Journal · doi:10.1002/chem.201905496 · Cited by 15

A solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein)

Buchko, G. W., Tarasevich, B. J., Roberts, J., Snead, M. L., & Shaw, W. J. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.03.006 · Cited by 15

PSCD Domains of Pleuralin-1 from the Diatom Cylindrotheca fusiformis : NMR Structures and Interactions with Other Biosilica-Associated Proteins

Sanctis, S. D., Wenzler, M., Kröger, N., Malloni, W. M., Sumper, M., Deutzmann, R., Zadravec, P., Brunner, E., Kremer, W., & Kalbitzer, H. R. (2016) · Structure · doi:10.1016/j.str.2016.04.021 · Cited by 15

Structure-Activity Relationship of α Mating Pheromone from the Fungal Pathogen Fusarium oxysporum

Vitale, S., Partida‐Hanon, A., Serrano, S., Martínez‐del‐Pozo, Á., Pietro, A. D., Turrà, D., & Bruix, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.766311 · Cited by 15

Two Conformational States of Turkey Ovomucoid Third Domain at Low pH: Three-Dimensional Structures, Internal Dynamics, and Interconversion Kinetics and Thermodynamics,

Song, J., Laskowski, M., QASIM, M. A., & Markley, J. L. (2003) · Biochemistry · doi:10.1021/bi034053f · Cited by 15

Hiding in plain sight: Complex interaction patterns between Tau and 14-3-3ζ protein variants

Crha, R., Kozeleková, A., Hofrová, A., Iľkovičová, L., Gašparik, N., Kadeřávek, P., & Hritz, J. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.130802 · Cited by 17

Structure and activity of contryphan-Vc2: Importance of the d -amino acid residue

Drane, S. B., Robinson, S. D., MacRaild, C. A., Chhabra, S., Chittoor, B., Morales, R. A. V., Leung, E. W. W., Belgi, A., Espino, S. S., Olivera, B. M., et al. (2017) · Toxicon · doi:10.1016/j.toxicon.2017.02.012 · Cited by 14

A Lasso‐Inspired Bicyclic Peptide: Synthesis, Structure and Properties

Martín-Gómez, H., Alberício, F., & Tulla‐Puche, J. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201803899 · Cited by 14

CARD domain of rat RIP2 kinase: Refolding, solution structure, pH-dependent behavior and protein-protein interactions

Goncharuk, S. A., Artemieva, L. E., Tabakmakher, V. М., Arseniev, A. S., & Mineev, K. S. (2018) · PLoS ONE · doi:10.1371/journal.pone.0206244 · Cited by 14

Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747

Heinkel, F., Shen, L. L., Richard‐Greenblatt, M., Okon, M., Bui, J. M., Gee, C. L., Gay, L. M., Alber, T., Av‐Gay, Y., Gsponer, J. A., et al. (2018) · Structure · doi:10.1016/j.str.2018.04.018 · Cited by 14

Solution NMR Structure of Titin N2A Region Ig Domain I83 and Its Interaction with Metal Ions

Kelly, C. M., Pace, N., Gage, M. J., & Pfuhl, M. A. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166977 · Cited by 14

Solution structure of the soluble domain of the NfeD protein YuaF from Bacillus subtilis

Walker, C. A., Hinderhofer, M., Witte, D. J., Boos, W., & Möller, H. M. (2008) · Journal of Biomolecular NMR · doi:10.1007/s10858-008-9261-3 · Cited by 14

Nucleation ofβ-Hairpin Structures with Cis Amide Bonds inE-Vinylogous Proline-Containing Peptides

Chakraborty, T. K., Ghosh, A., Kumar, S., & Kunwar, A. C. (2003) · The Journal of Organic Chemistry · doi:10.1021/jo034361j · Cited by 14

CD28 hinge used in chimeric antigen receptor (CAR) T-cells exhibits local structure and conformational exchange amidst global disorder

Folimonova, V., Chen, X., Negi, H., Schwieters, C. D., Li, J., Byrd, R. A., Taylor, N. N., Youkharibache, P., & Walters, K. J. (2024) · Communications Biology · doi:10.1038/s42003-024-06770-w · Cited by 13

Gausemycin Antibiotic Family Acts via Ca2+-Dependent Membrane Targeting

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Reciprocal antagonism of PIN1-APC/CCDH1 governs mitotic protein stability and cell cycle entry

Ke, S., Dang, F., Wang, L., Chen, J.-Y., Naik, M. T., Li, W., Thavamani, A., Kim, N., Naik, N. M., Sui, H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47427-w · Cited by 15

