Jun Zeng
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Jun Zeng has a total of 2 co-authors. Here are the top co-authors by number of shared publications:
George B. Rudy
Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital
1 shared publication- Herbert Treutlein
Applied Physics, School of Applied Sciences, RMIT University, GPO Box 2476V, Melbourne, Victoria, 3001, Australia, and Cytopia Research Pty. Ltd., PO Box 6492, St. Kilda Road Central, Melbourne, Victoria, 8008, Australia
1 shared publication
Latest Publications
- 1 June 2001
- Published by Springer Nature in Journal of Computer-Aided Molecular Design
- Vol. 15 (6) , 573-586
Predicting sequences and structures of MHC-binding peptides: a computational combinatorial approach
Peptides bound to MHC molecules on the surface of cells convey critical information about the cellular milieu to immune system T cells. Predicting which peptides can bind an MHC molecule, and...
- 1 June 2001
- Published by Springer Nature in Journal of Computer-Aided Molecular Design
- Vol. 15 (6) , 573-586
Predicting sequences and structures of MHC-binding peptides: a computational combinatorial approach
Peptides bound to MHC molecules on the surface of cells convey critical information about the cellular milieu to immune system T cells. Predicting which peptides can bind an MHC molecule, and...
- 1 October 2000
- Published by Bentham Science Publishers Ltd. in Combinatorial Chemistry & High Throughput Screening
- Vol. 3 (5) , 355-362
Mini-Review: Computational Structure-Based Design of Inhibitors that Target Protein Surfaces
Finding drugs that inhibit protein-protein interactions is usually difficult. While computeraided design is used widely to facilitate the drug discovery process for protein targets with well-defined binding pockets, its application to the design of inhibitors targeting a protein surface is very limited. In this mini-review we address two aspects of this issue: firstly, we overview the current state of design methodology for inhibitors specifically targeting protein surfaces, and secondly, we briefly outline recent advances in computational methods for structure-based drug design. These methods are closely related to protein docking and protein recognition, the difference being that in ligand design, ligands are built on a fragment-by-fragment basis. A novel scheme of computational combinatorial ligand design developed for the design of inhibitors that interfere with protein-protein interaction is described in detail. Current applications and limitations of this methodology, as well as its future prospects, are discussed.
- 1 October 2000
- Published by Bentham Science Publishers Ltd. in Combinatorial Chemistry & High Throughput Screening
- Vol. 3 (5) , 355-362
Mini-Review: Computational Structure-Based Design of Inhibitors that Target Protein Surfaces
Finding drugs that inhibit protein-protein interactions is usually difficult. While computeraided design is used widely to facilitate the drug discovery process for protein targets with well-defined binding pockets, its application to the design of inhibitors targeting a protein surface is very limited. In this mini-review we address two aspects of this issue: firstly, we overview the current state of design methodology for inhibitors specifically targeting protein surfaces, and secondly, we briefly outline recent advances in computational methods for structure-based drug design. These methods are closely related to protein docking and protein recognition, the difference being that in ligand design, ligands are built on a fragment-by-fragment basis. A novel scheme of computational combinatorial ligand design developed for the design of inhibitors that interfere with protein-protein interaction is described in detail. Current applications and limitations of this methodology, as well as its future prospects, are discussed.