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Nmr studies of the rates of proline cis – trans isomerization in oligopeptides
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/bip.1976.360151012openalex-snapshot
The X‐Pro peptide bond as an nmr probe for conformational studies of flexible linear peptides
inferredcites →https://doi.org/10.1002/bip.1976.360151013openalex-snapshot
Nmr studies of the molecular conformations in the linear oligopeptides H‐( L ‐Ala) n ‐ L ‐Pro‐OH
inferredcites →https://doi.org/10.1002/bip.1977.360160415openalex-snapshot
Determination of the rates and barriers to conformational isomerization in the dipeptide L ‐pro‐ L ‐4hyp by direct 13C nmr thermal equilibration
inferredcites →https://doi.org/10.1002/bip.1977.360160707openalex-snapshot
Cis‐Trans equilibrium and kinetic studies of acetyl‐ L ‐proline and glycyl‐ L ‐proline
inferredcites →https://doi.org/10.1002/bip.1979.360181015openalex-snapshot
Conformational energy studies of linear dipeptides H‐X‐ L ‐Pro‐OH
inferredcites →https://doi.org/10.1002/hlca.19720550614openalex-snapshot
Conformational Studies of Cyclic Pentapeptides by Proton Magnetic Resonance Spectroscopy
inferredcites →https://doi.org/10.1016/0014-5793(72)80464-2openalex-snapshot
Manifestation in the 13C‐NMR spectra of two different molecular conformations of a cyclic pentapeptide
inferredcites →https://doi.org/10.1016/0014-5793(74)80475-8openalex-snapshot
Two cis‐prolines in the Bence‐Jones protein Rei and the cis‐pro‐bend
inferredcites →https://doi.org/10.1016/0014-5793(74)80674-5openalex-snapshot
A novel approach for studies of the molecular conformations in flexible polypeptides
inferredcites →https://doi.org/10.1016/0022-2364(78)90001-xopenalex-snapshot
Fourier transform NMR pulse methods for the measurement of slow-exchange rates
inferredcites →https://doi.org/10.1016/0022-2836(78)90411-4openalex-snapshot
Possible implications of many proline residues for the kinetics of protein unfolding and refolding
inferredcites →https://doi.org/10.1016/0968-0004(77)90231-6openalex-snapshot
NMR in biological research: Peptides and proteins
inferredcites →https://doi.org/10.1016/s0006-291x(71)80207-3openalex-snapshot
Hindered rotation in N-methylformamide. A peptide-bond model system
inferredcites →https://doi.org/10.1016/s0021-9258(18)63395-2openalex-snapshot
The Three-Dimensional Structure of Ribonuclease-S
inferredcites →https://doi.org/10.1016/s0079-6565(66)80004-3openalex-snapshot
High resolution nuclear magnetic double and multiple resonance
inferredcites →https://doi.org/10.1021/bi00612a036openalex-snapshot
Further evidence suggesting that the slow phase in protein unfolding and refolding is due to proline isomerization: a kinetic study of carp parvalbumins
inferredcites →https://doi.org/10.1021/bi00693a026openalex-snapshot
Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
inferredcites →https://doi.org/10.1021/ja01057a007openalex-snapshot
cis and trans Configurations of the Peptide Bond in N-Monosubstituted Amides by Nuclear Magnetic Resonance
inferredcites →https://doi.org/10.1021/jo00953a021openalex-snapshot
Carbon-13 magnetic resonance spectroscopy. Spectrum of proline in oligopeptides
inferredcites →https://doi.org/10.1021/ma60014a013openalex-snapshot
Calculation of the Conformation of the Pentapeptide cyclo-(Glycylglycylglycylprolylprolyl). I. A Complete Energy Map
inferredcites →https://doi.org/10.1021/ma60020a022openalex-snapshot
A Nuclear Magnetic Resonance Study of Poly(L-proline) in Aqueous and Aqueous Salt Solutions
inferredcites →https://doi.org/10.1038/221235a0openalex-snapshot
Structure of Subtilisin BPN′ at 2.5 Å Resolution
inferredcites →https://doi.org/10.1039/c29710001209openalex-snapshot
Evaluation of the thermodynamic parameters for the interconversion of the conformational isomers of two N-acyl-prolines by nuclear magnetic resonance spectroscopy
inferredcites →https://doi.org/10.1073/pnas.74.10.4178openalex-snapshot
Unfolding and refolding occur much faster for a proline-free proteins than for most proline-containing proteins.
inferredcites →https://doi.org/10.1073/pnas.75.10.4764openalex-snapshot
Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerization
inferredcites →https://doi.org/10.1073/pnas.76.12.6157openalex-snapshot
Role of proline isomerization in folding of ribonuclease A at low temperatures
inferredcites →https://doi.org/10.1073/pnas.77.2.795openalex-snapshot
Evidence for involvement of proline cis-trans isomerization in the slow unfolding reaction of RNase A.
