Influence of proline residues on protein conformation

Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features

Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320 · see citing works

The protein data bank: A computer-based archival file for macromolecular structures

Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80200-3 · Cited by 8,582 · see citing works

The Anatomy and Taxonomy of Protein Structure

Richardson, J. S. (1981) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60520-3 · Cited by 3,378 · see citing works

Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins

Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a001 · Cited by 2,172 · see citing works

A graphics model building and refinement system for macromolecules

Jones, T. A. (1978) · Journal of Applied Crystallography · doi:10.1107/s0021889878013308 · Cited by 1,848 · see citing works

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 1,380 · see citing works

Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

Brandts, J. F., Halvorson, H. R., & Brennan, M. (1975) · Biochemistry · doi:10.1021/bi00693a026 · Cited by 1,120 · see citing works

Helix geometry in proteins

Barlow, D. J., & Thornton, J. M. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90641-9 · Cited by 1,066 · see citing works

Analysis and prediction of the different types of β-turn in proteins

Wilmot, C. M., & Thornton, J. M. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90103-9 · Cited by 981 · see citing works

Folding of immunogenic peptide fragments of proteins in water solution

Dyson, H. J., Rance, M., Houghten, R. A., Lerner, R. A., & Wright, P. E. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90446-9 · Cited by 737 · see citing works

Structure of the Gene Encoding the Immunodominant Surface Antigen on the Sporozoite of the Human Malaria Parasite Plasmodium falciparum

Dame, J. B., Williams, J. L., McCutchan, T. F., Weber, J. L., Wirtz, R. A., Hockmeyer, W. T., Maloy, W. L., Haynes, J. D., Schneider, I., Roberts, D. R., et al. (1984) · Science · doi:10.1126/science.6204383 · Cited by 712 · see citing works

Conformational Analysis of the 20 Naturally Occurring Amino Acid Residues Using ECEPP

Zimmerman, S. S., Pottle, M. S., Némethy, G., & Scheraga, H. A. (1977) · Macromolecules · doi:10.1021/ma60055a001 · Cited by 686 · see citing works

Chain reversals in proteins

Lewis, P. N., Momany, F. A., & Scheraga, H. A. (1973) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(73)90350-4 · Cited by 665 · see citing works

Conformational preferences of amino acids in globular proteins

Levitt, M. (1978) · Biochemistry · doi:10.1021/bi00613a026 · Cited by 654 · see citing works

β-Turns and their distortions: a proposed new nomenclature

Wilmot, C. M., & Thornton, J. M. (1990) · Protein Engineering Design and Selection · doi:10.1093/protein/3.6.479 · Cited by 390 · see citing works

Nmr studies of the rates of proline cis – trans isomerization in oligopeptides

Grathwohl, C., & Wüthrich, K. (1981) · Biopolymers · doi:10.1002/bip.1981.360201209 · Cited by 388 · see citing works

Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences

McCaldon, P., & Argos, P. (1988) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340040204 · Cited by 266 · see citing works

Conformational energies and configurational statistics of copolypeptides containing l-proline

SCHIMMEL, P. R., & Flory, P. J. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90237-4 · Cited by 247 · see citing works

An explanation for the rare occurrence of cis peptide units in proteins and polypeptides

Ramachandran, G. N., & MITRA, A. K. (1976) · Journal of Molecular Biology · doi:10.1016/s0022-2836(76)80019-8 · Cited by 202 · see citing works

Orthogonal packing of .beta.-pleated sheets in proteins

Chothia, C., & Janin, J. (1982) · Biochemistry · doi:10.1021/bi00260a009 · Cited by 144 · see citing works

Amino acid distribution in protein secondary structures

Argos, P., & Palau, J. (1982) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1982.tb02619.x · Cited by 97 · see citing works

HERA—A program to draw schematic diagrams of protein secondary structures

Hutchinson, E. G., & Thornton, J. M. (1990) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340080303 · Cited by 97 · see citing works

A novel approach for studies of the molecular conformations in flexible polypeptides

Wüthrich, K., & Grathwohl, C. (1974) · FEBS Letters · doi:10.1016/0014-5793(74)80674-5 · Cited by 69 · see citing works

A protein sequence/structure database

(1988) · Nature · doi:10.1038/335745a0 · Cited by 64 · see citing works

A relational database of protein structures designed for flexible enquiries about conformation

