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1
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84909878970
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Papers of particular, published within the annual period of review, have been highlighted as: of special interest of outstanding interest
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3
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0007760726
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The S-Peptide S-Protein System: a Model for Hormone-Receptor Interaction
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Acc Chem Res
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Finn1
Hofmann2
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4
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0026582848
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Heat Capacity Changes for Protein-Peptide Interactions in the Ribonuclease S System
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A calorimetric investigation of the contribution of the side chains of S-peptide to binding, which provides insight into specific side-chain recognition.
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(1992)
Biochemistry
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Varadarajan1
Connelly2
Sturtevant3
Richards4
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6
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0000447708
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Conformational Analysis of Enkephalin and Conformational Activity Relationship
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S. Underfriend, J. Meienhofer, Academic Press Incorporated, New York
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The Peptides
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Schiller1
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12
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0026766974
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Constrained Peptides: Models of Bioactive Peptides and Protein Substructures
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Review of the use of covalent constraints in determining the receptor-bound conformation of peptides.
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(1992)
Annu Rev Biochem
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, pp. 387-418
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Rizo1
Gierasch2
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14
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0025997018
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Medicinal Chemistry in the Golden Age of Biology: Lessons from Steroid and Peptide Research
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(1991)
Angew Chem
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Hirschmann1
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25
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85023284562
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Peptidomimetics Derived from Natural Products
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in press, A review of natural products that have been isolated on the basis of their ability to bind to peptide receptors.
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(1992)
Med Res Rev
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Wiley1
Rich2
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27
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84909851982
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3D-QSAR of Angiotensin-converting Enzyme and Thermolysin Inhibitors: a Comparison of CoMFA Models Based on Deduced and Experimentally Determined, Active Site Geometries
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in press, The authors compare a predictive model of binding affinity for a receptor of unknown structure with one derived from the crystal structure of thermolysin-inhibitor complexes showing comparable predictive abilities.
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(1992)
J Am Chem Soc
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DePriest1
Mayer2
Naylor3
Marshall4
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28
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0025778840
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Atomic Structure of Acetylcholinesterase from Torpedo california: a Proteolytic Acetylcholine-binding Protein
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This paper reports a crystal structure of one of the most efficient enzymes, and confirms the absence of an anionic site for choline recognition.
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Science
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Sussman1
Harel2
Frollow3
Oefner4
Goldman5
Toker6
Silman7
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30
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0024561064
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Determination of the Conformation of Molecular Complexes of Aricidin Aglycon with Ac2-l-Lys-d-Ala-d-Ala and A Ac-y-Gin-l-Lys(Ac)-d-Ala-d-Ala: an Application of Nuclear Magnetic Resonance Spectroscopy and Distance Geometry in the Modeling Peptides
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J Am Chem Soc
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Mueller1
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31
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Aspects of Molecular Recognition: Solvent Exclusion and Dimerization of the Antibiotic Ristocetin when Bound to a Model Bacterial Cell-wall Precursor
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J Am Chem Soc
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Waltho1
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33
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0026030568
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Chemistry and Biology of the Immunophilins and their Immunosuppressive Ligands
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A review of rapid development in understanding the chemistry and biology of cyclosporin, FK506 and rapamycin.
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Science
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Schreiber1
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34
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0026315509
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Receptor-induced Conformation Change of the Immunosuppressant Cyclosporin
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NMR studies indicate conformational changes in cyclosporin from crystal structure or NMR solution structure of isolated cyclosporin on binding to cyclophilin.
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(1991)
Science
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Wüthrich1
Freyberg2
Weber3
Wider4
Traber5
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35
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0026686692
-
A Model of the Cyclophilin/Cyclosporin A (CsA) Complex from NMR and X-ray Data Suggests that CsA Binds as a Transition-state Analogue
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NMR studies indicate conformational changes in cyclosporin from crystal structure or NMR solution structure of isolated cyclosporin on binding to cyclophilin.
