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

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 8,574

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

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

A graphics model building and refinement system for macromolecules

Jones, T. A. (1978) · Journal of Applied Crystallography · doi:10.1107/s0021889878013308 · Cited by 1,833

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

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 1,116

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 1,064

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 985

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

Protein thermostabilization by proline substitutions

Watanabe, K., & Suzuki, Y. (1998) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/s1381-1177(97)00031-3 · Cited by 86

Gating of Shaker-type Channels Requires the Flexibility of S6 Caused by Prolines

Labro, A. J., Raes, A. L., Bellens, I., Ottschytsch, N., & Snyders, D. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306097200 · Cited by 86

Why are the same protein folds used to perform different functions?

Finkelstein, A. V., Gutun, A. M., & Badretdinov, A. Y. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81407-q · Cited by 86

Integrin LFA‐1 alpha subunit contains an ICAM‐1 binding site in domains V and VI.

Stanley, P., Bates, P. A., Harvey, J., Bennett, R. I., & Hogg, N. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06447.x · Cited by 86

Intrinsic Ribosome Destabilization Underlies Translation and Provides an Organism with a Strategy of Environmental Sensing

Chadani, Y., Niwa, T., Izumi, T., Sugata, N., Nagao, A., Suzuki, T., Chiba, S., Ito, K., & Taguchi, H. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.020 · Cited by 87

Prolyl Isomerization and Its Catalysis in Protein Folding and Protein Function

Schmidpeter, P. A. M., & Schmid, F. X. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.01.023 · Cited by 85

Metabolic quirks and the colourful history of the Euglena gracilis secondary plastid.

Vanclová, A. M. G. N., Zoltner, M., Kelly, S., Soukal, P., Záhonová, K., Füssy, Z., Ebenezer, T. E., Dobáková, E. L., Eliáš, M., Lukeš, J., et al. (2019) · New Phytologist · doi:10.1111/nph.16237 · Cited by 63

Effect of Sequence on Peptide Geometry in 5-tert-Butylprolyl Type VI β-Turn Mimics

Halab, L., & Lubell, W. D. (2002) · Journal of the American Chemical Society · doi:10.1021/ja012442w · Cited by 84

Hepatitis C Virus Glycoprotein E2 Contains a Membrane-proximal Heptad Repeat Sequence That Is Essential for E1E2 Glycoprotein Heterodimerization and Viral Entry

Drummer, H. E., & Poumbourios, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405098200 · Cited by 83

Thermodynamic effects of proline introduction on protein stability

Prajapati, R. S., Das, M., Sreeramulu, S., Sirajuddin, M., Srinivasan, S., Krishnamurthy, V., Ranjani, R., Ramakrishnan, C., & Varadarajan, R. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21215 · Cited by 82

Investigating the Putative Glycine Hinge in Shaker Potassium Channel

Ding, S., Ingleby, L., Ahern, C. A., & Horn, R. (2005) · The Journal of General Physiology · doi:10.1085/jgp.200509287 · Cited by 82

NMR Structure of the Human Prion Protein with the Pathological Q212P Mutation Reveals Unique Structural Features

Ilc, G., Giachin, G., Jaremko, M., Jaremko, Ł., Benetti, F., Plavec, J., Zhukov, I., & Legname, G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011715 · Cited by 82

Influence of Medium and Long Range Interactions in Different Structural Classes of Globular Proteins

Gromiha, M. M., & Selvaraj, S. (1997) · Journal of Biological Physics · doi:10.1023/a:1004981409616 · Cited by 82

Repeat regions R1 and R2 in the P97 paralogue Mhp271 of Mycoplasma hyopneumoniae bind heparin, fibronectin and porcine cilia

Deutscher, A. T., Jenkins, C., Minion, F. C., Seymour, L. M., Padula, M. P., Dixon, N. E., Walker, M. J., & Djordjevic, S. P. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07345.x · Cited by 79

Structural characterization of VGVAPG, an elastin‐derived peptide

Floquet, N., Héry‐Huynh, S., Dauchez, M., Derreumaux, P., Tamburro, A. M., & Alix, A. J. P. (2004) · Biopolymers · doi:10.1002/bip.20029 · Cited by 79