Islam, S. A., & Sternberg, M. J. E. (1989) · Protein Engineering Design and Selection · doi:10.1093/protein/2.6.431 · Cited by 58 · see citing works

Basic proline-rich proteins from human parotid saliva: complete covalent structures of proteins IB-1 and IB-6

Kauffman, D. L., Hofmann, T., Bennick, A., & Keller, P. J. (1986) · Biochemistry · doi:10.1021/bi00357a013 · Cited by 43 · see citing works

The crystal structure of t-amyloxycarbonyl- L -prolyl- L -prolyl- L -proline

Kartha, G., Ashida, T., & Kakudo, M. (1974) · Acta Crystallographica Section B · doi:10.1107/s0567740874005930 · Cited by 31 · see citing works

Conformational energy studies of linear dipeptides H‐X‐ L ‐Pro‐OH

Hetzel, R., & Wüthrich, K. (1979) · Biopolymers · doi:10.1002/bip.1979.360181015 · Cited by 27 · see citing works

A novel supersecondary structure in globular proteins comprising the collagen-like helix and β-turn

Ananthanarayanan, V. S., Soman, K. V., & Ramakrishnan, C. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90211-7 · Cited by 11 · see citing works

[19] Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors

Ballesteros, J. A., & Weinstein, H. (1995) · Methods in neurosciences · doi:10.1016/s1043-9471(05)80049-7 · Cited by 3,001 · see citing works

Stereochemical quality of protein structure coordinates

Morris, A. L., MacArthur, M. W., Hutchinson, E. G., & Thornton, J. M. (1992) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340120407 · Cited by 1,547 · see citing works

The Rosetta All-Atom Energy Function for Macromolecular Modeling and Design

Alford, R. F., Leaver-Fay, A., Jeliazkov, J. R., O’Meara, M. J., DiMaio, F. P., Park, H., Shapovalov, M. V., Renfrew, P. D., Mulligan, V. K., Kappel, K., et al. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00125 · Cited by 1,532 · see citing works

The importance of being proline: the interaction of proline‐rich motifs in signaling proteins with their cognate domains

Kay, B. K., Williamson, M. P., & Sudol, M. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.2.231 · Cited by 1,214 · see citing works

Cis−Trans Isomerization of Organic Molecules and Biomolecules: Implications and Applications

Dugave, C., & Demange, L. (2003) · Chemical Reviews · doi:10.1021/cr0104375 · Cited by 1,033 · see citing works

Application of the multimolecule and multiconformational RESP methodology to biopolymers: Charge derivation for DNA, RNA, and proteins

Cieplak, P., Cornell, W. D., Bayly, C. I., & Kollman, P. A. (1995) · Journal of Computational Chemistry · doi:10.1002/jcc.540161106 · Cited by 1,012 · see citing works

The structure and function of proline-rich regions in proteins

Williamson, M. P. (1994) · Biochemical Journal · doi:10.1042/bj2970249 · Cited by 999 · see citing works

Interactions between Polyphenols and Macromolecules: Quantification Methods and Mechanisms

Bourvellec, C. L., & Renard, C. M. G. C. (2011) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2010.499808 · Cited by 858 · see citing works

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729 · see citing works

Multiple Interactions between Polyphenols and a Salivary Proline-Rich Protein Repeat Result in Complexation and Precipitation

Baxter, N. J., Lilley, T. H., Haslam, E., & Williamson, M. P. (1997) · Biochemistry · doi:10.1021/bi9700328 · Cited by 681 · see citing works

Chemical Modifications Designed to Improve Peptide Stability: Incorporation of Non-Natural Amino Acids, Pseudo-Peptide Bonds, and Cyclization

Gentilucci, L., Marco, R. D., & Cerisoli, L. (2010) · Current Pharmaceutical Design · doi:10.2174/138161210793292555 · Cited by 591 · see citing works

Critical assessment of methods of protein structure prediction (CASP)—Round <scp>XIV</scp>

Kryshtafovych, A., Schwede, T., Topf, M., Fidelis, K., & Moult, J. (2021) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26237 · Cited by 503 · see citing works

Invited review: Caseins and the casein micelle: Their biological functions, structures, and behavior in foods

Holt, C., Carver, J. A., Ecroyd, H. W., & Thorn, D. C. (2013) · Journal of Dairy Science · doi:10.3168/jds.2013-6831 · Cited by 501 · see citing works

