Elucidating the folding problem of helical peptides using empirical parameters

NMR with Proteins and Nucleic Acids

Wüthrich, K. (1986) · Europhysics news · doi:10.1051/epn/19861701011 · Cited by 8,028

Statistical mechanics of chain molecules

Flory, P. J., & Volkenstein, M. V. (1969) · Biopolymers · doi:10.1002/bip.1969.360080514 · Cited by 6,449

NMR of Proteins and Nucleic Acids

(2006) · Royal Society of Chemistry eBooks · doi:10.1039/9781847555236-00336 · Cited by 5,874

Determination of the helix and β form of proteins in aqueous solution by circular dichroism

Chen, Y.-H., Yang, J. T., & Chau, K. H. (1974) · Biochemistry · doi:10.1021/bi00713a027 · Cited by 2,070

Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains

Zimm, B., & Bragg, J. K. (1959) · The Journal of Chemical Physics · doi:10.1063/1.1730390 · Cited by 1,801

Structure of ubiquitin refined at 1.8 A resolution.

Vijay-Kumar, S., Bugg, C., & Cook, W. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90679-6 · Cited by 1,636

Amino Acid Preferences for Specific Locations at the Ends of α Helices

Richardson, J. S., & Richardson, D. C. (1988) · Science · doi:10.1126/science.3381086 · Cited by 1,364

A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino Acids

O’Neil, K. T., & DeGrado, W. F. (1990) · Science · doi:10.1126/science.2237415 · Cited by 1,186

Calculation of conformational ensembles from potentials of mena force

Sippl, M. J. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80269-4 · Cited by 1,068

A Novel, Highly Stable Fold of the Immunoglobulin Binding Domain of Streptococcal Protein G

Gronenborn, A. M., Filpula, D. R., Essig, N. Z., Achari, A., Whitlow, M. D., Wingfield, P. T., & Clore, G. M. (1991) · Science · doi:10.1126/science.1871600 · Cited by 816

Regulation of Androgen Receptor Activity by Transient Interactions of Its Transactivation Domain with General Transcription Regulators

Mol, E. D., Szulc, E., Sanza, C. D., Martínez-Cristóbal, P., Bertoncini, C. W., Fenwick, R. B., Frigolé‐Vivas, M., Masin, M., Hunter, I., Buzón, V., et al. (2017) · Structure · doi:10.1016/j.str.2017.11.007 · Cited by 55

Molten globule structure of equine β-lactoglobulin probed by hydrogen exchange

Kobayashi, T., Ikeguchi, M., & Sugai, S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3761 · Cited by 54

Stabilizing nonpolar/polar side‐chain interactions in the α‐helix

Andrew, C. D., Penel, S., Jones, G. R., & Doig, A. J. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.1161 · Cited by 54

Protein Folding: Matching Theory and Experiment

Laurents, D. V., & Baldwin, R. L. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77530-7 · Cited by 54

Structural analysis of peptides encompassing all α-helices of three α/β parallel proteins: Che-Y, flavodoxin and P21-Ras: Implications for α-Helix stability and the folding of α/β parallel proteins

Muñoz, V., Serrano, L., Jiménez, M., & Rico, M. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80145-7 · Cited by 45

The role of Buergi‐Dunitz interactions in the structural stability of proteins

Fufezan, C. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22800 · Cited by 53

Bioinformatic analysis of protein structure–function relationships: case study of leukocyte elastase (ELA2) missense mutations

Thusberg, J., & Vihinen, M. (2006) · Human Mutation · doi:10.1002/humu.20407 · Cited by 52

Ab initio Tertiary Structure Prediction of Proteins

Klepeis, J. L., & Floudas, C. A. (2003) · Journal of Global Optimization · doi:10.1023/a:1021331514642 · Cited by 53

Empirical parameterization of a model for predicting peptide helix/coil equilibrium populations

Andersen, N. H., & Tong, H. (1997) · Protein Science · doi:10.1002/pro.5560060913 · Cited by 53