inferredcites →https://doi.org/10.1111/j.1432-1033.1978.tb12641.xopenalex-snapshot
The Role of Cis-Trans Isomerization of Peptide Bonds in the Coil Triple Helix Conversion of Collagen
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Structure of the LAV6 peptide: A nucleation site for the correct receptor-induced refolding of the CD4-binding domain of HIV1 gp 120
inferred← citeshttps://doi.org/10.1002/(sici)1097-0282(199707)42:1<49::aid-bip5>3.0.co;2-1openalex-snapshot
FKBP-like catalysis of peptidyl-prolyl bond isomerization by micelles and membranes
inferred← citeshttps://doi.org/10.1002/(sici)1097-0282(19980415)45:5<381::aid-bip6>3.0.co;2-hopenalex-snapshot
Local control of peptide conformation: Stabilization ofcis proline peptide bonds by aromatic proline interactions
inferred← citeshttps://doi.org/10.1002/(sici)1097-0282(1999)51:2<121::aid-bip2>3.0.co;2-oopenalex-snapshot
Pseudo-prolines: Induction ofcis/trans-conformational interconversion by decreased transition state barriers
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NMR and protein dynamics
inferred← citeshttps://doi.org/10.1002/(sici)1099-1387(199808)4:5<364::aid-psc159>3.0.co;2-oopenalex-snapshot
Trans-cis amide bond isomerization in fulleroprolines
inferred← citeshttps://doi.org/10.1002/(sici)1521-3757(20000317)112:6<1163::aid-ange1163>3.0.co;2-hopenalex-snapshot
Ein-Atom-Substitution in Peptiden: Bildung eines photoschaltbaren Elements im Peptidrückgrat durch Thioxylierung
inferred← citeshttps://doi.org/10.1002/0471250570.spi095openalex-snapshot
Protein Processing, Processing in the Endoplasmic Reticulum and G olgi Network
inferred← citeshttps://doi.org/10.1002/1439-7633(20010803)2:7/8<524::aid-cbic524>3.0.co;2-popenalex-snapshot
Metal Ion Effects on the cis/trans Isomerization Equilibrium of Proline in Short-Chain Peptides: A Solution NMR Study
inferred← citeshttps://doi.org/10.1002/1522-2683(200107)22:12<2409::aid-elps2409>3.0.co;2-copenalex-snapshot
Determination of thecis-trans isomerization barrier of severalL-peptidyl-L-proline dipeptides by dynamic capillary electrophoresis and computer simulation
inferred← citeshttps://doi.org/10.1002/9781118183373.ch4openalex-snapshot
Short‐Distance FRET Applied to the Polypeptide Chain
inferred← citeshttps://doi.org/10.1002/9783527619498.ch25openalex-snapshot
Prolyl Isomerization in Protein Folding
inferred← citeshttps://doi.org/10.1002/9783527636402.ch14openalex-snapshot
From Dynamics to Kinetics: Investigation of Interconverting Stereoisomers and Catalyzed Reactions
inferred← citeshttps://doi.org/10.1002/ajoc.202500622openalex-snapshot
Biomimetic Cavity‐Induced Catalysis Inside Synthetic Containers
inferred← citeshttps://doi.org/10.1002/ange.201003389openalex-snapshot
Elektronentransfer in Peptiden: der Einfluss geladener Aminosäuren
inferred← citeshttps://doi.org/10.1002/anie.201003389openalex-snapshot
Electron Transfer in Peptides: The Influence of Charged Amino Acids
inferred← citeshttps://doi.org/10.1002/bies.201900250openalex-snapshot
Peptidylprolylisomerases, Protein Folders, or Scaffolders? The Example of FKBP51 and FKBP52
inferred← citeshttps://doi.org/10.1002/bip.20164openalex-snapshot
O‐acylation of hydroxyproline residues: Effect on peptide‐bond isomerization and collagen stability
inferred← citeshttps://doi.org/10.1002/bip.20643openalex-snapshot
Synthesis of a new π‐deficient phenylalanine derivative from a common 1,4‐diketone intermediate and study of the influence of aromatic density on prolyl amide isomer population
inferred← citeshttps://doi.org/10.1002/bip.21620openalex-snapshot
Systematic conformational investigations of peptoids and peptoid–peptide chimeras
inferred← citeshttps://doi.org/10.1002/bip.21716openalex-snapshot
Effects of ring contraction on the conformational preferences of α‐substituted proline analogs
inferred← citeshttps://doi.org/10.1002/bip.360240119openalex-snapshot
Prolyl isomerization: How significant for in vivo protein folding?
