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B M Dunn

Showing results (111-120 of 123) with videos related to

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Biochemistry|January 31, 1995
Effect of point mutations on the kinetics and the inhibition of human immunodeficiency virus type 1 protease: relationship to drug resistanceY Lin, X Lin, L Hong, et al.
Biochemistry|September 8, 1992
X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitorsJ Cooper, W Quail, C Frazao, et al.
Advances in Experimental Medicine and Biology|January 1, 1988
Aspartic proteinases and inhibitors for their control in health and diseaseJ Kay, R A Jupp, C G Norey, et al.
Protein Science : a Publication of the Protein Society|November 25, 1998
Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAVJ Kervinen, J Lubkowski, A Zdanov, et al.
Biochemistry|June 9, 1992
Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobic*hydrophobic- or -aromatic*pro- cleavage sitesJ T Griffiths, L H Phylip, J Konvalinka, et al.
The Journal of Infectious Diseases|February 15, 2001
Human immunodeficiency virus type 1 protease genotype predicts immune and viral responses to combination therapy with protease inhibitors (PIs) in PI-naive patientsE E Perez, S L Rose, B Peyser, et al.
Journal of Medicinal Chemistry|September 3, 1993
Specificity in the binding of inhibitors to the active site of human/primate aspartic proteinases: analysis of P2-P1-P1'-P2' variationC M Rao, P E Scarborough, J Kay, et al.
The Journal of Biological Chemistry|May 15, 1990
Sensitive, soluble chromogenic substrates for HIV-1 proteinaseA D Richards, L H Phylip, W G Farmerie, et al.
Advances in Experimental Medicine and Biology|January 1, 1991
Substrate cleavage by HIV-1 proteinaseR A Jupp, A D Richards, L H Phylip, et al.
The Journal of Biological Chemistry|October 24, 2000
The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiaeL H Phylip, W E Lees, B G Brownsey, et al.
Pageof 13

Showing results (111-120 of 123) with videos related to

Sort By:
Pageof 13
Biochemistry|January 31, 1995
Effect of point mutations on the kinetics and the inhibition of human immunodeficiency virus type 1 protease: relationship to drug resistanceY Lin, X Lin, L Hong, et al.
Biochemistry|September 8, 1992
X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitorsJ Cooper, W Quail, C Frazao, et al.
Advances in Experimental Medicine and Biology|January 1, 1988
Aspartic proteinases and inhibitors for their control in health and diseaseJ Kay, R A Jupp, C G Norey, et al.
Protein Science : a Publication of the Protein Society|November 25, 1998
Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAVJ Kervinen, J Lubkowski, A Zdanov, et al.
Biochemistry|June 9, 1992
Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobic*hydrophobic- or -aromatic*pro- cleavage sitesJ T Griffiths, L H Phylip, J Konvalinka, et al.
The Journal of Infectious Diseases|February 15, 2001
Human immunodeficiency virus type 1 protease genotype predicts immune and viral responses to combination therapy with protease inhibitors (PIs) in PI-naive patientsE E Perez, S L Rose, B Peyser, et al.
Journal of Medicinal Chemistry|September 3, 1993
Specificity in the binding of inhibitors to the active site of human/primate aspartic proteinases: analysis of P2-P1-P1'-P2' variationC M Rao, P E Scarborough, J Kay, et al.
The Journal of Biological Chemistry|May 15, 1990
Sensitive, soluble chromogenic substrates for HIV-1 proteinaseA D Richards, L H Phylip, W G Farmerie, et al.
Advances in Experimental Medicine and Biology|January 1, 1991
Substrate cleavage by HIV-1 proteinaseR A Jupp, A D Richards, L H Phylip, et al.
The Journal of Biological Chemistry|October 24, 2000
The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiaeL H Phylip, W E Lees, B G Brownsey, et al.
Pageof 13