CH–π hydrogen bonds in biological macromolecules

Nishio, M., Umezawa, Y., Fantini, J., Weiss, M. S., & Chakrabarti, P. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp00099d · Cited by 470 · see citing works

Cis–trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel

Lummis, S. C. R., Beene, D. L., Lee, L. W., Lester, H. A., Broadhurst, R. W., & Dougherty, D. A. (2005) · Nature · doi:10.1038/nature04130 · Cited by 455 · see citing works

A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering

Bernadó, P., Blanchard, L., Timmins, P. A., Marion, D., Ruigrok, R. W. H., & Blackledge, M. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506202102 · Cited by 436 · see citing works

An analysis of protein domain linkers: their classification and role in protein folding

George, R. A., & Heringa, J. (2002) · Protein Engineering Design and Selection · doi:10.1093/protein/15.11.871 · Cited by 429 · see citing works

Formation of tight junction: determinants of homophilic interaction between classic claudins

Piorntek, J., Winkler, L., Wolburg, H., Müller, S. L., Zuleger, N., Piehl, C., Wiesner, B., Krause, G., & Blasig, I. E. (2007) · The FASEB Journal · doi:10.1096/fj.07-8319com · Cited by 399 · see citing works

Polyphenols, astringency and proline-rich proteins

Luck, G., Liao, H., Baxter, N. J., Grimmer, H. R., Warminski, E. E., Williamson, M. P., Lilley, T. H., & Haslam, E. (1994) · Phytochemistry · doi:10.1016/0031-9422(94)85061-5 · Cited by 397 · see citing works

Role of proline in cell wall synthesis and plant development and its implications in plant ontogeny

Kishor, P. B. K. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2015.00544 · Cited by 386 · see citing works

The Structure and Function of Proline Recognition Domains

Zarrinpar, A., Bhattacharyya, R. P., & Lim, W. A. (2003) · Science Signaling · doi:10.1126/stke.2003.179.re8 · Cited by 375 · see citing works

Proline-induced Distortions of Transmembrane Helices

Cordes, F. S., Bright, J. N., & Sansom, M. S. P. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01006-9 · Cited by 365 · see citing works

Side-chain effects on peptidyl-prolyl cis/trans isomerisation

Reimer, U., Scherer, G., Drewello, M., Kruber, S., Schutkowski, M., & Fischer, G. S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1770 · Cited by 353 · see citing works

Mutations of the KISS1 gene in disorders of puberty

Silveira, L. G., Noel, S. D., Silveira-Neto, A. P., Abreu, A. P., Brito, V. N., Santos, M. G., Bianco, S. D. C., Kuohung, W., Xu, S., Gryngarten, M., et al. (2010) · The Journal of Clinical Endocrinology &amp; Metabolism · doi:10.1210/jc.2009-2421 · Cited by 352 · see citing works

Blocker protection in the pore of a voltage-gated K+ channel and its structural implications

del Camino, D., Holmgren, M., Liu, Y., & Yellen, G. (2000) · Nature · doi:10.1038/35002099 · Cited by 333 · see citing works

Sequence, Structure, and Function of Peptide Self-Assembled Monolayers

Nowinski, A. K., Sun, F., White, A. D., Keefe, A. J., & Jiang, S. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3006868 · Cited by 325 · see citing works

Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment.

Li, S., Goto, N. K., Williams, K. A., & Deber, C. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6676 · Cited by 321 · see citing works

Non-proline Cis peptide bonds in proteins

Jabs, A., Weiss, M. S., & Hilgenfeld, R. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2459 · Cited by 315 · see citing works

Proline Alleviates Abiotic Stress Induced Oxidative Stress in Plants

Zulfiqar, F., & Ashraf, M. (2022) · Journal of Plant Growth Regulation · doi:10.1007/s00344-022-10839-3 · Cited by 315 · see citing works

Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations 1 1Edited by J. M. Thornton

Pal, D., & Chakrabarti, P. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3217 · Cited by 315 · see citing works

Aromatic–Proline Interactions: Electronically Tunable CH/π Interactions

Zondlo, N. J. (2012) · Accounts of Chemical Research · doi:10.1021/ar300087y · Cited by 313 · see citing works

Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH

Kjærgaard, M., Brander, S., & Poulsen, F. M. (2011) · Journal of Biomolecular NMR · doi:10.1007/s10858-011-9472-x · Cited by 308 · see citing works

