A fluorine scan of non-peptidic inhibitors of neprilysin: Fluorophobic and fluorophilic regions in an enzyme active site

[1]  G. Klebe,et al.  Potent inhibitors of tRNA-guanine transglycosylase, an enzyme linked to the pathogenicity of the Shigella bacterium: charge-assisted hydrogen bonding. , 2007, Angewandte Chemie.

[2]  F. Diederich,et al.  Fluorine in Pharmaceuticals: Looking Beyond Intuition , 2007, Science.

[3]  Manfred Kansy,et al.  Predicting and Tuning Physicochemical Properties in Lead Optimization: Amine Basicities , 2007, ChemMedChem.

[4]  F. Diederich,et al.  Nonphosphate Inhibitors of IspE Protein, a Kinase in the Non‐Mevalonate Pathway for Isoprenoid Biosynthesis and a Potential Target for Antimalarial Therapy , 2007, ChemMedChem.

[5]  F. Diederich,et al.  Structure‐Based Design and Synthesis of the First Weak Non‐Phosphate Inhibitors for IspF, an Enzyme in the Non‐Mevalonate Pathway of Isoprenoid Biosynthesis , 2007 .

[6]  F. Diederich,et al.  A Novel Synthesis of Highly Substituted Perhydropyrrolizines, Perhydroindolizines, and Pyrrolidines: Inhibition of the Peptidyl‐Prolyl cis/trans Isomerase (PPIase) Pin1 , 2007 .

[7]  F. Diederich,et al.  Mapping the Fluorophilicity of a Hydrophobic Pocket: Synthesis and Biological Evaluation of Tricyclic Thrombin Inhibitors Directing Fluorinated Alkyl Groups into the P Pocket , 2006, ChemMedChem.

[8]  Manfred Kansy,et al.  A Fluorine Scan at the Catalytic Center of Thrombin: CF, COH, and COMe Bioisosterism and Fluorine Effects on pKa and log D Values , 2006, ChemMedChem.

[9]  F. Diederich,et al.  Second-Generation Inhibitors for the Metalloprotease Neprilysin Based on Bicyclic Heteroaromatic Scaffolds: Synthesis, Biological Activity, and X-ray Crystal Structure Analysis , 2005 .

[10]  F. Diederich,et al.  A New Class of Inhibitors for the Metalloprotease Neprilysin Based on a Central Imidazole Scaffold , 2005 .

[11]  W. R. Dolbier,et al.  Fluorine chemistry at the millennium , 2005 .

[12]  F. Diederich,et al.  Structure‐Based Design, Synthesis, and in vitro Evaluation of Nonpeptidic Neprilysin Inhibitors , 2004, Chembiochem : a European journal of chemical biology.

[13]  C. Urch,et al.  Experimental Measurement of Noncovalent Interactions Between Halogens and Aromatic Rings , 2004, Chembiochem : a European journal of chemical biology.

[14]  Martin Stahl,et al.  Fluorine in Medicinal Chemistry , 2004, Chembiochem : a European journal of chemical biology.

[15]  F. Diederich,et al.  A fluorine scan of the phenylamidinium needle of tricyclic thrombin inhibitors: effects of fluorine substitution on pKa and binding affinity and evidence for intermolecular C-F...CN interactions. , 2004, Organic & biomolecular chemistry.

[16]  E. Kool,et al.  Selective pairing of polyfluorinated DNA bases. , 2004, Journal of the American Chemical Society.

[17]  B. Roques,et al.  Structural analysis of neprilysin with various specific and potent inhibitors. , 2004, Acta crystallographica. Section D, Biological crystallography.

[18]  Paul Seiler,et al.  A fluorine scan of thrombin inhibitors to map the fluorophilicity/fluorophobicity of an enzyme active site: evidence for C-F...C=O interactions. , 2003, Angewandte Chemie.

[19]  F. Diederich,et al.  Interactions with aromatic rings in chemical and biological recognition. , 2003, Angewandte Chemie.