A Variable Region 3 (V3) Mutation Determines a Global Neutralization Phenotype and CD4-Independent Infectivity of a Human Immunodeficiency Virus Type 1 Envelope Associated with a Broadly Cross-Reactive, Primary Virus-Neutralizing Antibody Response

Zhang, P. F., Bouma, P., Park, E. J., Margolick, J. B., Robinson, J. E., Zolla‐Pazner, S., Flora, M. N., & Quinnan, G. V. (2002) · Journal of Virology · doi:10.1128/jvi.76.2.644-655.2002 · Cited by 79

Local Propensities and Statistical Potentials of Backbone Dihedral Angles in Proteins

Betancourt, M. R., & Skolnick, J. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.06.091 · Cited by 78

β-Turn Preferences Induced by 2,3-Methanophenylalanine Chirality

Jiménez, A. I., Cativiela, C., Aubry, A., & Marraud, M. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9807439 · Cited by 80

Sequence-Specific Unusual (1→2)-Type Helical Turns in α/β-Hybrid Peptides

Prabhakaran, P., Kale, S. S., Puranik, V. G., Rajamohanan, P. R., Chetina, O. V., Howard, J. A. K., Hofmann, H., & Sanjayan, G. J. (2008) · Journal of the American Chemical Society · doi:10.1021/ja804297f · Cited by 77

Stereochemical Criteria for Prediction of the Effects of Proline Mutations on Protein Stability

Pahuja, K. B., Madhusudhan, M. S., Adkar, B. V., Chakrabarti, P., Ramakrishnan, C., Šali, A., & Varadarajan, R. (2005) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0030241 · Cited by 77

Processing of peptide and hormone precursors at the dibasic cleavage sites

Rholam, M., & Fahy, C. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0007-5 · Cited by 76

Directed evolution to probe protein allostery and integrin I domains of 200,000-fold higher affinity

Jin, M. M., Song, G., Carman, C. V., Kim, Y., Astrof, N. S., Shimaoka, M., Wittrup, K. D., & Springer, T. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601164103 · Cited by 76

Prolyl Isomerases

Schmid, F. X. (2001) · Advances in protein chemistry · doi:10.1016/s0065-3233(01)59008-7 · Cited by 76

The Crystal Structure of H-2Dd MHC Class I Complexed with the HIV-1-Derived Peptide P18-I10 at 2.4 Å Resolution

Achour, A., Persson, K., Harris, R. A., Sundbäck, J., Sentman, C. L., Lindqvist, Y., Schneider, G., & Kärre, K. (1998) · Immunity · doi:10.1016/s1074-7613(00)80602-0 · Cited by 75

Modifications of the amide bond and conformational constraints in pseudopeptide analogues

Marraud, M., Dupont, V., Grand, V., Zerkout, S., Lecoq, A., BOUSSARD, G., Vidal, J., Collet, A., & Aubry, A. (1993) · Biopolymers · doi:10.1002/bip.360330715 · Cited by 75

Fluorinated Prolines as Conformational Tools and Reporters for Peptide and Protein Chemistry

Verhoork, S. J. M., Killoran, P. M., & Coxon, C. R. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00787 · Cited by 73

Conformational landscape of substituted prolines

Ganguly, H. K., & Basu, G. (2020) · Biophysical Reviews · doi:10.1007/s12551-020-00621-8 · Cited by 73

Kv Channel Gating Requires a Compatible S4-S5 Linker and Bottom Part of S6, Constrained by Non-interacting Residues

Labro, A. J., Raes, A. L., Grottesi, A., Hoorick, D. V., Sansom, M. S. P., & Snyders, D. J. (2008) · The Journal of General Physiology · doi:10.1085/jgp.200810048 · Cited by 73

Analysis of Loops that Mediate Protein–Protein Interactions and Translation into Submicromolar Inhibitors

Siegert, T. R., Bird, M. J., Makwana, K. M., & Kritzer, J. A. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b05656 · Cited by 74

