Proteochemometrics mapping of the interaction space for retroviral proteases and their substrates.

[1]  Peteris Prusis,et al.  Proteochemometric analysis of small cyclic peptides' interaction with wild‐type and chimeric melanocortin receptors , 2007, Proteins.

[2]  Peteris Prusis,et al.  A Look Inside HIV Resistance through Retroviral Protease Interaction Maps , 2007, PLoS Comput. Biol..

[3]  L. Eriksson Multi- and megavariate data analysis , 2006 .

[4]  Peteris Prusis,et al.  Prediction of indirect interactions in proteins , 2006, BMC Bioinformatics.

[5]  M. Jaskólski,et al.  Crystal structure of human T cell leukemia virus protease, a novel target for anticancer drug design. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[6]  Asim Kumar Debnath,et al.  Application of 3D-QSAR techniques in anti-HIV-1 drug design--an overview. , 2005, Current pharmaceutical design.

[7]  Peteris Prusis,et al.  Proteochemometrics: A Tool for Modeling the Molecular Interaction Space , 2005 .

[8]  E. Freire,et al.  Adaptive inhibitors of the HIV-1 protease. , 2005, Progress in biophysics and molecular biology.

[9]  E. Freire,et al.  Design of inhibitors against HIV, HTLV-I, and Plasmodium falciparum aspartic proteases , 2004, Biological chemistry.

[10]  A. Velázquez‐Campoy,et al.  Thermodynamic rules for the design of high affinity HIV-1 protease inhibitors with adaptability to mutations and high selectivity towards unwanted targets. , 2004, The international journal of biochemistry & cell biology.

[11]  Hugo Kubinyi,et al.  Chemogenomics in Drug Discovery: A Medicinal Chemistry Perspective , 2004 .

[12]  J. Randolph,et al.  Peptidomimetic inhibitors of HIV protease. , 2004, Current topics in medicinal chemistry.

[13]  Rajni Garg,et al.  HIV-1 protease inhibitors: a comparative QSAR analysis. , 2003, Current medicinal chemistry.

[14]  P. Prusis,et al.  Melanocortin Receptors: Ligands and Proteochemometrics Modeling , 2003, Annals of the New York Academy of Sciences.

[15]  Peteris Prusis,et al.  QSAR and proteo-chemometric analysis of the interaction of a series of organic compounds with melanocortin receptor subtypes. , 2003, Journal of medicinal chemistry.

[16]  B. Dunn,et al.  Aspartic Peptidase Inhibitors: Implications in Drug Development , 2003, Critical reviews in biochemistry and molecular biology.

[17]  T. Lundstedt,et al.  Proteochemometrics modeling of the interaction of amine G-protein coupled receptors with a diverse set of ligands. , 2002, Molecular pharmacology.

[18]  T. Lundstedt,et al.  Proteo-chemometrics analysis of MSH peptide binding to melanocortin receptors. , 2002, Protein engineering.

[19]  Garrett M Morris,et al.  Defining HIV-1 protease substrate selectivity. , 2002, Current drug targets. Infectious disorders.

[20]  E. Freire,et al.  Designing drugs against heterogeneous targets , 2002, Nature Biotechnology.

[21]  Zachary Q. Beck,et al.  Identification of efficiently cleaved substrates for HIV-1 protease using a phage display library and use in inhibitor development. , 2000, Virology.

[22]  A Wlodawer,et al.  Structural and biochemical studies of retroviral proteases. , 2000, Biochimica et biophysica acta.

[23]  T. Lundstedt,et al.  Experimental design and optimization , 1998 .

[24]  S. Wold,et al.  New chemical descriptors relevant for the design of biologically active peptides. A multivariate characterization of 87 amino acids. , 1998, Journal of medicinal chemistry.

[25]  M. Lindgren,et al.  Investigation of an allosteric site of HIV-1 proteinase involved in inhibition by Cu2+. , 1998, Advances in experimental medicine and biology.

[26]  L. Polgár,et al.  Rate-determining Steps in HIV-1 Protease Catalysis , 1996, The Journal of Biological Chemistry.

[27]  J. Erickson,et al.  Structural mechanisms of HIV drug resistance. , 1996, Annual review of pharmacology and toxicology.

[28]  I. Boros,et al.  Substrate-dependent mechanisms in the catalysis of human immunodeficiency virus protease. , 1994, Biochemistry.

[29]  D Norbeck,et al.  Characterization of human immunodeficiency virus type 1 variants with increased resistance to a C2-symmetric protease inhibitor , 1994, Journal of virology.

[30]  I. Wakeling,et al.  A test of significance for partial least squares regression , 1993 .

[31]  L. Kuo,et al.  Activity and dimerization of human immunodeficiency virus protease as a function of solvent composition and enzyme concentration. , 1992, The Journal of biological chemistry.

[32]  J. Louis,et al.  Kinetic and modeling studies of S3-S3' subsites of HIV proteinases. , 1992, Biochemistry.

[33]  J. Tang,et al.  Kinetic studies of human immunodeficiency virus type 1 protease and its active-site hydrogen bond mutant A28S. , 1991, The Journal of biological chemistry.

[34]  T. Meek,et al.  Human immunodeficiency virus-1 protease. 2. Use of pH rate studies and solvent kinetic isotope effects to elucidate details of chemical mechanism. , 1991, Biochemistry.

[35]  I. Weber,et al.  Comparison of inhibitor binding in HIV‐1 protease and in non‐viral aspartic proteases: the role of the flap , 1990, FEBS letters.

[36]  William G. Bardsley,et al.  Optimal design for model discrimination using the F-test with non-linear biochemical models. Criteria for choosing the number and spacing of experimental points , 1989 .

[37]  B. Efron Better Bootstrap Confidence Intervals , 1987 .

[38]  S. Wold Cross-Validatory Estimation of the Number of Components in Factor and Principal Components Models , 1978 .

[39]  Y. Cheng,et al.  Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. , 1973, Biochemical pharmacology.