Moses Prabu-Jeyabalan

Structural analysis of human immunodeficiency virus type 1 CRF01_AE protease in complex with the substrate p1-p6. (2008)

Bandaranayake, Rajintha M., Prabu-Jeyabalan, Moses, Kakizawa, Junko, Sugiura, Wataru, Schiffer, Celia A.

The effect of amino acid variability between human immunodeficiency virus type 1 (HIV-1) clades on structure and the emergence of resistance mutations in HIV-1 protease has become an area of...

Role of invariant Thr80 in human immunodeficiency virus type 1 protease structure, function, and viral infectivity (2006)

Foulkes-Murzycki, Jennifer E., Prabu-Jeyabalan, Moses, Cooper, Deyna, Henderson, Gavin J., Harris, Janera, Swanstrom, Ronald I., ...

Sequence variability associated with human immunodeficiency virus type 1 (HIV-1) is useful for inferring structural and/or functional constraints at specific residues within the viral protease....

Substrate envelope and drug resistance: crystal structure of RO1 in complex with wild-type human immunodeficiency virus type 1 protease (2006)

Prabu-Jeyabalan, Moses, King, Nancy M., Nalivaika, Ellen A., Heilek-Snyder, Gabrielle, Cammack, Nick, Schiffer, Celia A.

In our previous crystallographic studies of human immunodeficiency virus type 1 (HIV-1) protease-substrate complexes, we described a conserved "envelope" that appears to be important for substrate...

Mechanism of substrate recognition by drug-resistant human immunodeficiency virus type 1 protease variants revealed by a novel structural intermediate (2006)

Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., Romano, Keith, Schiffer, Celia A.

Human immunodeficiency virus type 1 (HIV-1) protease processes and cleaves the Gag and Gag-Pol polyproteins, allowing viral maturation, and therefore is an important target for antiviral therapy....

Structural basis for coevolution of a human immunodeficiency virus type 1 nucleocapsid-p1 cleavage site with a V82A drug-resistant mutation in viral protease (2004)

Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., King, Nancy M., Schiffer, Celia A.

Maturation of human immunodeficiency virus (HIV) depends on the processing of Gag and Pol polyproteins by the viral protease, making this enzyme a prime target for anti-HIV therapy. Among the...

Structural and thermodynamic basis for the binding of TMC114, a next-generation human immunodeficiency virus type 1 protease inhibitor (2004)

King, Nancy M., Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., De Bethune, Marie-Pierre, Schiffer, Celia A.

TMC114, a newly designed human immunodeficiency virus type 1 (HIV-1) protease inhibitor, is extremely potent against both wild-type (wt) and multidrug-resistant (MDR) viruses in vitro as well as in...

Viability of a drug-resistant human immunodeficiency virus type 1 protease variant: structural insights for better antiviral therapy (2002)

Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., King, Nancy M., Schiffer, Celia A.

Under the selective pressure of protease inhibitor therapy, patients infected with human immunodeficiency virus (HIV) often develop drug-resistant HIV strains. One of the first drug-resistant...

Point mutants of EHEC intimin that diminish Tir recognition and actin pedestal formation highlight a putative Tir binding pocket (2002)

Liu, Hui, Radhakrishnan, Padhma, Magoun, Loranne, Prabu-Jeyabalan, Moses, Campellone, Kenneth Geno, Savage, Pamela Joyce, ...

Attachment to host cells by enterohaemorrhagic Escherichia coli (EHEC) is associated with the formation of a highly organized cytoskeletal structure containing filamentous actin, termed an attaching...

Lack of synergy for inhibitors targeting a multi-drug-resistant HIV-1 protease (2002)

King, Nancy M., Melnick, Laurence, Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., Yang, Shiow-Shong, Gao, Yun, ...

The three-dimensional structures of indinavir and three newly synthesized indinavir analogs in complex with a multi-drug-resistant variant (L63P, V82T, I84V) of HIV-1 protease were determined to...

Lack of synergy for inhibitors targeting a multi-drug-resistant HIV-1 protease (2002)

King, Nancy M., Melnick, Laurence, Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., Yang, Shiow-Shong, Gao, Yun, ...

The three-dimensional structures of indinavir and three newly synthesized indinavir analogs in complex with a multi-drug-resistant variant (L63P, V82T, I84V) of HIV-1 protease were determined to...

Viability of a Drug-Resistant Human Immunodeficiency Virus Type 1 Protease Variant: Structural Insights for Better Antiviral Therapy

Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., King, Nancy M., Schiffer, Celia A.

Under the selective pressure of protease inhibitor therapy, patients infected with human immunodeficiency virus (HIV) often develop drug-resistant HIV strains. One of the first drug-resistant...

Structural and Thermodynamic Basis for the Binding of TMC114, a Next-Generation Human Immunodeficiency Virus Type 1 Protease Inhibitor

King, Nancy M., Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., Wigerinck, Piet, De Béthune, Marie-Pierre, Schiffer, Celia A.

TMC114, a newly designed human immunodeficiency virus type 1 (HIV-1) protease inhibitor, is extremely potent against both wild-type (wt) and multidrug-resistant (MDR) viruses in vitro as well as in...