A New Approach to Docking in the β2-Adrenergic Receptor That Exploits the Domain Structure of G-Protein-Coupled Receptors

Gouldson, P. R., Snell, C. R., & Reynolds, C. A. (1997) · Journal of Medicinal Chemistry · doi:10.1021/jm960647n · Cited by 73

Peptide Self-Replication Enhanced by a Proline Kink

Li, X., & Chmielewski, J. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja036569s · Cited by 72

Determination of the Three-Dimensional Structure of Margatoxin by 1H, 13C, 15N Triple-Resonance Nuclear Magnetic Resonance Spectroscopy

Johnson, B. A., Stevens, S. P., & Williamson, J. M. (1994) · Biochemistry · doi:10.1021/bi00254a015 · Cited by 72

Composites of local structure propensities: Evidence for local encoding of long-range structure

Shortle, D. (2002) · Protein Science · doi:10.1110/ps.31002 · Cited by 71

Cotranslational Incorporation of a Structurally Diverse Series of Proline Analogues in an Escherichia coli Expression System

Kim, W., George, A., Evans, M., & Conticello, V. P. (2004) · ChemBioChem · doi:10.1002/cbic.200400052 · Cited by 70

The First Transmembrane Segment of the Dopamine D2 Receptor: Accessibility in the Binding-Site Crevice and Position in the Transmembrane Bundle

Shi, L., Simpson, M. M., Ballesteros, J. A., & Javitch, J. A. (2001) · Biochemistry · doi:10.1021/bi011204a · Cited by 70

Saturation mutagenesis of the human interleukin 6 receptor-binding site: implications for its three-dimensional structure.

Savino, R., Lahm, A., Giorgio, M., Cabibbo, A., Tramontano, A. L., & Ciliberto, G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.9.4067 · Cited by 70

Can a pairwise contact potential stabilize native protein folds against decoys obtained by threading?

Vendruscolo, M., Najmanovich, R., & Domany, E. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(20000201)38:2 · Cited by 115

The effect of the polyproline II (PPII) conformation on the denatured state entropy

Ferreon, J. C., & Hilser, V. J. (2003) · Protein Science · doi:10.1110/ps.0237803 · Cited by 69

Substituted 2-Azabicyclo[2.1.1]hexanes as Constrained Proline Analogues: Implications for Collagen Stability

Jenkins, C. L., Lin, G., Duo, J., Rapolu, D., Guzei, I. A., Raines, R. T., & Krow, G. R. (2004) · The Journal of Organic Chemistry · doi:10.1021/jo049242y · Cited by 69

Mutations in human glycine N-methyltransferase give insights into its role in methionine metabolism

Luka, Z., Cerone, R., Phillips, J. A., Mudd, H. S., & Wagner, C. (2001) · Human Genetics · doi:10.1007/s00439-001-0648-4 · Cited by 69

Topography of Nicotinic Acetylcholine Receptor Membrane-embedded Domains

Barrantes, F. J., Antollini, S. S., Blanton, M., & PRIETO, M. J. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005246200 · Cited by 69

Identification of selectivity‐determining residues in cytochrome P450 monooxygenases: A systematic analysis of the substrate recognition site 5

Seifert, A., & Pleiss, J. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22242 · Cited by 68

Prediction of peptides binding to the PKA RIIα subunit using a hierarchical strategy

Hou, T., Li, Y., & Wang, W. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr294 · Cited by 67

Biofunctional domains of the Mycoplasma pneumoniae P30 adhesin

Dallo, S. F., Lazzell, A. L., Chavoya, A., Reddy, S. P., & Baseman, J. B. (1996) · Infection and Immunity · doi:10.1128/iai.64.7.2595-2601.1996 · Cited by 67

Molecular cloning of a mammalian nuclear phosphoprotein NUCKS, which serves as a substrate for Cdk1 in vivo

Østvold, A. C., Norum, J. H., Mathiesen, S. B. W., Wanvik, B., Sefland, I., & Grundt, K. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02120.x · Cited by 67

Aza‐peptides II. X‐Ray structures of aza‐alanine and aza‐asparagine‐containing peptides