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(1992)
J Am Chem Soc
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Fesik1
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36
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0025835156
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The NMR Structure of Cyclosporin A Bound to Cyclophilin in Aqueous Solution
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NMR studies indicate conformational changes in cyclosporin from crystal structure or NMR solution structure of isolated cyclosporin on binding to cyclophilin.
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(1991)
Biochemistry
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Weber1
Weber2
Freyberg3
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37
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0026538405
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Cyclosporin-A-Cyclophilin Complex Formation — a Model Based on X-ray and NMR Data
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This paper describes a model of cyclosporin and cyclophilin derived from a combination of NMR data on cyclosporin bound to cyclophilin and the crystal structure of isolated cyclophilin.
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FEBS Lett
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Spitzfaden1
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38
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0026637286
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Novel Backbone Conformation of Cyclosporin A: the Complex with Lithium Chloride
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A lithium complex of cyclosporin is shown to have all trans amide bonds in a conformation similar to that seen when cyclosporin binds to cyclophilin.
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(1992)
J Am Chem Soc
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Kock1
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Seebach3
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39
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0026651050
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Lithium Chloride Perturbation of cis-trans Peptide Bond Equilibria Effect of Conformational Equilibria in Cyclosporin A and on Time-dependent Inhibition of Cyclophilin
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The formation of a lithium complex of cyclosporin eliminates the time-lag for expression of inhibition of peptidyl prolyl isomerase activity, suggesting that the trans conformer is recognized specifically by the enzyme.
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(1992)
Journal of the American Chemical Society
, vol.114
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Kofran1
Kuzmic2
Kishore3
Gemmecker4
Fesik5
Rich6
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42
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0026532051
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A Conformation of Cyclosporin A in Aqueous Environment Revealed by the X-ray Structure of a Cyclosporin-Fab Complex
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The conformation of cyclosporin in an antibody complex is similar to that seen when complexed with lithium or with cyclophilin, and is different from the conformation of cyclosporin in crystal structure or in organic solvents.
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(1992)
Science
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Altschuh1
Vix2
Rees3
Thierry4
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43
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0026587998
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Structural Evidence for Induced Fit as a Mechanism for Antibody-Antigen Recognition
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Changes in the conformations of loops as well as in side-chain orientations argue for induced fit as a means of antibodies accomodating chemical structures never seen previously.
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(1992)
Science
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Rini1
Schulze Gahmen2
Wilson3
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47
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0026757989
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Three-dimensional Structure of an Angiotensin II-Fab Complex at 3 Å: Hormone Recognition by an Anti-idiotypic Antibody
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A turn motif for recognition of the antibody complex of the peptide hormone AII is identified. As the antibody is an anti-anti-idiotope and shows some specificity similarities with AII receptor, its recognition site may mimic the hormone's biological receptor.
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(1992)
Science
, vol.257
, pp. 502-507
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Garcia1
Ronco2
Veroust3
Brünger4
Amzel5
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49
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0026705594
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Recognition of Angiotensin II: Antibodies at Different Levels of an Idiotypic Network Are Superimposable
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Sequence similarities in antibodies that recognize angiotensin II argue for anti-idiotope fidelity.
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(1992)
Science
, vol.257
, pp. 528-531
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Garcia1
Desiderio2
Ronco3
Veroust4
Amzel5
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55
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0026794581
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The Three-dimensional Structure of HLA-B27 at 21 Å Resolution suggests a General Mechanism for Tight Peptide Binding to MHC
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in press, The high resolution structure reveals a possible general motif for class I MHC binding proteins.
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(1992)
Cell
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Madden1
Gorga2
Strominger3
Wiley4
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56
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0001581895
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Peptide Binding to the Major Histocompatibility Molecules
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A recent review of the structural basis for MHC recognition of peptides.
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Curr Opin Struct Biol
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Madden1
Wiley2
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63
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0026042333
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Sequence Analysis of Peptides Bound to MHC Class II Molecules
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The elution and structural determination of peptides associated with MHC class II molecules indicate a marked heterogeneity in length, ranging from 13 to 17 residues, in contrast to the length of eight to nine residues seen for class I associated peptides.