inferred← citeshttps://doi.org/10.1002/bip.360290123openalex-snapshot
Enkephalin analogues containing β‐naphthylalanine at the fourth position
inferred← citeshttps://doi.org/10.1002/bip.360311207openalex-snapshot
Assignment of the 1H‐nmr resonances of the four rotamers of β‐casomorphin‐5 in DMSO
inferred← citeshttps://doi.org/10.1002/bip.360311404openalex-snapshot
Conformational heterogeneity of quinoxaline peptides in solution
inferred← citeshttps://doi.org/10.1002/bip.360320807openalex-snapshot
Morphiceptin and β‐casomorphin‐5 analogues containing a reduced peptide bond: Selective μ‐receptor agonists and a novel μ antagonist, H‐Tyr‐Proψ(CH2‐NH)Phe‐Pro‐Gly‐OH
inferred← citeshttps://doi.org/10.1002/bip.360330507openalex-snapshot
1H‐ and 13C‐nmr investigations on cis–trans isomerization of proline peptide bonds and conformation of aromatic side chains in H‐Trp‐(Pro)n‐Tyr‐OH peptides
inferred← citeshttps://doi.org/10.1002/bip.360340910openalex-snapshot
Conformational differences between cis and trans proline isomers of a peptide antigen representing the receptor binding domain of Pseudomonas aeruginosa as studied by 1H‐nmr
inferred← citeshttps://doi.org/10.1002/bip.360360204openalex-snapshot
Multiple interconverting conformers of the cyclic tetrapeptide tentoxin, [cyclo‐( L ‐MeAla1‐ L ‐Leu2‐MePhe[(Z)Δ]3‐Gly4)], as seen by two‐dimensional 1H‐nmr spectroscopy
inferred← citeshttps://doi.org/10.1002/bip.360360608openalex-snapshot
1H‐nmr studies on the structure of a new thionin from barley endosperm
inferred← citeshttps://doi.org/10.1002/cbic.201700548openalex-snapshot
Propensity for cis‐Proline Formation in Unfolded Proteins
inferred← citeshttps://doi.org/10.1002/cbic.202500476openalex-snapshot
Phenyl Urea as an Aglet for Stabilizing Trans Proline: A Mimic of Ile–Phe Zipper
inferred← citeshttps://doi.org/10.1002/chem.200702029openalex-snapshot
Designed Peptides with Homochiral and Heterochiral Diproline Templates as Conformational Constraints
inferred← citeshttps://doi.org/10.1002/chem.202203017openalex-snapshot
Probing Peptidylprolyl Bond cis/trans Status Using Distal 19F NMR Reporters
inferred← citeshttps://doi.org/10.1002/chin.198619370openalex-snapshot
ChemInform Abstract: NMR Studies of Amino Acids, Peptides, and Proteins: a Brief Review, 1980‐1982
inferred← citeshttps://doi.org/10.1002/cmr.a.10094openalex-snapshot
Measuring ligand‐protein binding using NMR diffusion experiments
inferred← citeshttps://doi.org/10.1002/elps.1150190224openalex-snapshot
Separation of cis/trans conformers of human and salmon calcitonin by low temperature capillary electrophoresis
inferred← citeshttps://doi.org/10.1002/elps.200305746openalex-snapshot
Determination of the cis‐trans isomerization barrier of enalaprilat by dynamic capillary electrophoresis and computer simulation
inferred← citeshttps://doi.org/10.1002/elps.200900599openalex-snapshot
Investigation of the stereodynamics of molecules and catalyzed reactions by CE
inferred← citeshttps://doi.org/10.1002/hlca.19950780218openalex-snapshot
Structure‐Lipophilicity and Structure‐Polarity relationships of amino acids and peptides
inferred← citeshttps://doi.org/10.1002/hlca.200390347openalex-snapshot
Derivatives of Coenzyme F430 with a Covalently Attached α‐Axial Ligand. Part I
inferred← citeshttps://doi.org/10.1002/jhet.4532openalex-snapshot
Total synthesis of a reversed cyclopurpuracin using a combination of solid and solution phase methods
inferred← citeshttps://doi.org/10.1002/jps.22069openalex-snapshot
Elucidating the Pathways of Degradation of Denagliptin
inferred← citeshttps://doi.org/10.1002/nbm.1940030303openalex-snapshot
Spin‐exchange NMR spectroscopy in studies of the kinetics of enzymes and membrane transport
inferred← citeshttps://doi.org/10.1002/pro.5560010710openalex-snapshot
Cis proline mutants of ribonuclease A. II. Elimination of the slow‐folding forms by mutation
inferred← citeshttps://doi.org/10.1002/pro.5560020514openalex-snapshot
NMR analysis of staphylococcal nuclease thermal quench refolding kinetics
inferred← citeshttps://doi.org/10.1002/pro.5560030717openalex-snapshot
Multiple conformations of the sea anemone polypeptide anthopleurin‐A in solution
inferred← citeshttps://doi.org/10.1002/pro.5560060821openalex-snapshot
Multiple conformations of a human interleukin‐3 variant
inferred← citeshttps://doi.org/10.1002/pro.70044openalex-snapshot
Conformational dynamics in specialized C2H2 zinc finger domains enable zinc‐responsive gene repression in S. pombe
inferred← citeshttps://doi.org/10.1002/prot.20759openalex-snapshot
A dynamic N‐capping motif in cytochrome b5: Evidence for a pH‐controlled conformational switch
inferred← citeshttps://doi.org/10.1002/prot.21294openalex-snapshot
Probing nascent structures in peptides using natural abundance 13C NMR relaxation and reduced spectral density mapping