André, F., BOUSSARD, G., Bayeul, D., Claude Didierjean, B., Aubry, A., & Marraud, M. (1997) · Journal of Peptide Research · doi:10.1111/j.1399-3011.1997.tb01163.x · Cited by 67

Flanking regions determine the structure of the poly-glutamine in Huntingtin through mechanisms common among glutamine-rich human proteins

Urbanek, A., Popovic, M., Morató, A., Estaña, A., Elena-Real, C. A., Mier, P., Fournet, A., Allemand, F., Delbecq, S., Andrade-Navarro, M. A., et al. (2020) · Structure · doi:10.1016/j.str.2020.04.008 · Cited by 66

Designed Peptides with Homochiral and Heterochiral Diproline Templates as Conformational Constraints

Chatterjee, B., Saha, I., Raghothama, S., Aravinda, S., Rai, R., Shamala, N., & Balaram, P. (2008) · Chemistry - A European Journal · doi:10.1002/chem.200702029 · Cited by 66

Impact of Cis‐proline analogs on peptide conformation

Che, Y., & Marshall, G. R. (2005) · Biopolymers · doi:10.1002/bip.20431 · Cited by 66

Cyanovirin-N: a sugar-binding antiviral protein with a new twist

Botos, I., & Wlodawer, A. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s000180300023 · Cited by 66

Protein Prosthesis: A Nonnatural Residue Accelerates Folding and Increases Stability

Arnold, U., Hinderaker, M. P., Köditz, J., Golbik, R. P., Ulbrich‐Hofmann, R., & Raines, R. T. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0351239 · Cited by 66

Understanding the Role of Stereoelectronic Effects in Determining Collagen Stability. 2. A Quantum Mechanical/Molecular Mechanical Study of (Proline-Proline-Glycine)n Polypeptides

Improta, R., Mele, F., Crescenzi, O., Benzi, C., & Barone, V. (2002) · Journal of the American Chemical Society · doi:10.1021/ja020187p · Cited by 66

Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme

Nicholson, H., Tronrud, D. E., Becktel, W. J., & Matthews, B. W. (1992) · Biopolymers · doi:10.1002/bip.360321103 · Cited by 66

Propensities, probabilities, and the Boltzmann hypothesis

Shortle, D. (2003) · Protein Science · doi:10.1110/ps.0306903 · Cited by 66

Azaproline as a β‐turn‐inducer residue opposed to proline

Zouikri, M., Vicherat, A., Aubry, A., Marraud, M., & BOUSSARD, G. (1998) · Journal of Peptide Research · doi:10.1111/j.1399-3011.1998.tb00648.x · Cited by 66

Prediction of transmembrane β‐strands from hydrophobic characteristics of proteins

Gromiha, M. M., & Ponnuswamy, P. K. (1993) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1993.tb00149.x · Cited by 66

ITIH4 acts as a protease inhibitor by a novel inhibitory mechanism

Pihl, R., Jensen, R. K., Poulsen, E. C., Jensen, L., Hansen, A. G., Thøgersen, I. B., Dobó, J., Gál, P., Andersen, G. R., Enghild, J. J., et al. (2021) · Science Advances · doi:10.1126/sciadv.aba7381 · Cited by 65

A Putative Gene sbe3-rs for Resistant Starch Mutated from SBE3 for Starch Branching Enzyme in Rice (Oryza sativa L.)

Yang, R., Sun, C., Bai, J., Luo, Z., Shi, B., Zhang, J., Yan, W., & Piao, Z. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043026 · Cited by 65

Aspects of protein energetics and dynamics

Rashin, A. A. (1993) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(93)90017-e · Cited by 65

Collisionally activated dissociation and tandem mass spectrometry of intact hemoglobin β-chain variant proteins with electrospray ionization

Light‐Wahl, K. J., Loo, J. A., Edmonds, C. G., Smith, R. D., Witkowska, H. E., Shackleton, C. H. L., & Wu, C. C. (1993) · Journal of Mass Spectrometry · doi:10.1002/bms.1200220203 · Cited by 65