Structural Basis for Coevolution of a Human Immunodeficiency Virus Type 1 Nucleocapsid-p1 Cleavage Site with a V82A Drug-Resistant Mutation in Viral Protease

Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., King, Nancy M., Schiffer, Celia A.

Maturation of human immunodeficiency virus (HIV) depends on the processing of Gag and Pol polyproteins by the viral protease, making this enzyme a prime target for anti-HIV therapy. Among the...

Substrate Envelope and Drug Resistance: Crystal Structure of RO1 in Complex with Wild-Type Human Immunodeficiency Virus Type 1 Protease

Prabu-Jeyabalan, Moses, King, Nancy M., Nalivaika, Ellen A., Heilek-Snyder, Gabrielle, Cammack, Nick, Schiffer, Celia A.

In our previous crystallographic studies of human immunodeficiency virus type 1 (HIV-1) protease-substrate complexes, we described a conserved “envelope” that appears to be important for...

Mechanism of Substrate Recognition by Drug-Resistant Human Immunodeficiency Virus Type 1 Protease Variants Revealed by a Novel Structural Intermediate

Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., Romano, Keith, Schiffer, Celia A.

Human immunodeficiency virus type 1 (HIV-1) protease processes and cleaves the Gag and Gag-Pol polyproteins, allowing viral maturation, and therefore is an important target for antiviral therapy....

Role of Invariant Thr80 in Human Immunodeficiency Virus Type 1 Protease Structure, Function, and Viral Infectivity

Foulkes, Jennifer E., Prabu-Jeyabalan, Moses, Cooper, Deyna, Henderson, Gavin J., Harris, Janera, Swanstrom, Ronald, ...

Sequence variability associated with human immunodeficiency virus type 1 (HIV-1) is useful for inferring structural and/or functional constraints at specific residues within the viral protease....

Viability of a Drug-Resistant Human Immunodeficiency Virus Type 1 Protease Variant: Structural Insights for Better Antiviral Therapy

Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., King, Nancy M., Schiffer, Celia A.

Under the selective pressure of protease inhibitor therapy, patients infected with human immunodeficiency virus (HIV) often develop drug-resistant HIV strains. One of the first drug-resistant...

Structural and Thermodynamic Basis for the Binding of TMC114, a Next-Generation Human Immunodeficiency Virus Type 1 Protease Inhibitor

King, Nancy M., Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., Wigerinck, Piet, De Béthune, Marie-Pierre, Schiffer, Celia A.

TMC114, a newly designed human immunodeficiency virus type 1 (HIV-1) protease inhibitor, is extremely potent against both wild-type (wt) and multidrug-resistant (MDR) viruses in vitro as well as in...

Structural Basis for Coevolution of a Human Immunodeficiency Virus Type 1 Nucleocapsid-p1 Cleavage Site with a V82A Drug-Resistant Mutation in Viral Protease

Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., King, Nancy M., Schiffer, Celia A.

Maturation of human immunodeficiency virus (HIV) depends on the processing of Gag and Pol polyproteins by the viral protease, making this enzyme a prime target for anti-HIV therapy. Among the...

Substrate Envelope and Drug Resistance: Crystal Structure of RO1 in Complex with Wild-Type Human Immunodeficiency Virus Type 1 Protease

Prabu-Jeyabalan, Moses, King, Nancy M., Nalivaika, Ellen A., Heilek-Snyder, Gabrielle, Cammack, Nick, Schiffer, Celia A.

In our previous crystallographic studies of human immunodeficiency virus type 1 (HIV-1) protease-substrate complexes, we described a conserved “envelope” that appears to be important for...

Mechanism of Substrate Recognition by Drug-Resistant Human Immunodeficiency Virus Type 1 Protease Variants Revealed by a Novel Structural Intermediate

Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., Romano, Keith, Schiffer, Celia A.

Human immunodeficiency virus type 1 (HIV-1) protease processes and cleaves the Gag and Gag-Pol polyproteins, allowing viral maturation, and therefore is an important target for antiviral therapy....

Role of Invariant Thr80 in Human Immunodeficiency Virus Type 1 Protease Structure, Function, and Viral Infectivity

Foulkes, Jennifer E., Prabu-Jeyabalan, Moses, Cooper, Deyna, Henderson, Gavin J., Harris, Janera, Swanstrom, Ronald, ...

Sequence variability associated with human immunodeficiency virus type 1 (HIV-1) is useful for inferring structural and/or functional constraints at specific residues within the viral protease....

Lack of synergy for inhibitors targeting a multi-drug-resistant HIV-1 protease

King, Nancy M., Melnick, Laurence, Prabu-Jeyabalan, Moses, Nalivaika, Ellen A., Yang, Shiow-Shong, Gao, Yun, ...

The three-dimensional structures of indinavir and three newly synthesized indinavir analogs in complex with a multi-drug-resistant variant (L63P, V82T, I84V) of HIV-1 protease were determined to...

Structural Analysis of Human Immunodeficiency Virus Type 1 CRF01_AE Protease in Complex with the Substrate p1-p6▿

Bandaranayake, Rajintha M., Prabu-Jeyabalan, Moses, Kakizawa, Junko, Sugiura, Wataru, Schiffer, Celia A.

The effect of amino acid variability between human immunodeficiency virus type 1 (HIV-1) clades on structure and the emergence of resistance mutations in HIV-1 protease has become an area of...