A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study

Chaves‐Arquero, B., Pantoja‐Uceda, D., Roque, A., Ponte, I., Suau, P., & Jiménez, M. A. (2018) · Journal of Biomolecular NMR · doi:10.1007/s10858-018-0213-2 · Cited by 12

Examining Topoisomers of a Snake-Venom-Derived Peptide for Improved Antimicrobial and Antitumoral Properties

Carrera-Aubesart, A., Defaus, S., Pérez‐Peinado, C., Sandín, D., Torrent, M., Jiménez, M. A., & Andreu, D. (2022) · Biomedicines · doi:10.3390/biomedicines10092110 · Cited by 13

An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility

Durney, M. A., Wechselberger, R. W., Kalodimos, C. G., Kaptein, R., Vorgias, C. E., & Boelens, R. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00247-9 · Cited by 13

Self-assembled fibrillar networks comprised of a naturally-occurring cyclic peptide—LOB3

Rogers, M. A., Feng, Q., Ladizhansky, V., Good, D. B., Smith, A. K., Corridini, M., Grahame, D. A. S., Bryksa, B. C., Jadhav, P. D., Sammynaiken, S., et al. (2016) · RSC Advances · doi:10.1039/c6ra05154e · Cited by 13

Structure and Unfolding of the Third Type III Domain from Human Fibronectin

Stine, J. M., Sun, Y., Armstrong, G. S., Bowler, B. E., & Briknarová, K. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00818 · Cited by 13

Conformational Dynamics in FKBP Domains: Relevance to Molecular Signaling and Drug Design

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Periplasmic Expression of 4/7 α-Conotoxin TxIA Analogs in E. coli Favors Ribbon Isomer Formation – Suggestion of a Binding Mode at the α7 nAChR

Hamdaoui, Y. E., Wu, X., Clark, R. J., Giribaldi, J., Anangi, R., Craik, D. J., King, G. F., Dutertre, S., Kaas, Q., Herzig, V., et al. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00577 · Cited by 13

Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization

Matsumura, K., Shimomura, T., Kubo, Y., Oka, T., Kobayashi, N., Imai, S., Yanase, N., Akimoto, M., Fukuda, M., Yokogawa, M., et al. (2021) · BMC Molecular and Cell Biology · doi:10.1186/s12860-020-00337-3 · Cited by 13

Fluorine NMR study of proline-rich sequences using fluoroprolines

Sinnaeve, D., Bouzayene, A. B., Ottoy, E., Hofman, G.-J., Erdmann, É., Linclau, B., Kuprov, I., Martins, J. C., Torbeev, V. Y., & Kieffer, B. (2021) · Magnetic Resonance · doi:10.5194/mr-2-795-2021 · Cited by 12

The Structure of the Neuropeptide Bradykinin Bound to the Human G‐Protein Coupled Receptor Bradykinin B2 as Determined by Solid‐State NMR Spectroscopy

Lopez, J. J., Shukla, A. K., Reinhart, C., Schwalbe, H., Michel, H., & Glaubitz, C. (2008) · Angewandte Chemie · doi:10.1002/ange.200704282 · Cited by 13

2-Alkyl-2-carboxy-azetidines as scaffolds for the induction of γ-turns

Baeza, J. L., Gerona‐Navarro, G., de Vega, M. J. P., García‐López, M. T., González‐Muñiz, R., & Martín‐Martinez, M. (2007) · Tetrahedron Letters · doi:10.1016/j.tetlet.2007.03.126 · Cited by 13

Conformational studies of RGDechi peptide by natural‐abundance NMR spectroscopy

Farina, B., Gatto, A. D., Comegna, D., Gaetano, S. D., Capasso, D., Isernia, C., Saviano, M., Fattorusso, R., Zaccaro, L., & Russo, L. (2019) · Journal of Peptide Science · doi:10.1002/psc.3166 · Cited by 13

Structure and allosteric activity of a single-disulfide conopeptide from Conus zonatus at human α3β4 and α7 nicotinic acetylcholine receptors

Mohan, M. K., Abraham, N., Rajesh, R. P., Jayaseelan, B. F., Ragnarsson, L. K. N., Lewis, R. J., & Sarma, S. P. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012098 · Cited by 12

Characterization of the Pilotin-Secretin Complex from the Salmonella enterica Type III Secretion System Using Hybrid Structural Methods

Majewski, D. D., Okon, M., Heinkel, F., Robb, C. S., Vuckovic, M., McIntosh, L. P., & Strynadka, N. C. J. (2020) · Structure · doi:10.1016/j.str.2020.08.006 · Cited by 12