Missense mutations in the DNA-binding/dimerization domain of NFIX cause Sotos-like features

Yoneda, Y., Saitsu, H., Touyama, M., Makita, Y., Miyamoto, A., Hamada, K., Kurotaki, N., Tomita, H., Nishiyama, K., Tsurusaki, Y., et al. (2012) · Journal of Human Genetics · doi:10.1038/jhg.2012.7 · Cited by 64

IDPConformerGenerator: A Flexible Software Suite for Sampling the Conformational Space of Disordered Protein States

Teixeira, J. M. C., Liu, Z. H., Namini, A., Li, J., Vernon, R. M., Krzeminski, M., Shamandy, A. A., Zhang, O., Haghighatlari, M., Yu, L., et al. (2022) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.2c03726 · Cited by 63

Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues

Watanabe, K., Kitamura, K., & Suzuki, Y. (1996) · Applied and Environmental Microbiology · doi:10.1128/aem.62.6.2066-2073.1996 · Cited by 63

Proline Affects Oligomerization of a Coiled Coil by Inducing a Kink in a Long Helix

Chang, D., Cheng, S., Trivedi, V. D., & Lin, K.-L. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4182 · Cited by 63

Proline Analogues

Kubyshkin, V., & Rubini, M. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00007 · Cited by 64

A Plasmodium falciparum 48/45 single epitope R0.6C subunit protein elicits high levels of transmission blocking antibodies

Singh, S. K., Roeffen, W., Andersen, G., Bousema, T., Christiansen, M., Sauerwein, R. W., & Theisen, M. (2015) · Vaccine · doi:10.1016/j.vaccine.2015.02.040 · Cited by 62

Molecular Basis for Proline- and Arginine-Rich Peptide Inhibition of Proteasome

Anbanandam, A., Albarado, D. C., Tı̂rziu, D., Simons, M., & Veeraraghavan, S. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.09.021 · Cited by 62

Disordered proteins studied by chemical shifts

Kjærgaard, M., & Poulsen, F. M. (2011) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2011.10.001 · Cited by 68

Diproline Templates as Folding Nuclei in Designed Peptides. Conformational Analysis of Synthetic Peptide Helices Containing Amino Terminal Pro-Pro Segments

Rai, R., Aravinda, S., Kanagarajadurai, K., Raghothama, S., Shamala, N., & Balaram, P. (2006) · Journal of the American Chemical Society · doi:10.1021/ja060674v · Cited by 61

Testing computational prediction of missense mutation phenotypes: Functional characterization of 204 mutations of human cystathionine beta synthase

Wei, Q., Wang, L., Wang, Q., Kruger, W. D., & Dunbrack, R. L. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22722 · Cited by 62

Effects of amino acid composition, finite size of proteins, and sparse statistics on distance‐dependent statistical pair potentials

Rykunov, D., & Fiser, A. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21279 · Cited by 63

Solvent and conformation dependence of amide I vibrations in peptides and proteins containing proline

Roy, S., Lessing, J., Meisl, G., Ganim, Z., Tokmakoff, A., Knoester, J., & Jansen, T. L. C. (2011) · The Journal of Chemical Physics · doi:10.1063/1.3665417 · Cited by 61

Stabilization of local structures by π–CH and aromatic–backbone amide interactions involving prolyl and aromatic residues

Tóth, G., Murphy, R. F., & Lovas, S. (2001) · Protein Engineering Design and Selection · doi:10.1093/protein/14.8.543 · Cited by 61

Molecular Epidemiology and Evolution of Human Respiratory Syncytial Virus and Human Metapneumovirus

Gaunt, E. R., Jansen, R. R., Poovorawan, Y., Templeton, K. E., Toms, G. L., & Peter Simmonds, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017427 · Cited by 61

Unravelling the folding of bacteriorhodopsin

Booth, P. J. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00125-0 · Cited by 61

Respiratory insufficiency in desminopathy patients caused by introduction of proline residues in desmin c‐terminal α‐helical segment