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(1991)
Nature
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Rudensky1
Preston-Hurlburt2
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Janeway5
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64
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0025939201
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Self and Foreign Peptides Interact with Intact and Disassembled MHC Class II Antigen HLA-DR Via Tryptophan Pockets
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A study of the changes in the intrinsic tryptophan fluorescence of complexes of an MHC class iI system indicates that two tryptophan residues of the MHC protein are involved in complex formation.
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(1991)
Biochemistry
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, pp. 9177-9187
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Kropshofer1
Bohlinger2
Max3
Kalbacher4
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65
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0024571818
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Human Leukocyte and Porcine Pancreatic Elastase. X-ray Crystal Structures, Mechanisms, Substrate Specificity, and Mechanism-based Inhibitors
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Biochemistry
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Bode1
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69
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0026344399
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The Three-dimensional Structure of the Aspartyl Protease from the HIV-1 Isolate BRU
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The crystal structure of HIV-1 protease derived from refolded, recombinant protein expressed in E. coli shows essentially the same three-dimensional structure as that from chemically synthesized material, even though it differs by several amino acid replacements.
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(1991)
Biochimie
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Spinelli1
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71
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Structure and Function of Retroviral Proteases
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A review of retroviral proteases, a subclass of aspartate proteinases, with the emphasis placed on HIV protease.
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(1991)
Annu Rev Biophys Chem
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, pp. 299-320
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Fitzgerald1
Springer2
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72
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0026345896
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A Cumulative Specificity Model for Proteases from Human Immunodeficiency Virus Types 1 and 2, Inferred from Statistical Analysis of an Extended Substrate Database
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An investigation of the substrate specificity of the HIV-1 protease utilizing 40 protein substrates suggests highest stringency at the P1, P2 and P2′ positions of the substrate.
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J Biol Chem
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Poorman1
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73
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0026316549
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Analysis of Retroviral Protease Cleavage Sites Reveals Two Types of Cleavage Sites and the Structural Requirements of the P1 Amino Acid
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A study of the known retroviral protease cleavage sites from 10 different retroviruses allows grouping into two classes on the basis of the sequence composition flanking the scissile bond.
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J Biol Chem
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Pettit1
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74
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0026044822
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Analysis of the Subsite Preferences of HIV-1 Proteinase Using MA/CA Junction Peptides Substituted at the P3-P1′ Positions
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Residues P3, P2, P1 and P1′ are systematically varied in a synthetic heptapeptide substrate of HIV-1 proteinase. Only peptides containing Phe, Trp, Leu or Met at P1 are cleaved.
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(1991)
Arch Biochem Biophys
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Billich1
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76
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0026520387
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Converting Trypsin to Chymotrypsin: the Role of Surface Loops
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An intriguing report in which loops distant from the active site are found to affect catalysis and the recognition of peptidase (but not esterase) substrates.
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Science
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Hedstrom1
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79
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0026317997
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Novel Binding Mode of Highly Potent HIV-proteinase Inhibitors Incorporating the (R)-Hydroxyethylamine Isostere
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The crystal structure of Roche inhibitor complexed to the HIV protease confirms a model to explain a switch in chiral preference for the transition-state hydroxyl group.
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J Med Chem
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Krohn1
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82
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Another example of HIV protease complexed with a novel inhibitor showing conservation of protease structure.
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J Am Chem Soc
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Bone1
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85
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0026730489
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Structure-based Strategies for Drug Design and Discovery
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A review of approaches to the design of novel inhibitors, illustrated by work on the HIV protease.
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Science
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Kuntz1
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86
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0025774665
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Effect of Hydroxyl Group Configuration in Hydroxethylamine Dipeptide Isosteres on HIV Protease Inhibitors. Evidence for Multiple Binding Modes
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Molecular modeling of the Roche inhibitor offers an explanation for the preference of this compound for a transition-state hydroxyl with a chirality opposite to that of other substrate-based inhibitors.