Stabilisation of α-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding

Taddei, N., Chiti, F., Fiaschi, T., Bucciantini, M., Capanni, C., Stefani, M., Serrano, L., Dobson, C. M., & Ramponi, G. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3870 · Cited by 53

An exceptionally stable helix from the ribosomal protein L9: implications for protein folding and stability

Kuhlman, B. A., Yang, H. Y., Boice, J. A., Fairman, R., & Raleigh, D. P. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1146 · Cited by 53

The role of context on α‐helix stabilization: Host‐guest analysis in a mixed background peptide model

Yang, J., Spek, E. J., Gong, Y., Zhou, H., & Kallenbach, N. R. (1997) · Protein Science · doi:10.1002/pro.5560060614 · Cited by 52

Structural and oxygen binding properties of dimeric horse myoglobin

Nagao, S., Osuka, H., Yamada, T., Uni, T., Shomura, Y., Imai, K., Higuchi, Y., & Hirota, S. (2012) · Dalton Transactions · doi:10.1039/c2dt30893b · Cited by 52

Comparisons of the conformational biases imposed bytrans-2,3-methanomethionine and α-methylmethionine

Burgess, K., Li, W., Lim, D., & Moye-Sherman, D. (1997) · Biopolymers · doi:10.1002/(sici)1097-0282(19971005)42:4 · Cited by 17

Understanding Cold Denaturation: The Case Study of Yfh1

Adrover, M., Esposito, V., Martorell, G., Pastore, A., & Temussi, P. A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1070174 · Cited by 50

What can we learn about protein folding from Ising-like models?

Muñoz, V. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00192-5 · Cited by 50

The folding pathway of the cell-cycle regulatory protein p13suc1: clues for the mechanism of domain swapping.

Schymkowitz, J., Rousseau, F., Irvine, L., & Itzhaki, L. (2000) · Structure · doi:10.1016/s0969-2126(00)00084-8 · Cited by 54

Functionalized Protein-like Structures from Conformationally Defined Synthetic Combinatorial Libraries

Pérez‐Payá, E., Houghten, R. A., & Blondelle, S. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4120 · Cited by 50

Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus

Corazza, A., Rosano, C., Pagano, K., Alverdi, V., Esposito, G., Capanni, C., Bemporad, F., Plakoutsi, G., Stefani, M., Chiti, F., et al. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20703 · Cited by 49

Targeting mechanism of the retinoblastoma tumor suppressor by a prototypical viral oncoprotein

Chemes, L. B., Sanchez, I. E., Smal, C., & Gay, G. D. P. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07540.x · Cited by 49

Measuring Dynamic Flexibility of the Coil State of a Helix-forming Peptide

Lapidus, L. J., Eaton, W. A., & Hofrichter, J. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00193-6 · Cited by 49

Structure and dynamics of a designed helix-loop-helix dimer in dilute aqueous trifluoroethanol solution. A strategy for NMR spectroscopic structure determination of molten globules in the rational design of native-like proteins

Olofsson, S., & Baltzer, L. (1996) · Folding and Design · doi:10.1016/s1359-0278(96)00050-8 · Cited by 49

Position dependence of amino acid intrinsic helical propensities II: Non‐charged polar residues: Ser, Thr, Asn, and Gln

Petukhov, M., Uegaki, K., Yumoto, N., Yoshikawa, S., & Serrano, L. G. (1999) · Protein Science · doi:10.1110/ps.8.10.2144 · Cited by 49

Modulation of the intrinsic helix propensity of an intrinsically disordered protein reveals long-range helix-helix interactions.