Cleavage N-Terminal to Proline: Analysis of a Database of Peptide Tandem Mass Spectra

Breci, L. A., Tabb, D. L., Yates, J. R., & Wysocki, V. H. (2003) · Analytical Chemistry · doi:10.1021/ac026359i · Cited by 307 · see citing works

The Ramachandran plots of glycine and pre-proline

Ho, B. K., & Brasseur, R. (2005) · BMC Structural Biology · doi:10.1186/1472-6807-5-14 · Cited by 305 · see citing works

Inter-residue interactions in protein folding and stability

Gromiha, M. M., & Selvaraj, S. (2003) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2003.09.003 · Cited by 303 · see citing works

Structure and function of the WW domain

Sudol, M. (1996) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(96)00008-9 · Cited by 296 · see citing works

Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution

Kjærgaard, M., & Poulsen, F. M. (2011) · Journal of Biomolecular NMR · doi:10.1007/s10858-011-9508-2 · Cited by 294 · see citing works

Derivation of rules for comparative protein modeling from a database of protein structure alignments

Šali, A., & Overington, J. P. (1994) · Protein Science · doi:10.1002/pro.5560030923 · Cited by 294 · see citing works

Positional cloning of a global regulator of anterior–posterior patterning in mice

Schumacher, A., Faust, C. J., & Magnuson, T. (1996) · Nature · doi:10.1038/383250a0 · Cited by 292 · see citing works

The alphabet of intrinsic disorder

Theillet, F., Kalmár, L., Tompa, P., Han, K., Selenko, P., Dunker, A. K., Daughdrill, G. W., & Uversky, V. N. (2013) · Intrinsically Disordered Proteins · doi:10.4161/idp.24360 · Cited by 283 · see citing works

Proline: The Distribution, Frequency, Positioning, and Common Functional Roles of Proline and Polyproline Sequences in the Human Proteome

Morgan, A. A., & Rubenstein, E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053785 · Cited by 281 · see citing works

Structure of the Kinase Domain of an Imatinib-Resistant Abl Mutant in Complex with the Aurora Kinase Inhibitor VX-680

Young, M. A., Shah, N. P., Chao, L. H., Seeliger, M. A., Milanov, Z. V., Biggs, W., Treiber, D. K., Patel, H., Zarrinkar, P. P., Lockhart, D. J., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2788 · Cited by 277 · see citing works

The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 å resolution: structural characterization of proline-substitution sites for protein thermostabilization

Watanabe, K., Hata, Y., Kizaki, H., Katsube, Y., & Suzuki, Y. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1018 · Cited by 276 · see citing works

A ribosome‐associated peptidyl‐prolyl cis/trans isomerase identified as the trigger factor.

Stoller, G., RÜCKNAGEL, K. P., Nierhaus, K. H., Schmid, F. X., Fischer, G. S., & Rahfeld, J. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00177.x · Cited by 275 · see citing works

Prolyl Isomerases: Role in Protein Folding

Schmid, F. X., Mayr, L. M., Mücke, M., & Schönbrunner, E. R. (1993) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60563-x · Cited by 267 · see citing works

An electronic effect on protein structure

Hinderaker, M. P., & Raines, R. T. (2003) · Protein Science · doi:10.1110/ps.0241903 · Cited by 266 · see citing works

Development of α-Helical Calpain Probes by Mimicking a Natural Protein–Protein Interaction

Jo, H., Meinhardt, N., Wu, Y., Kulkarni, S., Hu, X., Low, K. E., Davies, P. L., DeGrado, W. F., & Greenbaum, D. C. (2012) · Journal of the American Chemical Society · doi:10.1021/ja307599z · Cited by 261 · see citing works

A survey of left‐handed polyproline II helices

Stapley, B. J., & Creamer, T. P. (1999) · Protein Science · doi:10.1110/ps.8.3.587 · Cited by 256 · see citing works

A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes

Hamazaki, J., Iemura, S., Natsume, T., Yashiroda, H., Tanaka, K., & Murata, S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601338 · Cited by 254 · see citing works

Histones: At the Crossroads of Peptide and Protein Chemistry

Müller, M. M., & Muir, T. W. (2015) · Chemical Reviews · doi:10.1021/cr5003529 · Cited by 247 · see citing works