inferred← citeshttps://doi.org/10.1002/prot.26589openalex-snapshot
Insights into the solution structure and transcriptional regulation of the MazE9 antitoxin in Mycobacterium tuberculosis
inferred← citeshttps://doi.org/10.1002/prot.340120210openalex-snapshot
Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate
inferred← citeshttps://doi.org/10.1002/prot.340170110openalex-snapshot
Primary structure effects on peptide group hydrogen exchange
inferred← citeshttps://doi.org/10.1002/qua.22413openalex-snapshot
Adaptively biased molecular dynamics: An umbrella sampling method with a time‐dependent potential
inferred← citeshttps://doi.org/10.1002/qua.22875openalex-snapshot
Free energy and structure of polyproline peptides: An ab initio and classical molecular dynamics investigation
inferred← citeshttps://doi.org/10.1006/jmbi.1997.0960openalex-snapshot
Folding of the disulfide-bonded β-sheet protein tendamistat: rapid two-state folding without hydrophobic collapse 1 1Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1043openalex-snapshot
The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1219openalex-snapshot
Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease Δ131Δ, using NMR methods with improved resolution
inferred← citeshttps://doi.org/10.1006/jmbi.1998.1770openalex-snapshot
Side-chain effects on peptidyl-prolyl cis/trans isomerisation
inferred← citeshttps://doi.org/10.1006/jmbi.1998.2173openalex-snapshot
Stability and folding of the cell cycle regulatory protein, p13 suc1 1 1Edited by F. E. Cohen
inferred← citeshttps://doi.org/10.1006/jmbi.1998.2420openalex-snapshot
Stability and folding of the tumour suppressor protein p16 1 1Edited by J. Karn
inferred← citeshttps://doi.org/10.1006/jmbi.1998.2425openalex-snapshot
Folding and assembly of an antibody Fv fragment, a heterodimer stabilized by antigen 1 1Edited by P. E. Wright
inferred← citeshttps://doi.org/10.1006/jmbi.1999.2941openalex-snapshot
Folding Pathway of FKBP12 and Characterisation of the Transition State
inferred← citeshttps://doi.org/10.1006/jmbi.1999.3217openalex-snapshot
Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations 1 1Edited by J. M. Thornton
inferred← citeshttps://doi.org/10.1006/jmbi.2000.4002openalex-snapshot
Multiple roles of prolyl residues in structure and folding 1 1Edited by C. Robert Matthews
inferred← citeshttps://doi.org/10.1006/jmbi.2001.4535openalex-snapshot
Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR11Edited by P. E. Wright
inferred← citeshttps://doi.org/10.1007/0-306-46850-6_13openalex-snapshot
Chaperone and foldase coexpression in the baculovirus-insect cell expression system
inferred← citeshttps://doi.org/10.1007/978-1-62703-017-5_12openalex-snapshot
Recipes for Free Energy Calculations in Biomolecular Systems
inferred← citeshttps://doi.org/10.1007/978-3-642-54640-2_24openalex-snapshot
Physicochemical Measurements
inferred← citeshttps://doi.org/10.1007/978-94-011-0683-2_248openalex-snapshot
Conformational differences between the cis and trans proline isomers of a synthetic antigen from the pilus of Pseudomonas aeruginosa
inferred← citeshttps://doi.org/10.1007/bf00179349openalex-snapshot
Effect of disulfide bridge formation on the NMR spectrum of a protein: Studies on oxidized and reduced Escherichia coli thioredoxin
inferred← citeshttps://doi.org/10.1007/bf00350396openalex-snapshot
Chaperone and foldase coexpression in the baculovirus-insect cell expression system
inferred← citeshttps://doi.org/10.1007/bf01901697openalex-snapshot
Folding pathway of guanidine-denatured disulfide-intact wild-type and mutant bovine pancreatic ribonuclease A
inferred← citeshttps://doi.org/10.1007/bf02443459openalex-snapshot
Conformational investigation of a novel dipeptide based molecular scaffold
inferred← citeshttps://doi.org/10.1007/s00018-009-0014-6openalex-snapshot
Functional aspects of protein flexibility
inferred← citeshttps://doi.org/10.1007/s00018-022-04179-4openalex-snapshot
Impact of distant peptide substrate residues on enzymatic activity of SlyD
inferred← citeshttps://doi.org/10.1007/s00249-006-0121-3openalex-snapshot
A molecular dynamics study of Cyclophilin A free and in complex with the Ala-Pro dipeptide
inferred← citeshttps://doi.org/10.1007/s00726-011-0921-3openalex-snapshot
A straightforward route to enantiopure 2-substituted-3,4-dehydro-β-proline via ring closing metathesis
inferred← citeshttps://doi.org/10.1007/s00726-011-1211-9openalex-snapshot
Cis–trans peptide variations in structurally similar proteins
inferred← citeshttps://doi.org/10.1007/s00792-009-0233-7openalex-snapshot
The contribution of proline residues to protein stability is associated with isomerization equilibrium in both unfolded and folded states
inferred← citeshttps://doi.org/10.1007/s10337-012-2311-8openalex-snapshot