Iesmantavicius, V., Jensen, M. R., Ozenne, V., Blackledge, M., Poulsen, F., & Kjaergaard, M. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4045532 · Cited by 47

About TFE: Old and New Findings

Vincenzi, M., Mercurio, F. A., & Leone, M. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190214152439 · Cited by 48

Quantitative chirality of helicenes

Katzenelson, O., Edelstein, J., & Avnir, D. (2000) · Tetrahedron Asymmetry · doi:10.1016/s0957-4166(00)00235-4 · Cited by 48

Conformation-dependent environments in folding proteins

Fernández, A. (2001) · The Journal of Chemical Physics · doi:10.1063/1.1338507 · Cited by 47

PEP-19, an Intrinsically Disordered Regulator of Calmodulin Signaling

Kleerekoper, Q., & Putkey, J. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808067200 · Cited by 47

Esculentin-2CHa: A host-defense peptide with differential cytotoxicity against bacteria, erythrocytes and tumor cells

Attoub, S., Mechkarska, M., Sonnevend, Á., Radosavljevic, G. D., Jovanović, I., Lukić, M. L., & Conlon, J. M. (2012) · Peptides · doi:10.1016/j.peptides.2012.11.004 · Cited by 47

The dimerization domain of the HIV‐1 capsid protein binds a capsid protein‐derived peptide: A biophysical characterization

Garzón, M. T., Lidón‐Moya, M. C., Barrera, F. N., Prieto, A., Gómez, J., Mateu, M. G., & Neira, J. L. (2004) · Protein Science · doi:10.1110/ps.03555304 · Cited by 47

Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: Secondary structure propensities are not conserved in proteins with the same fold

Ramı́rez-Alvarado, M., Serrano, L. G., & Blanco, F. J. (1997) · Protein Science · doi:10.1002/pro.5560060119 · Cited by 47

Intrinsic Stability of Individual α Helices Modulates Structure and Stability of the Apomyoglobulin Molten Globule Form

Kiefhaber, T., & Baldwin, R. L. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0479 · Cited by 47

Computational design of a water‐soluble analog of phospholamban

Slovic, A. M., Summa, C. M., Lear, J. D., & DeGrado, W. F. (2003) · Protein Science · doi:10.1110/ps.0226603 · Cited by 45

Murine model of autosomal dominant retinitis pigmentosa generated by targeted deletion at codon 307 of the rds-peripherin gene.

McNally, N., Kenna, P., Rancourt, D., Ahmed, T., Stitt, A. W., Colledge, W., Lloyd, D. G., Palfi, A., O'Neill, B., Humphries, M., et al. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.9.1005 · Cited by 48

Quantification of Conformational Entropy Unravels Effect of Disordered Flanking Region in Coupled Folding and Binding

Theisen, F. F., Staby, L., Tidemand, F. G., O’Shea, C., Prestel, A., Willemoës, M., Kragelund, B. B., & Skriver, K. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c04214 · Cited by 45

Membrane-active peptides: binding, translocation, and flux in lipid vesicles

Almeida, P. (2014) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamem.2014.04.014 · Cited by 48

Data-Driven Prediction and Design of bZIP Coiled-Coil Interactions

Potapov, V., Kaplan, J. B., & Keating, A. E. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004046 · Cited by 45

Emergence and evolution of an interaction between intrinsically disordered proteins

Hultqvist, G., Åberg, E., Camilloni, C., Sundell, G. N., Andersson, E., Dogan, J., Celestine, N., Vendruscolo, M., & Jemth, P. (2017) · eLife · doi:10.7554/elife.16059 · Cited by 45

Thermodynamics Of α‐Helix Formation

Makhatadze, G. (2005) · Advances in protein chemistry · doi:10.1016/s0065-3233(05)72008-8 · Cited by 34

The Importance of a Gatekeeper Residue on the Aggregation of Transthyretin

Sant’Anna, R., Braga, C. A. C. A., Varejão, N., Pimenta, K. M., Graña‐Montes, R., Alves, A. A., Cortines, J. R., Cordeiro, Y., Ventura, S., & Foguel, D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.563981 · Cited by 44

Modulating repeat protein stability: The effect of individual helix stability on the collective behavior of the ensemble