Peptidomimetics – A Versatile Route to Biologically Active Compounds

Grauer, A., & König, B. (2009) · European Journal of Organic Chemistry · doi:10.1002/ejoc.200900599 · Cited by 247 · see citing works

Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions

Bochicchio, B., & Tamburro, A. M. (2002) · Chirality · doi:10.1002/chir.10153 · Cited by 246 · see citing works

Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins fromE. coli

Thomas, J. G., Ayling, A., & Baneyx, F. (1997) · Applied Biochemistry and Biotechnology · doi:10.1007/bf02785589 · Cited by 241 · see citing works

Peptidylproline cis/trans isomerases

Gałat, A., & Metcalfe, S. M. (1995) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(94)00009-x · Cited by 240 · see citing works

Tandem mass spectrometry of very large molecules. 2. Dissociation of multiply charged proline-containing proteins from electrospray ionization

Loo, J. A., Edmonds, C. G., & Smith, R. D. (1993) · Analytical Chemistry · doi:10.1021/ac00052a020 · Cited by 239 · see citing works

Structure of the SH3-Guanylate Kinase Module from PSD-95 Suggests a Mechanism for Regulated Assembly of MAGUK Scaffolding Proteins

McGee, A. W., Dakoji, S., Olsen, O., Bredt, D. S., Lim, W. A., & Prehoda, K. E. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00411-7 · Cited by 239 · see citing works

Stabilization of alpha-helical structures in short peptides via end capping

Forood, B., Feliciano, E. J., & Nambiar, K. P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.3.838 · Cited by 235 · see citing works

Proline and ROS: A Unified Mechanism in Plant Development and Stress Response?

Renzetti, M., Funck, D., & Trovato, M. (2024) · Plants · doi:10.3390/plants14010002 · Cited by 233 · see citing works

Tragedy in a heartbeat: malfunctioning desmin causes skeletal and cardiac muscle disease

Goldfarb, L. G., & Dalakas, M. C. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38027 · Cited by 232 · see citing works

Structural models of human apolipoprotein A-I: a critical analysis and review

Brouillette, C. G., Anantharamaiah, G. M., Engler, J. A., & Borhani, D. W. (2001) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(01)00081-6 · Cited by 232 · see citing works

Experimentally observed conformation‐dependent geometry and hidden strain in proteins

Karplus, P. A. (1996) · Protein Science · doi:10.1002/pro.5560050719 · Cited by 224 · see citing works

Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes

Fischer, G. S., & Aumüller, T. (2003) · Springer eBooks · doi:10.1007/s10254-003-0011-3 · Cited by 221 · see citing works

Protein Prosthesis: 1,5-Disubstituted[1,2,3]triazoles as cis-Peptide Bond Surrogates

Tam, A., Arnold, U., Soellner, M. B., & Raines, R. T. (2007) · Journal of the American Chemical Society · doi:10.1021/ja075865s · Cited by 220 · see citing works

Activity of wheat α‐amylase inhibitors towards bruchid α‐amylases and structural explanation of observed specificities

Franco, O. L., Rigden, D. J., Melo, F. R., Bloch, C., Silva, C. P., & Grossi‐de‐Sá, M. F. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01199.x · Cited by 219 · see citing works

The interrelationships of side-chain and main-chain conformations in proteins

Chakrabarti, P., & Pal, D. (2001) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(01)00005-0 · Cited by 219 · see citing works

Glycine Residues Provide Flexibility for Enzyme Active Sites

Yan, B. X., & Sun, Y. Q. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3190 · Cited by 216 · see citing works

Direct detection of transient α‐helical states in islet amyloid polypeptide

Williamson, J. A., & Miranker, A. D. (2006) · Protein Science · doi:10.1110/ps.062486907 · Cited by 215 · see citing works

Predicting oligomerization states of coiled coils

Woolfson, D. N., & Alber, T. (1995) · Protein Science · doi:10.1002/pro.5560040818 · Cited by 214 · see citing works

Host−Guest Study of Left-Handed Polyproline II Helix Formation

Kelly, M., Chellgren, B. W., Rucker, A. L., Troutman, J. M., Fried, M. G., Miller, A., & Creamer, T. P. (2001) · Biochemistry · doi:10.1021/bi011043a · Cited by 210 · see citing works

Proline-rich, amphipathic cell-penetrating peptides

Pujals, S., & Giralt, E. (2007) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.09.012 · Cited by 209 · see citing works