Kinetic Study on the Isomerization of Perindopril by HPLC
inferred← citeshttps://doi.org/10.1007/s10858-011-9538-9openalex-snapshot
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis
inferred← citeshttps://doi.org/10.1007/s10930-005-7589-zopenalex-snapshot
Botulinum Neurotoxin Types A, B, and E: Fragmentations by Autoproteolysis and Other Mechanisms Including by O-Phenanthroline–Dithiothreitol, and Association of the Dinucleotides NAD+/NADH with the Heavy Chain of the Three Neurotoxins
inferred← citeshttps://doi.org/10.1007/s11030-012-9399-5openalex-snapshot
Synthesis, pharmacological evaluation and conformational investigation of endomorphin-2 hybrid analogues
inferred← citeshttps://doi.org/10.1007/s11103-026-01735-5openalex-snapshot
Use of translational fusions to express functional Klebsiella oxytoca dinitrogenase reductase in plant mitochondria
inferred← citeshttps://doi.org/10.1007/s11248-026-00504-wopenalex-snapshot
Ectopic expression of a Penicillium oxalicum cyclophilin gene in Arabidopsis thaliana imparts tolerance to cold stress
inferred← citeshttps://doi.org/10.1007/s12192-017-0791-zopenalex-snapshot
Proline isomerization in the C-terminal region of HSP27
inferred← citeshttps://doi.org/10.1007/s12551-015-0171-9openalex-snapshot
Investigating dynamic interdomain allostery in Pin1
inferred← citeshttps://doi.org/10.1007/s13361-016-1418-9openalex-snapshot
Statistical Examination of the a and a + 1 Fragment Ions from 193 nm Ultraviolet Photodissociation Reveals Local Hydrogen Bonding Interactions
inferred← citeshttps://doi.org/10.1016/0003-2670(95)00006-lopenalex-snapshot
Nuclear magnetic resonance spectroscopic analysis of the selective complexation of the cis and trans isomers of phenylalanylproline by β-cyclodextrin
inferred← citeshttps://doi.org/10.1016/0014-5793(90)80697-hopenalex-snapshot
Peptidyl‐prolyl cis‐trans isomerase does not affect the Pro‐43 cis‐trans isomerization rate in folded calbindin D9k
inferred← citeshttps://doi.org/10.1016/0014-5793(95)00982-fopenalex-snapshot
Novel disulfide‐constrained pentapeptides as models for β‐VIa turns in proteins
inferred← citeshttps://doi.org/10.1016/0014-5793(95)01042-dopenalex-snapshot
A model for transmembrane helix with a cis‐Proline in the middle
inferred← citeshttps://doi.org/10.1016/0021-9673(92)85124-copenalex-snapshot
High-performance liquid chromatographic separation of cis-trans isomers of proline-containing peptides
inferred← citeshttps://doi.org/10.1016/0021-9673(94)85172-7openalex-snapshot
High-performance liquid chromatographic separation of cis—trans isomers of proline-containing peptides
inferred← citeshttps://doi.org/10.1016/0021-9673(95)01059-9openalex-snapshot
Isolation and identification of peptide conformers by reversed-phase high-performance liquid chromatography and NMR at low temperature
inferred← citeshttps://doi.org/10.1016/0021-9673(96)00241-5openalex-snapshot
Kinetic study on the cis-trans isomerization of peptidyl-proline dipeptides
inferred← citeshttps://doi.org/10.1016/0022-2364(92)90376-iopenalex-snapshot
Analysis of inversion-magnetization-transfer experiments
inferred← citeshttps://doi.org/10.1016/0022-2836(86)90265-2openalex-snapshot
Folding mechanism of porcine ribonuclease
inferred← citeshttps://doi.org/10.1016/0022-2836(88)90446-9openalex-snapshot
Folding of immunogenic peptide fragments of proteins in water solution
inferred← citeshttps://doi.org/10.1016/0022-2836(91)90721-hopenalex-snapshot
Influence of proline residues on protein conformation
inferred← citeshttps://doi.org/10.1016/0022-2836(92)90822-2openalex-snapshot
A peptide model for proline isomerism in the unfolded state of staphylococcal nuclease
inferred← citeshttps://doi.org/10.1016/0022-2836(92)90841-7openalex-snapshot
Similarities and differences between human cyclophilin A and other β-barrel structures
inferred← citeshttps://doi.org/10.1016/0022-2836(92)90976-qopenalex-snapshot
Proline cis-trans isomers in calbindin D9k observed by X-ray crystallography
inferred← citeshttps://doi.org/10.1016/0022-2836(94)90044-2openalex-snapshot
Stabilization of a type VI turn in a family of linear peptides in water solution
inferred← citeshttps://doi.org/10.1016/0040-4039(94)02244-6openalex-snapshot
A short synthesis of bicyclic dipeptides corresponding to Xxx-L-Pro and Xxx-D-Pro having constrained cis-proline amides
inferred← citeshttps://doi.org/10.1016/0040-4039(95)00673-zopenalex-snapshot
Conformational analysis of a triproline-derived helical template and its peptide conjugates
inferred← citeshttps://doi.org/10.1016/0040-4039(95)00706-iopenalex-snapshot
Synthesis and analysis of a macrocyclic triproline-derived template containing a local conformational constraint
inferred← citeshttps://doi.org/10.1016/0040-4039(95)00707-jopenalex-snapshot
Efficient helix nucleation by a macrocyclic triproline-derived template