Biological functions, genetic and biochemical characterization, and NMR structure determination of the small zinc finger protein HVO_2753 from Haloferax volcanii

Zahn, S., Kubatova, N., Pyper, D. J., Cassidy, L., Saxena, K., Tholey, A., Schwalbe, H., & Soppa, J. (2020) · FEBS Journal · doi:10.1111/febs.15559 · Cited by 12

The natural, peptaibolic peptide SPF-5506-A 4 adopts a β-bend spiral structure, shows low hemolytic activity and targets membranes through formation of large pores

Christoffersen, H. F., Hansen, S. K., Vad, B. S., Nielsen, E. N., Nielsen, J. T., Vosegaard, T., Skrydstrup, T., & Otzen, D. E. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.03.003 · Cited by 11

Pro4 prolyl peptide bond isomerization in human galectin-7 modulates the monomer-dimer equilibrum to affect function

Miller, M. C., Nesmelova, I. V., Daragan, V. A., Ippel, H., Michalak, M., Dregni, A. J., Kaltner, H., Kopitz, J., Gabius, H., & Mayo, K. H. (2020) · Biochemical Journal · doi:10.1042/bcj20200499 · Cited by 11

The C-Terminus of Panusin, a Lobster β-Defensin, Is Crucial for Optimal Antimicrobial Activity and Serum Stability

Bello‐Madruga, R., Valle, J., Jiménez, M. A., Torrent, M., Montero-Alejo, V., & Andreu, D. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15061777 · Cited by 11

Structural and functional characterisation of Tst2, a novel TRPV1 inhibitory peptide from the Australian sea anemone Telmatactis stephensoni

Elnahriry, K. A., Wai, D. C. C., Ashwood, L. M., Naseem, M. U., Szanto, T. G., Guo, S., Panyi, G., Prentis, P. J., & Norton, R. S. (2023) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2023.140952 · Cited by 11

Solution Structure of a Sponge-Derived Cystine Knot Peptide and Its Notable Stability

Li, H., Su, M., Hamann, M. T., Bowling, J. J., Kim, H. S., & Jung, J. H. (2014) · Journal of Natural Products · doi:10.1021/np400899a · Cited by 11

Ordered and Isomerically Stable Bicyclic Peptide Scaffolds Constrained through Cystine Bridges and Proline Turns

Lin, P. J., Yao, H., Zha, J., Zhao, Y., & Wu, C. (2019) · ChemBioChem · doi:10.1002/cbic.201800788 · Cited by 11

Structural, Dynamic, and Functional Characterization of a DnaX Mini-intein Derived from Spirulina platensis Provides Important Insights into Intein-Mediated Catalysis of Protein Splicing

Boral, S., Maiti, S., Basak, A. J., Lee, W., & De, S. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00828 · Cited by 11

Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans

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Semaphorin 3A—Glycosaminoglycans Interaction as Therapeutic Target for Axonal Regeneration

Pérez, Y., Bonet, R., Corredor, M., Domingo, C., Moure, A., Messeguer, Á., Bujons, J., & Alfonso, I. (2021) · Pharmaceuticals · doi:10.3390/ph14090906 · Cited by 12

Peptide bond conformation in peptides and proteins probed by dipolar coupling-chemical shift tensor correlation solid-state NMR

Mukhopadhyay, D., Gupta, C., Theint, T., & Jaroniec, C. P. (2018) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2018.10.015 · Cited by 10

Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts

Shen, Y., & Bax, A. (2009) · Journal of Biomolecular NMR · doi:10.1007/s10858-009-9395-y · Cited by 147

COMMUNICATION Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts

Shen, Y., & Bax, A. (2009)

Statistically significant dependence of the Xaa-Pro peptide bond conformation on secondary structure and amino acid sequence

Pahlke, D., Freund, C., Leitner, D., & Labudde, D. (2005) · BMC Structural Biology · doi:10.1186/1472-6807-5-8 · Cited by 39

NMR strategy for determining Xaa-Pro peptide bond configurations in proteins: Mutants of staphylococcal nuclease with altered configuration at proline-117

Hinck, A. P., Eberhardt, E. S., & Markley, J. L. (1993) · Biochemistry · doi:10.1021/bi00095a009 · Cited by 30

The X‐Pro peptide bond as an nmr probe for conformational studies of flexible linear peptides

Grathwohl, C., & Wüthrich, K. (1976) · Biopolymers · doi:10.1002/bip.1976.360151012 · Cited by 272