Cortajarena, A. L., Mochrie, S. G. J., & Regan, L. (2011) · Protein Science · doi:10.1002/pro.638 · Cited by 44

A helix‐turn motif in the C‐terminal domain of histone H1

Vila, R., Ponte, I., Suau, P., Jiménez, M. A., & Rico, M. (2000) · Protein Science · doi:10.1110/ps.9.4.627 · Cited by 44

A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins – Lessons from the sodium proton exchanger 1 (NHE1)

Hendus-Altenburger, R., Lambrughi, M., Terkelsen, T., Pedersen, S. F., Papaleo, E., Lindorff‐Larsen, K., & Kragelund, B. B. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.05.015 · Cited by 44

Monte Carlo Studies of Folding, Dynamics, and Stability in α-Helices

Shental-Bechor, D., Kirca, S., Ben‐Tal, N., & Haliloǧlu, T. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.050708 · Cited by 43

An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties

Mechkarska, M., Prajeep, M., Radosavljevic, G. D., Jovanović, I., Baloushi, A. A., Sonnevend, Á., Lukić, M. L., & Conlon, J. M. (2013) · Peptides · doi:10.1016/j.peptides.2013.10.015 · Cited by 43

Improved Stability of the Jun-Fos Activator Protein-1 Coiled Coil Motif

Mason, J., Hagemann, U., & Arndt, K. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701828200 · Cited by 42

Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix protein

Bruun, S. W., Iešmantavičius, V., Danielsson, J., & Poulsen, F. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003004107 · Cited by 42

Reading protein sequences backwards.

Lacroix, E., Viguera, A., & Serrano, L. (1998) · Folding & design · doi:10.1016/s1359-0278(98)00013-3 · Cited by 40

Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface

Pielak, G. J., Auld, D. S., Beasley, J. R., Betz, S. F., Cohen, D. S., Doyle, D. F., Finger, S. A., Fredericks, Z. L., & Hilgen-Willis, S. (1995) · Biochemistry · doi:10.1021/bi00010a017 · Cited by 42

Ab initioprediction of helical segments in polypeptides

Klepeis, J. L., & Floudas, C. A. (2001) · Journal of Computational Chemistry · doi:10.1002/jcc.10002 · Cited by 42

Structural characterization and comparative modeling of PD-Ls 1–3, type 1 ribosome-inactivating proteins from summer leaves of Phytolacca dioica L.

Maro, A. D., Chambery, A., Carafa, V., Costantini, S., Colonna, G., & Parente, A. (2008) · Biochimie · doi:10.1016/j.biochi.2008.10.008 · Cited by 41

NMR Analysis of Synthetic Human Serum Albumin α-Helix 28 Identifies Structural Distortion upon Amadori Modification

Howard, M. J., & Smales, C. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501480200 · Cited by 41

Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy

Piai, A., Calçada, E. O., Tarenzi, T., Grande, A. D., Váradi, M., Tompa, P., Felli, I. C., & Pierattelli, R. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2015.11.3516 · Cited by 41

Domain Swapping of the Heme and N-Terminal α-Helix inHydrogenobacter thermophilusCytochromec552Dimer

Hayashi, Y., Nagao, S., Osuka, H., Komori, H., Higuchi, Y., & Hirota, S. (2012) · Biochemistry · doi:10.1021/bi3011303 · Cited by 42

New Stochastic Strategy to Analyze Helix Folding

Moret, M. A., Bisch, P. M., Mundim, K. C., & Pascutti, P. G. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75471-4 · Cited by 41

Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent

Conlon, J. M., Mechkarska, M., Prajeep, M., Arafat, K., Zarić, M., Lukić, M. L., & Attoub, S. (2012) · Amino Acids · doi:10.1007/s00726-012-1395-7 · Cited by 41

Fast folding of a helical protein initiated by the collision of unstructured chains

Meisner, W. K., & Sosnick, T. R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404057101 · Cited by 41