inferred← citeshttps://doi.org/10.1016/0040-4039(95)00776-9openalex-snapshot
A short β-sheet containing proline nucleated by a 2,2′-substituted tolan β-turn mimetic
inferred← citeshttps://doi.org/10.1016/0076-6879(86)31037-1openalex-snapshot
[6]Proline isomerization studied with proteolytic enzymes
inferred← citeshttps://doi.org/10.1016/0076-6879(94)44016-6openalex-snapshot
[14] Prolyl oligopeptidases
inferred← citeshttps://doi.org/10.1016/0079-6107(87)90011-3openalex-snapshot
Folding and association of proteins
inferred← citeshttps://doi.org/10.1016/0167-4838(84)90285-1openalex-snapshot
Conformational specificity of chymotrypsin toward proline-containing substrates
inferred← citeshttps://doi.org/10.1016/0167-4838(87)90328-1openalex-snapshot
Proline isomerization and the slow folding reactions of the α subunit of tryptophan synthase from Escherichia coli
inferred← citeshttps://doi.org/10.1016/0167-4838(90)90117-xopenalex-snapshot
Cis-trans isomerization of an angiotensin I-converting enzyme inhibitor. An enzyme kinetic and nuclear magnetic resonance study
inferred← citeshttps://doi.org/10.1016/0167-4838(95)00238-3openalex-snapshot
Substrates containing phosphorylated residues adjacent to proline decrease the cleavage by proline-specific peptidases
inferred← citeshttps://doi.org/10.1016/j.abb.2015.03.021openalex-snapshot
The cis conformation of proline leads to weaker binding of a p53 peptide to MDM2 compared to trans
inferred← citeshttps://doi.org/10.1016/j.bbagen.2014.12.019openalex-snapshot
Control of protein function by prolyl isomerization
inferred← citeshttps://doi.org/10.1016/j.bbamem.2022.184075openalex-snapshot
Cell-Free Synthesis and Reconstitution of Bax in Nanodiscs: Comparison between Wild-Type Bax and a Constitutively Active Mutant
inferred← citeshttps://doi.org/10.1016/j.bbapap.2012.02.002openalex-snapshot
HIV-1 p6—Another viral interaction partner to the host cellular protein cyclophilin A
inferred← citeshttps://doi.org/10.1016/j.bioorg.2011.11.001openalex-snapshot
Cooperativity in monomeric enzymes with single ligand-binding sites
inferred← citeshttps://doi.org/10.1016/j.bmc.2007.02.050openalex-snapshot
Conformational analysis of endomorphin-2 analogs with phenylalanine mimics by NMR and molecular modeling
inferred← citeshttps://doi.org/10.1016/j.bpj.2012.11.3815openalex-snapshot
Conformational Plasticity of an Enzyme during Catalysis: Intricate Coupling between Cyclophilin A Dynamics and Substrate Turnover
inferred← citeshttps://doi.org/10.1016/j.bpj.2021.10.040openalex-snapshot
The trans-to-cis proline isomerization in E. coli Trx folding is accelerated by trans prolines
inferred← citeshttps://doi.org/10.1016/j.bpj.2023.08.012openalex-snapshot
Replacement of the native cis prolines by alanine leads to simplification of the complex folding mechanism of a small globular protein
inferred← citeshttps://doi.org/10.1016/j.bpj.2024.09.028openalex-snapshot
An integrative characterization of proline cis and trans conformers in a disordered peptide
inferred← citeshttps://doi.org/10.1016/j.bpj.2026.04.013openalex-snapshot
Fast folding of anthrax lethal factor N-terminal domain independent of proline isomerization
inferred← citeshttps://doi.org/10.1016/j.cell.2022.07.019openalex-snapshot
Accurate de novo design of membrane-traversing macrocycles
inferred← citeshttps://doi.org/10.1016/j.chroma.2007.04.027openalex-snapshot
Counter-current chromatographic estimation of hydrophobicity of Z-(cis) and E-(trans) enalapril and kinetics of cis/trans isomerization
inferred← citeshttps://doi.org/10.1016/j.chroma.2007.04.031openalex-snapshot
High-performance liquid chromatography and nuclear magnetic resonance study of linear tetrapeptides and octapeptides containing N-methylated amino acid residues
inferred← citeshttps://doi.org/10.1016/j.febslet.2006.08.024openalex-snapshot
Correlation of folding kinetics with the number and isomerization states of prolines in three homologous proteins of the RNase family
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.128304openalex-snapshot
Isomerization of proline-46 in the N-terminal tail of galectin-3 enhances T cell apoptosis via the ROS-ERK pathway
inferred← citeshttps://doi.org/10.1016/j.imlet.2014.11.002openalex-snapshot
Insights into peptidyl-prolyl cis–trans isomerase structure and function in immunocytes
inferred← citeshttps://doi.org/10.1016/j.jbi.2008.05.006openalex-snapshot
Prediction of cis/trans isomerization using feature selection and support vector machines
inferred← citeshttps://doi.org/10.1016/j.jmb.2004.04.021openalex-snapshot
Catalysis of Proline-directed Protein Phosphorylation by Peptidyl-prolyl cis/trans Isomerases
inferred← citeshttps://doi.org/10.1016/j.jmb.2005.02.050openalex-snapshot
Nuclear Magnetic Resonance Characterization of the Refolding Intermediate of β2-Microglobulin Trapped by Non-native Prolyl Peptide Bond