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J Med Chem
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Rich1
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87
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0026326821
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Structure of a Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-dependent Protein Kinase
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The three dimensional structure of a 20-residue peptide bound to cAMP-dependent protein kinase exhibits a mixed helix-extended chain motif.
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Science
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Knighton1
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88
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0026048737
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Investigation of an Octapeptide Inhibitor of Escherichia coli Ribonucleotide Reductase by Transferred Nuclear Overhauser Effect Spectroscopy
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NMR studies indicate a turn recognition motif for an octapeptide inhibitor which presumably prevents association of the enzyme's sub-units.
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Biochemistry
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Bushweiler1
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89
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The Three-dimensional Structure of Class P Glutathione S-transferase in Complex with Glutathione Sulfonate at 2.3 Å Resolution
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A glutathione analog binds to the enzyme's active site in an extended conformation.
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90
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0025786742
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Three-dimensional Structure of Echistatin, the Smallest Active RGD Protein
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The crystal structure of a small protein with an RGD sequence, the laminin-class receptor message, finds RDG message in a flexible loop.
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Reevaluating Equilibrium and Kinetic Binding Parameters for Lipophilic Drugs Based on a Structural Model for Drug Interaction with Biological Membranes
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A review of the role of biological membranes in affecting the conformation and distribution of drugs.
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Peptide-Membrane Interactions and a New Principle in Quantitative Structure-Activity Relationships
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Schwyzer1
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95
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Molecular Design of Transmembrane Ion Channels
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A review of the structure of the peptide antibiotic gramicidin and efforts to prove current models of its mechanism of action when complexed with membrane.
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Chemtracts Org Chem
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96
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Conformational Studies by Circular Dichroism, H-1-NMR, and Computer Simulations of Bombolitin-I and Bombolitin-III in Aqueous Solution Containing Surfactant Micelles
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Transferred Nuclear Overhauser Effect Analyses of Membrane-bound Enkephalin Analogues by 1H Nuclear Magnetic Resonance: Correlation between Activities and Membrane-bound Conformations
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Different Conformations for the Same Polypeptide Bound to Chaperones DnaK and GroEL
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Biochemistry
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Landry1
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100
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0026595140
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Different Conformations for the Same Polypeptide Bound to Chaperones DnaK and GroEL
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Transferred NOE experiments show that same peptide sequence binds to two different chaperon proteins with totally different recognition motifs (helical versus extended).
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Landry1
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101
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Solution Structure of a Calmodulin-Target Peptide Complex by Multidimensional NMR
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2+-binding domains of calmodulin by causing a deformation in its long helix.
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Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex
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Crystal structure of calmodulin-peptide complex giving details of helix deformation.
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Meador1
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103
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0025913120
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Deciphering the Structural Elements of Hirudin C-terminal Peptide that Bind to the Fibrinogen Recognition Site of α-Thrombin
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Conformation of Recombinant Desulfatohirudin in Aqueous Solution Determined by Nuclear Magnetic Resonance
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Conformational Stability of a Thrombin-binding Peptide Derived from the C-terminus
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10 helical turn, shows a predisposition to helical structure in solution.
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0026657151
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The Structure of Residues 7–16 of the Aα-Chain of Human Fibrinogen Bound to Bovine Thrombin at 2.3 Å Resolution
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A segment of fibrinogen bound to thrombin shows a turn conformation previously predicted by NMR, but with a different conformation.
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High-resolution NMR of Fibrinogen-like Peptides in Solution: Structure of a Thrombin-bound Peptide Corresponding to Residues 7–16 of the Aα-Chain of Human Fibrinogen
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The Refined 1.9 Å X-ray Crystal Structure of d-Phe-Pro-Arg-Chloromethylketone-inhibited Human α-Thrombin: Structural Analysis, Overall Structure, Electrostatic Properties, Detailed Active-site Geometry and Structure-Function Relationships
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A definitive analysis of the high-resolution structure of thrombin with a bound peptide inhibitor.
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Major Enhancement of the Affinity of an Enzyme for a Transition-state Analog by a Single Hydroxyl Group
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