Dagvadorj, A., Goudeau, B., Hilton‐Jones, D., Blancato, J. K., Shatunov, A., Casteras-Simon, M., Squier, W., Nagle, J. W., Goldfarb, L. G., & Vicart, P. (2003) · Muscle & Nerve · doi:10.1002/mus.10370 · Cited by 61

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Raybaud, A., Dodier, Y., Bissonnette, P., Simoes, M., Bichet, D. G., Sauvé, R., & Parent, L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607405200 · Cited by 61

Post‐translational hydroxylation at the N‐terminus of the prion protein reveals presence of PPII structure in vivo

Gill, A. C., Ritchie, M. A., Hunt, L. G., Steane, S. E., Davies, K. G., Bocking, S. P., Rhie, A. G. O., Bennett, A. D., & Hope, J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.20.5324 · Cited by 61

A connecting hinge represses the activity of endothelial nitric oxide synthase

Haque, M. M., Panda, K., Tejero, J., Aulak, K. S., Fadlalla, M., Mustovich, A. T., & Stuehr, D. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700332104 · Cited by 61

Determination of the Structure of the N-terminal Splice Region of the Cyclic AMP-specific Phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and Identification of the Membrane Association Domain Using Chimeric Constructs

Smith, K. J., Scotland, G., Beattie, J., Trayer, I. P., & Houslay, M. D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.28.16703 · Cited by 61

5-tert-Butylproline

Beausoleil, E., L'Archevêque, B., Bélec, L., Atfani, M., & Lubell, W. D. (1996) · The Journal of Organic Chemistry · doi:10.1021/jo9618738 · Cited by 61

Homology of the root adhesin of Pseudomonas fluorescens OE 28.3 with porin F of P. neruginosa and P. syringae

Mot, R. D., Proost, P., Damme, J. V., & Vanderleyden, J. (1992) · Molecular and General Genetics MGG · doi:10.1007/bf00292721 · Cited by 61

Structure of restriction endonuclease BamHI phased at 1.95 å resolution by MAD analysis

Newman, M., Strzelecka, T. E., Dorner, L. F., Schildkraut, I., & Aggarwal, A. K. (1994) · Structure · doi:10.1016/s0969-2126(00)00045-9 · Cited by 61

Efficient Synthesis of cis ‐3‐Substituted Prolines by Bidentate‐Assisted Palladium Catalysis

Feng, R., Wang, B., Liu, Y., Liu, Z., & Zhang, Y. (2014) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201403191 · Cited by 60

4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins

Newberry, R. W., & Raines, R. T. (2016) · Topics in heterocyclic chemistry · doi:10.1007/7081_2015_196 · Cited by 60

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Schuman, J. T., Campbell, A. P., Koganty, R. R., & Longenecker, B. M. (2003) · Journal of Peptide Research · doi:10.1034/j.1399-3011.2003.00031.x · Cited by 60

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Reimer, U., & Fischer, G. S. (2002) · Biophysical Chemistry · doi:10.1016/s0301-4622(02)00013-3 · Cited by 60

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Böhm, G. (1996) · Biophysical Chemistry · doi:10.1016/0301-4622(95)00120-4 · Cited by 60

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Williams, K. A., Farrow, N. A., Deber, C. M., & Kay, L. E. (1996) · Biochemistry · doi:10.1021/bi952897w · Cited by 60

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Schultz, D., & Baldwin, R. L. (1992) · Protein Science · doi:10.1002/pro.5560010709 · Cited by 60

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Coombs, G., Sak, M. H., & Miller, S. J. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201913563 · Cited by 59

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Taylor, C. M., Hardré, R., Edwards, P. J. B., & Park, J. H. (2003) · Organic Letters · doi:10.1021/ol035711r · Cited by 59

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Goudeau, B., Rodrigues‐Lima, F., Fischer, D., Casteras-Simon, M., Sambuughin, N., de Visser, M., Laforêt, P., Ferrer, X., Chapon, F., Sjöberg, G., et al. (2006) · Human Mutation · doi:10.1002/humu.20351 · Cited by 59

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Suh, J., Lee, Y., Park, C., Lee, K., Kim, S., & Choi, B. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00917.x · Cited by 58

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

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