inferred← citeshttps://doi.org/10.1016/j.jmb.2006.04.032openalex-snapshot
Probing Nature’s Knots: The Folding Pathway of a Knotted Homodimeric Protein
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.02.010openalex-snapshot
Energetic Coupling Between Native-State Prolyl Isomerization and Conformational Protein Folding
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.06.001openalex-snapshot
The Influence of Proline Isomerization and Off-Pathway Intermediates on the Folding Mechanism of Eukaryotic UMP/CMP Kinase
inferred← citeshttps://doi.org/10.1016/j.jmb.2009.02.021openalex-snapshot
Molecular Determinants of a Native-State Prolyl Isomerization
inferred← citeshttps://doi.org/10.1016/j.jmb.2009.05.080openalex-snapshot
Solution Characterization of the Extracellular Region of CD147 and Its Interaction with Its Enzyme Ligand Cyclophilin A
inferred← citeshttps://doi.org/10.1016/j.jmb.2012.11.004openalex-snapshot
Native-State Heterogeneity of β2-Microglobulin as Revealed by Kinetic Folding and Real-Time NMR Experiments
inferred← citeshttps://doi.org/10.1016/j.jmb.2014.11.021openalex-snapshot
Flexible Stoichiometry and Asymmetry of the PIDDosome Core Complex by Heteronuclear NMR Spectroscopy and Mass Spectrometry
inferred← citeshttps://doi.org/10.1016/j.jmb.2015.01.023openalex-snapshot
Prolyl Isomerization and Its Catalysis in Protein Folding and Protein Function
inferred← citeshttps://doi.org/10.1016/j.jmb.2015.11.023openalex-snapshot
Proline Conformation in a Functional Tau Fragment
inferred← citeshttps://doi.org/10.1016/j.jmb.2017.03.017openalex-snapshot
Broad Analysis of Vicinal Disulfides: Occurrences, Conformations with Cis or with Trans Peptides, and Functional Roles Including Sugar Binding
inferred← citeshttps://doi.org/10.1016/j.jmb.2021.167108openalex-snapshot
The Inherent Dynamics and Interaction Sites of the SARS-CoV-2 Nucleocapsid N-Terminal Region
inferred← citeshttps://doi.org/10.1016/j.jmb.2024.168587openalex-snapshot
Proline Peptide Bond Isomerization in Ubiquitin Under Folding and Denaturing Conditions by Pressure-Jump NMR
inferred← citeshttps://doi.org/10.1016/j.jmro.2022.100074openalex-snapshot
The LEF-1 high-mobility group box adopts residual structure in its DNA-free form
inferred← citeshttps://doi.org/10.1016/j.molcel.2005.12.017openalex-snapshot
Allosteric Regulation of Hsp70 Chaperones by a Proline Switch
inferred← citeshttps://doi.org/10.1016/j.molcel.2006.07.027openalex-snapshot
Structure and Mechanism of the Phosphotyrosyl Phosphatase Activator
inferred← citeshttps://doi.org/10.1016/j.molcel.2007.02.005openalex-snapshot
Prolyl cis-trans Isomerization as a Molecular Timer in Crk Signaling
inferred← citeshttps://doi.org/10.1016/j.molcel.2017.04.011openalex-snapshot
A Slow Conformational Switch in the BMAL1 Transactivation Domain Modulates Circadian Rhythms
inferred← citeshttps://doi.org/10.1016/j.str.2017.11.003openalex-snapshot
Multivalent Interactions with Fbw7 and Pin1 Facilitate Recognition of c-Jun by the SCFFbw7 Ubiquitin Ligase
inferred← citeshttps://doi.org/10.1016/j.str.2025.08.003openalex-snapshot
Light-induced conformational switching and magnetic sensitivity of Drosophila cryptochrome
inferred← citeshttps://doi.org/10.1016/j.tet.2006.04.021openalex-snapshot
The Ugi reaction with 2-substituted cyclic imines. Synthesis of substituted proline and homoproline derivatives
inferred← citeshttps://doi.org/10.1016/j.tet.2006.09.009openalex-snapshot
Effects of steric bulk and stereochemistry on the rates of diketopiperazine formation from N-aminoacyl-2,2-dimethylthiazolidine-4-carboxamides (Dmt dipeptide amides)—a model for a new prodrug linker system
inferred← citeshttps://doi.org/10.1016/s0003-2697(03)00437-8openalex-snapshot
Analysis of the isomeric composition of the proline peptide bond in an angiotensin-converting enzyme inhibitor using capillary electrophoresis
inferred← citeshttps://doi.org/10.1016/s0006-3495(99)77298-xopenalex-snapshot
The Role of Proline and Glycine in Determining the Backbone Flexibility of a Channel-Forming Peptide
inferred← citeshttps://doi.org/10.1016/s0009-2614(99)00969-0openalex-snapshot
The multicanonical weighted histogram analysis method for the free-energy landscape along structural transition paths
inferred← citeshttps://doi.org/10.1016/s0014-5793(97)00730-8openalex-snapshot
Remarkably slow folding of a small protein
inferred← citeshttps://doi.org/10.1016/s0014-5793(97)01350-1openalex-snapshot
The rate‐limiting steps for the folding of an antibody scFv fragment
inferred← citeshttps://doi.org/10.1016/s0021-9258(19)74014-9openalex-snapshot
NMR constrained solution structures for laminin peptide 11. Analogs define structural requirements for inhibition of tumor cell invasion of basement membrane matrix.