A three‐dimensional model of aromatase cytochrome P450

Graham-Lorence, S. E., Peterson, J. A., Amarneh, B., Simpson, E. R., & White, R. E. (1995) · Protein Science · doi:10.1002/pro.5560040605 · Cited by 209 · see citing works

Different roles of Enhanced Disease Susceptibility1 (EDS1) bound to and dissociated from Phytoalexin Deficient4 (PAD4) in Arabidopsis immunity

Rietz, S., Stamm, A., Malonek, S., Wagner, S., Becker, D., Medina‐Escobar, N., Vlot, A. C., Feys, B. J., Niefind, K., & Parker, J. E. (2011) · New Phytologist · doi:10.1111/j.1469-8137.2011.03675.x · Cited by 208 · see citing works

Molecular cloning, structural analysis and functional expression of the proline‐rich focal adhesion and microfilament‐associated protein VASP.

Haffner, C., Jarchau, T., Reinhard, M., Hoppe, J., Lohmann, S. M., & Walter, U. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb06971.x · Cited by 206 · see citing works

The structure of “unstructured” regions in peptides and proteins: Role of the polyproline II helix in protein folding and recognition*

Rath, A., Davidson, A. R., & Deber, C. M. (2005) · Biopolymers · doi:10.1002/bip.20227 · Cited by 201 · see citing works

Why do protein architectures have boltzmann‐like statistics?

Finkelstein, A. V., Badretdinov, A. Y., & Gutin, A. M. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340230204 · Cited by 200 · see citing works

Stereospecific Pseudoproline Ligation of N-Terminal Serine, Threonine, or Cysteine-Containing Unprotected Peptides

Tam, J. P., & Miao, Z. (1999) · Journal of the American Chemical Society · doi:10.1021/ja991153t · Cited by 197 · see citing works

Helical polymers for biological and medical applications

Leigh, T., & Fernández‐Trillo, F. (2020) · Nature Reviews Chemistry · doi:10.1038/s41570-020-0180-5 · Cited by 196 · see citing works

Geometry of nonbonded interactions involving planar groups in proteins

Chakrabarti, P., & Bhattacharyya, R. (2007) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2007.03.016 · Cited by 194 · see citing works

Neighbor-Dependent Ramachandran Probability Distributions of Amino Acids Developed from a Hierarchical Dirichlet Process Model

Ting, D., Wang, G., Shapovalov, M. V., Mitra, R., Jordan, M. I., & Dunbrack, R. L. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000763 · Cited by 193 · see citing works

ALK Mutations Conferring Differential Resistance to Structurally Diverse ALK Inhibitors

Heuckmann, J. M., Hölzel, M., Sos, M. L., Heynck, S., Balke‐Want, H., Koker, M., Peifer, M., Weiss, J. M., Lovly, C. M., Grütter, C., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1648 · Cited by 192 · see citing works

Secondary solute transport in bacteria

Poolman, B., & Konings, W. N. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90003-x · Cited by 191 · see citing works

Visualization of a water-selective pore by electron crystallography in vitreous ice

Ren, G., Reddy, V. S., Cheng, A., Melnyk, P., & Mitra, A. K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1398 · Cited by 188 · see citing works

Peptide bonds revisited

Weiss, M. S., Jabs, A., & Hilgenfeld, R. (1998) · Nature Structural & Molecular Biology · doi:10.1038/1368 · Cited by 188 · see citing works

Deviations from Planarity of the Peptide Bond in Peptides and Proteins

MacArthur, M. W., & Thornton, J. M. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0705 · Cited by 184 · see citing works

C—H⋯O hydrogen bond involving proline residues in α-helices

Chakrabarti, P., & Chakrabarti, S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2199 · Cited by 184 · see citing works

Proline Editing: A General and Practical Approach to the Synthesis of Functionally and Structurally Diverse Peptides. Analysis of Steric versus Stereoelectronic Effects of 4-Substituted Prolines on Conformation within Peptides

Pandey, A. K., Naduthambi, D., Thomas, K. M., & Zondlo, N. J. (2013) · Journal of the American Chemical Society · doi:10.1021/ja3109664 · Cited by 182 · see citing works

Multiple Proline Substitutions Cumulatively Thermostabilize Bacillus Cereus ATCC7064 Oligo‐1,6‐Glucosidase

Watanabe, K., Masuda, T., Ohashi, H., Mihara, H., & Suzuki, Y. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb20051.x · Cited by 179 · see citing works