Statistical Prediction and Molecular Dynamics Simulation

Cooke, B., & Schmidler, S. C. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.131623 · Cited by 40

The human prion protein α2 helix: A thermodynamic study of its conformational preferences

Tizzano, B., Palladino, P., de Capua, A., Marasco, D., Rossi, F., Benedetti, E., Pedone, C., Ragone, R., & Ruvo, M. (2005) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.20395 · Cited by 41

Photo-control of peptide helix content by an azobenzene cross-linker: steric interactions with underlying residues are not critical

Kumita, J. R., Flint, D. G., Smart, O. S., & Woolley, G. A. (2002) · Protein Engineering Design and Selection · doi:10.1093/protein/15.7.561 · Cited by 40

Structure and mechanism of maximum stability of isolated alpha-helical protein domains at a critical length scale

Zhao Qin, A., Fabre, A., & Buehler, M. J. (2013) · The European Physical Journal E · doi:10.1140/epje/i2013-13053-8 · Cited by 39

Helicity of short E‐R/K peptides

Sommese, R. F., Sivaramakrishnan, S., Baldwin, R. L., & Spudich, J. A. (2010) · Protein Science · doi:10.1002/pro.469 · Cited by 38

Synthesis, conformational analysis and biological properties of a dicarba derivative of the antimicrobial peptide, brevinin-1BYa

Hossain, M. A., Guilhaudis, L., Sonnevend, Á., Attoub, S., van Lierop, B. J., Robinson, A. J., Wade, J. D., & Conlon, J. M. (2011) · European Biophysics Journal · doi:10.1007/s00249-011-0679-2 · Cited by 39

Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: Secondary structure, antimicrobial activity, and mammalian cell toxicity

Leite, J. R. S. A., Brand, G. D., Silva, L. P., Kückelhaus, S. A. S., Bento, W. R. C., Araújo, A. L. T., Martins, G. R., Lazzari, A. M., & Bloch, C. (2007) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2007.03.016 · Cited by 39

General Anesthetic Action at an Internal Protein Site Involving the S4-S5 Cytoplasmic Loop of a Neuronal K+Channel

Harris, T., Shahidullah, M., Ellingson, J. S., & Covarrubias, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.7.4928 · Cited by 39

Cooperative folding of a protein mini domain: the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex 1 1Edited by P. E. Wright

Spector, S., Kuhlman, B. A., Fairman, R., Wong, E., Boice, J. A., & Raleigh, D. P. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1522 · Cited by 39

Unique Features of the Anti-parallel, Heterodimeric Coiled-coil Interaction between Methyl-cytosine Binding Domain 2 (MBD2) Homologues and GATA Zinc Finger Domain Containing 2A (GATAD2A/p66α)

Walavalkar, N. M., Gordon, N. C., & Williams, D. C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431346 · Cited by 38

An Undecided Coiled Coil

Croasdale, R., Ivins, F. J., Muskett, F., Daviter, T., Scott, D. J., Hardy, T., Smerdon, S., Fry, A., & Pfuhl, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.196972 · Cited by 20

An α-Helical Burst in the src SH3 Folding Pathway

Li, J.-S., Shinjo, M., Matsumura, Y., Morita, M., Baker, D., Ikeguchi, M., & Kihara, H. (2007) · Biochemistry · doi:10.1021/bi0618262 · Cited by 34

Artificial Intelligence Understands Peptide Observability and Assists With Absolute Protein Quantification

Zimmer, D. M., Schneider, K., Sommer, F., Schroda, M., & Mühlhaus, T. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.01559 · Cited by 37

Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the α-helix fragment

Blanco, F. J., Ortíz, Á. R., & Serrano, L. (1997) · Folding and Design · doi:10.1016/s1359-0278(97)00017-5 · Cited by 38

Navigating the Downhill Protein Folding Regime via Structural Homologues

Naganathan, A. N., Li, P., Pérez‐Jiménez, R., Sánchez‐Ruiz, J. M., & Muñoz, V. (2010) · Journal of the American Chemical Society · doi:10.1021/ja103612q · Cited by 38