inferred← citeshttps://doi.org/10.1016/s0021-9673(00)91064-1openalex-snapshot
Low temperature high-performance liquid chromatography of cis—trans proline dipeptides
inferred← citeshttps://doi.org/10.1016/s0022-2836(02)00036-0openalex-snapshot
Structural dynamics of the membrane translocation domain of colicin E9 and its interaction with TolB
inferred← citeshttps://doi.org/10.1016/s0022-2836(02)00922-1openalex-snapshot
Parallel Channels and Rate-limiting Steps in Complex Protein Folding Reactions: Prolyl Isomerization and the Alpha Subunit of Trp Synthase, a TIM Barrel Protein
inferred← citeshttps://doi.org/10.1016/s0022-2836(02)01444-4openalex-snapshot
The Coordination of the Isomerization of a Conserved Non-prolyl cis Peptide Bond with the Rate-limiting Steps in the Folding of Dihydrofolate Reductase
inferred← citeshttps://doi.org/10.1016/s0022-2836(03)00723-xopenalex-snapshot
Proline Replacements and the Simplification of the Complex, Parallel Channel Folding Mechanism for the Alpha Subunit of Trp Synthase, a TIM Barrel Protein
inferred← citeshttps://doi.org/10.1016/s0022-2836(83)80067-9openalex-snapshot
Folding of homologous proteins
inferred← citeshttps://doi.org/10.1016/s0022-2836(95)80039-5openalex-snapshot
Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding
inferred← citeshttps://doi.org/10.1016/s0040-4039(00)75983-1openalex-snapshot
Design and synthesis of a cis-gly-pro, type-VI turn, dipeptide mimetic and its use in fmoc-solid phase peptide synthesis
inferred← citeshttps://doi.org/10.1016/s0040-4039(00)93377-xopenalex-snapshot
Thermodynamic origin of prolyl peptide bond isomers
inferred← citeshttps://doi.org/10.1016/s0065-2725(08)60161-0openalex-snapshot
The Conformations of Acyl Groups in Heterocyclic Compounds
inferred← citeshttps://doi.org/10.1016/s0065-3233(00)53007-1openalex-snapshot
Folding and association of oligomeric and multimeric proteins
inferred← citeshttps://doi.org/10.1016/s0065-3233(08)60562-8openalex-snapshot
Mechanism of Enzymatic and Nonenzymatic Prolyl Cis-Trans Isomerization
inferred← citeshttps://doi.org/10.1016/s0065-3233(08)60563-xopenalex-snapshot
Prolyl Isomerases: Role in Protein Folding
inferred← citeshttps://doi.org/10.1016/s0066-4103(08)60225-2openalex-snapshot
NMR Studies of Amino Acids, Peptides, and Proteins: A Brief Review, 1980-1982
inferred← citeshttps://doi.org/10.1016/s0079-6107(01)00005-0openalex-snapshot
The interrelationships of side-chain and main-chain conformations in proteins
inferred← citeshttps://doi.org/10.1016/s0166-1280(00)00372-9openalex-snapshot
Peptide models XXIX. cis–trans Isomerism of peptide bonds: ab initio study on small peptide model compound; the 3D-Ramachandran map of formylglycinamide
inferred← citeshttps://doi.org/10.1016/s0969-2126(00)00045-9openalex-snapshot
Structure of restriction endonuclease BamHI phased at 1.95 å resolution by MAD analysis
inferred← citeshttps://doi.org/10.1016/s1074-5521(97)90254-4openalex-snapshot
Consensus chemistry and R-turn conformation of the active core of the insect kinin neuropeptide family
inferred← citeshttps://doi.org/10.1016/s1359-0278(97)00004-7openalex-snapshot
Dynamics of a type VI reverse turn in a linear peptide in aqueous solution
inferred← citeshttps://doi.org/10.1016/s1359-0278(98)00007-8openalex-snapshot
Parallel pathways in the folding of a short-term denatured scFv fragment of an antibody
inferred← citeshttps://doi.org/10.1016/s1380-7323(99)80054-5openalex-snapshot
Ways and Means to Enhance the Configurational Sampling of Small Peptides in Aqueous Solution in Molecular Dynamics Simulations
inferred← citeshttps://doi.org/10.1016/s1874-5989(99)80007-6openalex-snapshot
Chapter 5 Protein folding
inferred← citeshttps://doi.org/10.1017/s0022029900031150openalex-snapshot
Restrained molecular dynamics study of the interaction between bovine κ-casein peptide 98–111 and bovine chymosin and porcine pepsin
inferred← citeshttps://doi.org/10.1021/ac00115a015openalex-snapshot
Resolution of cis and trans isomers of peptides containing proline using capillary zone electrophoresis
inferred← citeshttps://doi.org/10.1021/ac011083kopenalex-snapshot
Cis−Trans Signatures of Proline-Containing Tryptic Peptides in the Gas Phase
inferred← citeshttps://doi.org/10.1021/ac052040xopenalex-snapshot
Isothermal Calorimetry as a Tool To Investigate Slow Conformational Changes in Proteins and Peptides
inferred← citeshttps://doi.org/10.1021/acs.analchem.5b02488openalex-snapshot
Determination of the cis–trans Isomerization Barriers of l -Alanyl- l -proline in Aqueous Solutions and at Water/Hydrophobic Interfaces by On-Line Temperature-Jump Relaxation HPLC and Dynamic On-Column Reaction HPLC
inferred← citeshttps://doi.org/10.1021/acs.biochem.5c00514openalex-snapshot
A Data Set of Simple 1-D and 2-D NMR Spectra of Peptides, including All Encoded Amino Acids, for Introductory Instruction in Protein Biomolecular NMR Spectroscopy
inferred← citeshttps://doi.org/10.1021/acs.biochem.6b00726openalex-snapshot
Homodimeric Escherichia coli Toxin CcdB (Controller of Cell Division or Death B Protein) Folds via Parallel Pathways
inferred← citeshttps://doi.org/10.1021/acs.biochem.7b00579openalex-snapshot
Incomplete Refolding of Antibody Light Chains to Non-Native, Protease-Sensitive Conformations Leads to Aggregation: A Mechanism of Amyloidogenesis in Patients?
inferred← citeshttps://doi.org/10.1021/acs.jcim.1c00771openalex-snapshot
Cyclosporin A: Conformational Complexity and Chameleonicity
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