[20]  P. Coric,et al.  Toward an optimal joint recognition of the S1' subsites of endothelin converting enzyme-1 (ECE-1), angiotensin converting enzyme (ACE), and neutral endopeptidase (NEP). , 2002, Journal of medicinal chemistry.

[21]  Bruce E. Smart,et al.  Fluorine substituent effects (on bioactivity) , 2001 .

[22]  T. Saido,et al.  Metabolic Regulation of Brain Aβ by Neprilysin , 2001, Science.

[23]  J. Schwartz,et al.  Vasopeptidase inhibitors: an emerging class of cardiovascular drugs. , 2001, Trends in pharmacological sciences.

[24]  D. Coates,et al.  The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function , 2001, BioEssays : news and reviews in molecular, cellular and developmental biology.

[25]  Chu-Young Kim,et al.  Contribution of Fluorine to Protein−Ligand Affinity in the Binding of Fluoroaromatic Inhibitors to Carbonic Anhydrase II , 2000 .

[26]  T. Saido,et al.  Reply to: 'Clearance of amyloid β-peptide from brain: transport or metabolism?' , 2000, Nature Medicine.

[27]  F. Winkler,et al.  Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon. , 2000, Journal of molecular biology.

[28]  T. Saido,et al.  Identification of the major Aβ1–42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition , 2000, Nature Medicine.

[29]  Christopher A. Hunter,et al.  Hydrogen-bond recognition of cyclic dipeptides in water , 1998 .

[30]  A. Jeng,et al.  Potent non-peptidic dual inhibitors of endothelin-converting enzyme and neutral endopeptidase 24.11 , 1997 .

[31]  K. Tanzawa,et al.  Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX , 1997, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[32]  Robin Taylor,et al.  Organic Fluorine Hardly Ever Accepts Hydrogen Bonds , 1997 .

[33]  Some influences of fluorine in bioorganic chemistry , 1997 .

[34]  Regine Bohacek,et al.  Three-Dimensional Models of ACE and NEP Inhibitors and Their Use in the Design of Potent Dual ACE/NEP Inhibitors , 1996 .

[35]  M. Fournié-Zaluski,et al.  Design of orally active dual inhibitors of neutral endopeptidase and angiotensin-converting enzyme with long duration of action. , 1996, Journal of medicinal chemistry.

[36]  L. Juliano,et al.  A highly selective assay for neutral endopeptidase based on the cleavage of a fluorogenic substrate related to Leu-enkephalin. , 1996, Analytical biochemistry.

[37]  Paul R. Gerber,et al.  MAB, a generally applicable molecular force field for structure modelling in medicinal chemistry , 1995, J. Comput. Aided Mol. Des..

[38]  M. Fournié-Zaluski,et al.  Inhibitors of neprilysin: design, pharmacological and clinical applications. , 1995, Methods in enzymology.

[39]  M. Fournié-Zaluski,et al.  Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology. , 1993, Pharmacological reviews.

[40]  H. Stein,et al.  CD10/neutral endopeptidase 24.11 hydrolyzes bombesin-like peptides and regulates the growth of small cell carcinomas of the lung. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[41]  R. Skidgel,et al.  Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones 1 , 1989, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[42]  A. Kenny,et al.  Role of endopeptidase‐24.11 in the inactivation of atrial natriuretic peptide , 1988, FEBS letters.

[43]  Davidr . Evans,et al.  Asymmetric synthesis of the enkephalinase inhibitor thiorphan , 1985 .

[44]  A. Turner,et al.  Substance P and [Leu]enkephalin are hydrolyzed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[45]  J. Schwartz,et al.  The enkephalinase inhibitor thiorphan shows antinociceptive activity in mice , 1980, Nature.

[46]  J. Schwartz,et al.  High-affinity enkephalin-degrading peptidase in brain is increased after morphine , 1978, Nature.

[47]  L. Stein,et al.  Analgesia induced in vivo by central administration of enkephalin in rat , 1976, Nature.

[48]  M. Kerr,et al.  The purification and specificity of a neutral endopeptidase from rabbit kidney brush border. , 1974, The Biochemical journal.