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http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_10/101021bi992112c/authorship/5
http://hub.abes.fr/acs/periodical/jmcmar/2002/volume_45/issue_15/101021jm020037p/authorship/9
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_46/101021bi00046a018/authorship/4
http://hub.abes.fr/acs/periodical/jmcmar/1994/volume_37/issue_9/101021jm00035a013/authorship/3
http://hub.abes.fr/acs/periodical/jcics1/1998/volume_38/issue_5/101021ci9800920/authorship/1
http://hub.abes.fr/acs/periodical/jmcmar/2007/volume_50/issue_8/101021jm0614073/authorship/8
http://hub.abes.fr/acs/periodical/jmcmar/1997/volume_40/issue_6/101021jm960596u/authorship/1
http://hub.abes.fr/acs/periodical/jpcafh/2005/volume_109/issue_20/101021jp0450181/authorship/2
http://hub.abes.fr/oup/periodical/carcin/2005/volume_27/issue_4/101093carcinbgi235/authorship/5
http://hub.abes.fr/acs/periodical/jacsat/2007/volume_129/issue_19/101021ja0688732/authorship/7
http://hub.abes.fr/acs/periodical/jmcmar/2004/volume_47/issue_20/101021jm049723/authorship/5
http://hub.abes.fr/acs/periodical/jcics1/2003/volume_43/issue_1/101021ci020048r/authorship/8
http://hub.abes.fr/acs/periodical/jmcmar/2005/volume_48/issue_3/101021jm0492709/authorship/7
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http://hub.abes.fr/acs/periodical/jcics1/2002/volume_42/issue_1/101021ci010056s/authorship/5
http://hub.abes.fr/acs/periodical/jcics1/2004/volume_44/issue_5/101021ci049881/authorship/5
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http://hub.abes.fr/acs/periodical/jmcmar/2001/volume_44/issue_25/101021jm0103965/authorship/8
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http://hub.abes.fr/acs/periodical/jacsat/2000/volume_122/issue_50/101021ja001989s/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_2/101021ja037929e/authorship/5
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http://hub.abes.fr/acs/periodical/jmcmar/2001/volume_44/issue_12/101021jm010052e/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_28/101021ja800964g/authorship/3
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http://hub.abes.fr/acs/periodical/jmcmar/2005/volume_48/issue_18/101021jm050352m/authorship/5
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http://hub.abes.fr/acs/periodical/jcics1/1993/volume_33/issue_4/101021ci00014a019/authorship/1
http://hub.abes.fr/acs/periodical/jcics1/1994/volume_34/issue_5/101021ci00021a032/authorship/2
http://hub.abes.fr/springer/periodical/10822/1992/volume_6/issue_5/B947C239F57A2014E053120B220ACB0F/authorship/1
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Conformationally Locked Nucleoside Analogs. Synthesis of Dideoxycarbocyclic Nucleoside Analogs Structurally Related to Neplanocin C
Chem-X and CAMBRIDGE. Comparison of computer generated chemical structures with x-ray crystallographic data
Discovery of HIV-1 Integrase Inhibitors by Pharmacophore Searching
Structure Activity of 3-Aryl-1,3-diketo-Containing Compounds as HIV-1Integrase Inhibitors
Structure, Stability, and NMR Properties of Lower Fullerenes C38−C50 and AzafullereneC44N6
Metal-Dependent Inhibition of HIV-1 Integrase
Differential Binding Modes of Diacylglycerol (DAG) and DAG Lactones toProtein Kinase C (PK-C)
Conformationally Constrained Analogues of Diacylglycerol (DAG). 25.Exploration of the sn-1 and sn-2 Carbonyl Functionality Reveals the EssentialRole of the sn-1 Carbonyl at the Lipid Interface in the Binding of DAG-Lactonesto Protein Kinase C
Experimental and Structural Evidence that Herpes 1 Kinaseand Cellular DNA Polymerase(s) Discriminate on the Basis ofSugar Pucker
Design and Synthesis of Conformationally Constrained Grb2 SH2 DomainBinding Peptides Employing α-Methylphenylalanyl Based PhosphotyrosylMimetics
Evidence that sequence homologous region in LRAT-like proteins possesses anti-proliferative activity and DNA binding properties: translational implications and mechanism of action
Sculpting the Bicyclo[3.1.0]hexane Template of CarbocyclicNucleosides to Improve Recognition by Herpes ThymidineKinase
Comprehensive Structural Studies of 2′,3′-Difluorinated Nucleosides: Comparison of Theory, Solution, and Solid State
An Optimized Protein Kinase C Activating Diacylglycerol Combining HighBinding Affinity (Ki) with Reduced Lipophilicity (log P)
Examination of Acylated 4-Aminopiperidine-4-carboxylic Acid Residues in thePhosphotyrosyl+1 Position of Grb2 SH2 Domain-Binding Tripeptides
Adenosine Deaminase Prefers a Distinct Sugar Ring Conformation for Binding andCatalysis: Kinetic and Structural Studies
Computational Chemistry on Commodity-Type Computers
Conformationally Constrained Analogues of Diacylglycerol (DAG). 23.Hydrophobic Ligand−Protein Interactions versus Ligand−Lipid Interactions ofDAG-Lactones with Protein Kinase C (PK-C)
Comparison of the NCI Open Database with Seven Large Chemical StructuralDatabases
Interactions of Conformationally Biased North and South2‘-Fluoro-2‘,3‘-dideoxynucleoside 5‘-Triphosphates with the Active Site of HIV-1Reverse Transcriptase
PROSIT: Pseudo-Rotational Online Service and Interactive Tool, Applied to aConformational Survey of Nucleosides and Nucleotides
HIV-1 Integrase Pharmacophore: Discovery of Inhibitors throughThree-Dimensional Database Searching
Molecular Modeling in the Discovery of Drug Leads
Antiretroviral Agents as Inhibitors of both Human Immunodeficiency VirusType 1 Integrase and Protease
PASS Biological Activity Spectrum Predictions in the Enhanced OpenNCI Database Browser
Conformationally Constrained Analoguesof Diacylglycerol. 18. The Incorporationof a Hydroxamate Moiety intoDiacylglycerol-Lactones ReducesLipophilicity and Helps Discriminatebetween sn-1 and sn-2 Binding Modes toProtein Kinase C (PK-C). Implications forIsozyme Specificity
Enhanced CACTVS Browser of the Open NCI Database
Discovery of Novel, Non-Peptide HIV-1 Protease Inhibitors by PharmacophoreSearching
Depsides and Depsidones as Inhibitors of HIV-1 Integrase: Discovery of NovelInhibitors through 3D Database Searching
QSAR of conformationally flexible molecules: Comparative Molecular Field Analysis of protein-tyrosine kinase inhibitors
Effects of Tyrphostins, Protein Kinase Inhibitors, on Human Immunodeficiency Virus Type 1 Integrase
National Cancer Institute Drug Information System 3D Database
Protein Kinase C. Modeling of the Binding Site and Prediction of Binding Constants
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