Folding Cooperativity in a Three-stranded β-Sheet Model

Roe, D. R., Horn̆ák, V., & Simmerling, C. L. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.07.036 · Cited by 38

LDL receptor/lipoprotein recognition: endosomal weakening of ApoB and ApoE binding to the convex face of the LR 5 repeat

Martínez-Oliván, J., Arias‐Moreno, X., Velázquez‐Campoy, A., Millet, Ó., & Sancho, J. (2014) · FEBS Journal · doi:10.1111/febs.12721 · Cited by 37

The Mechanical Unfolding of Ubiquitin through All-Atom Monte Carlo Simulation with a Gō-Type Potential

Kleiner, A., & Shakhnovich, E. I. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.081257 · Cited by 37

Extensive Formation of Off-Pathway Species during Folding of an α−β Parallel Protein Is Due to Docking of (Non)native Structure Elements in Unfolded Molecules

Nabuurs, S. M., Westphal, A. H., & van Mierlo, C. P. M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja803841n · Cited by 37

Molecular Features of an Alcohol Binding Site in a Neuronal Potassium Channel

Shahidullah, M., Harris, T., Germann, M. W., & Covarrubias, M. (2003) · Biochemistry · doi:10.1021/bi034738f · Cited by 37

Specific interactions of sticholysin I with model membranes: An NMR study

Castrillo, I., Araujo, N. A., Alegre‐Cebollada, J., Gavilanes, J. G., Martínez‐del‐Pozo, Á., & Bruix, M. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22712 · Cited by 37

The hymenochirins: A family of host-defense peptides from the Congo dwarf clawed frog Hymenochirus boettgeri (Pipidae)

Mechkarska, M., Prajeep, M., Coquet, L., Leprince, J., Jouenne, T., Vaudry, H., King, J. D., & Conlon, J. M. (2012) · Peptides · doi:10.1016/j.peptides.2012.03.029 · Cited by 37

Helicity of α(404–451) and β(394–445) tubulin C‐terminal recombinant peptides

Jiménez, M. A., Evangelio, J. A., Aranda, C., Lopez‐Brauet, A., Andreu, D., Rico, M., Lagos, R., Andreu, J. M., & Monasterio, O. (1999) · Protein Science · doi:10.1110/ps.8.4.788 · Cited by 37

Exploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands

Champness, J. N., Bennett, M. S., Wien, F., Visse, R., Summers, W. C., Herdewijn, P. A., Clercq, E. D., Ostrowski, T., Jarvest, R. L., & Sanderson, M. R. (1998) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(19980815)32:3 · Cited by 141

A family of antimicrobial and immunomodulatory peptides related to the frenatins from skin secretions of the Orinoco lime frog Sphaenorhynchus lacteus (Hylidae)

Conlon, J. M., Mechkarska, M., Radosavljevic, G. D., Attoub, S., King, J. D., Lukić, M. L., & McClean, S. (2014) · Peptides · doi:10.1016/j.peptides.2014.03.020 · Cited by 36

Cationic Polypeptoids with Optimized Molecular Characteristics toward Efficient Nonviral Gene Delivery

Zhu, L., Simpson, J. M., Xu, X., He, H., Zhang, D., & Yin, L. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.7b06031 · Cited by 36

The structure of the SBP-Tag–streptavidin complex reveals a novel helical scaffold bridging binding pockets on separate subunits

Barrette‐Ng, I. H., Wu, S., Tjia, W. M., Wong, S., & Ng, K. K.-S. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913002576 · Cited by 36

Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies

Kyle, H. F., Wickson, K. F., Stott, J., Burslem, G. M., Breeze, A. L., Tiede, C., Tomlinson, D. C., Warriner, S. L., Nelson, A. S., Wilson, A. J., et al. (2015) · Molecular BioSystems · doi:10.1039/c5mb00284b · Cited by 35

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