Tertiary and quaternary conformational changes in aspartate transcarbamylase: a normal mode study

Thomas, A. M., Hinsen, K., Field, M. J., & Pérahia, D. (1999) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(19990101)34:1 · Cited by 64 · see citing works

Towards a structural view of gating in potassium channels

Swartz, K. J. (2004) · Nature reviews. Neuroscience · doi:10.1038/nrn1559 · Cited by 175 · see citing works

Molecular packing in the feather keratin filament

Fraser, R., & Parry, D. A. D. (2008) · Journal of Structural Biology · doi:10.1016/j.jsb.2008.01.011 · Cited by 173 · see citing works

Stereospecific Interactions of Proline Residues in Protein Structures and Complexes

Bhattacharyya, R., & Chakrabarti, P. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00759-9 · Cited by 172 · see citing works

A Model for the Photosystem II Reaction Center Core Including the Structure of the Primary Donor P680,

Svensson, B., Etchebest, C., Tufféry, P., van Kan, P. J. M., Smith, J. C., & Styring, S. (1996) · Biochemistry · doi:10.1021/bi960764k · Cited by 172 · see citing works

Three-dimensional representations of G protein-coupled receptor structures and mechanisms

Visiers, I., Ballesteros, J. A., & Weinstein, H. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)43145-x · Cited by 171 · see citing works

Antitumor effects, cell selectivity and structure–activity relationship of a novel antimicrobial peptide polybia-MPI

Wang, K., Zhang, B., Zhang, W., Yan, J., Li, J., & Wang, R. (2008) · Peptides · doi:10.1016/j.peptides.2008.01.015 · Cited by 170 · see citing works

Scanning the Intracellular S6 Activation Gate in the Shaker K+ Channel

Hackos, D. H., Chang, T.-H., & Swartz, K. J. (2002) · The Journal of General Physiology · doi:10.1085/jgp.20028569 · Cited by 169 · see citing works

Pseudo-Prolines as a Molecular Hinge: Reversible Induction ofcisAmide Bonds into Peptide Backbones

Dumy, P., Keller, M., Ryan, D., Rohwedder, B., Wöhr, T., & Mutter, M. (1997) · Journal of the American Chemical Society · doi:10.1021/ja962780a · Cited by 167 · see citing works

Standard structures in proteins

Efimov, A. V. (1993) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(93)90015-c · Cited by 165 · see citing works

CD of proline‐rich polypeptides: Application to the study of the repetitive domain of maize glutelin‐2

Rabanal, F., Ludevid, M. D., Pons, M., & Giralt, E. (1993) · Biopolymers · doi:10.1002/bip.360330704 · Cited by 161 · see citing works

Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006.

Watanabe, K., Chishiro, K., Kitamura, K., & Suzuki, Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54226-5 · Cited by 155 · see citing works

Three‐Dimensional Structure in Solution of a Wheat Lipid‐Transfer Protein from Multidimensional 1H‐NMR Data

Gincel, É., Simorre, J., Caille, A., Marion, D., Ptak, M., & Vovelle, F. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb20066.x · Cited by 154 · see citing works

Comparative conformational studies of polypeptides containing a high percentage of proline

Helbecque, N., & Loucheux‐Lefebvre, M. H. (1981) · Macromolecules · doi:10.1021/ma50004a032 · Cited by 2 · see citing works

ChemInform Abstract: Some Conformational Aspects of Linear Peptides Containing Proline

Anteunis, M. J. O., & SLEECKX, J. J. M. (1988) · ChemInform · doi:10.1002/chin.198822345

Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability

Vitagliano, L., Berisio, R., Mastrangelo, A., Mazzarella, L., & Zagari, A. (2001) · Protein Science · doi:10.1110/ps.ps.26601a · Cited by 153 · see citing works

Extensive exploration of the conformational landscapes of neutral and terminally blocked prolines in the gas phase: A density functional theory study

Yang, Y., & Lin, Z. (2022) · Journal of Chemical Research · doi:10.1177/17475198221110480 · Cited by 1 · see citing works

Study of the influence of neighboring amino acids on proline conformation

Herrera, J. E. C., Morales, S. A. N., Tilvaldyev, S., Montellano, A. V., & Ortega, A. F. (2016) · Mediterranean Journal of Chemistry · doi:10.13171/mjc56/01607261513/flores-ortega