-Buyong Ma Researcher Activity Profile

Research Author Detailed Information 

Buyong Ma Publication Rate By Year

Buyong Ma has published 2 paper(s) in 2005, 5 paper(s) in 2006, 7 paper(s) in 2007, 2 paper(s) in 2008, for a total of 16 research publications in total.

Buyong B Ma Author Information

LAST NAME: ma

FIRST NAME: buyong

INITIALS: B

AFFILIATION:

Papers

Buyong Ma's Publication Record

1. Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effect. Year Published: 2007
Center for Cancer Research Nanobiology Program, SAIC-Frederick, Inc., NCI-Frederick, Frederick, Maryland 21702, USA. jangh@ncifcrf.gov <jangh@ncifcrf.gov>
2. Protein-protein interactions: organization, cooperativity and mapping in a bottom-up Systems Biology approach. Year Published: 2005
Koc University, Center for Computational Biology and Bioinformatics, and College of Engineering, Rumelifeneri Yolu, 34450 Sariyer Istanbul, Turkey.
3. The contribution of the Trp/Met/Phe residues to physical interactions of p53 with cellular proteins. Year Published: 2005
Basic Research Program, SAIC-Frederick, Inc., Laboratory of Experimental and Computational Biology, NCI-Frederick, Frederick, MD 21702, USA. mab@ncifcrf.gov
4. Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35. Year Published: 2006
Basic Research Program, SAIC-Frederick, Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, Maryland 21702, USA.
5. Simulations as analytical tools to understand protein aggregation and predict amyloid conformation. Year Published: 2006
Basic Research Program, SAIC-Frederick Inc, Center for Cancer Research, Nanobiology Program, NCI-Frederick, Frederick MD 21702, USA.
6. Interaction of protegrin-1 with lipid bilayers: membrane thinning effect. Year Published: 2006
Center for Cancer Research Nanobiology Program, SAIC-Frederick, Inc., NCI-Frederick, Frederick, Maryland 21702, USA.
7. Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Year Published: 2006
Basic Research Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA.
8. "Similarity trap" in protein-protein interactions could be carcinogenic: simulations of p53 core domain complexed with 53BP1 and BRCA1 BRCT domains. Year Published: 2006
Basic Research Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, National Cancer Institute-Frederick, Frederick, Maryland 21702, USA.
9. Sequence analysis of p53 response-elements suggests multiple binding modes of the p53 tetramer to DNA targets. Year Published: 2007
Basic Research Program, SAIC-Frederick Inc., Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA. mab@ncifcrf.gov
10. Trp/Met/Phe hot spots in protein-protein interactions: potential targets in drug design. Year Published: 2007
Basic Research Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA. mab@ncifcrf.gov
11. Ligand binding and circular permutation modify residue interaction network in DHFR. Year Published: 2007
Department of Biochemistry and Molecular Biology, Howard University College of Medicine, Washington, District of Columbia, United States of America.
12. Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities. Year Published: 2007
Basic Research Program, SAIC-Frederick Center for Cancer Research, Nanobiology Program, NCI-Frederick, Frederick, Maryland 21702, USA.
13. Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities. Year Published: 2007
Basic Research Program, SAIC-Frederick Center for Cancer Research, Nanobiology Program, NCI-Frederick, Frederick, Maryland 21702, USA.
14. Ligand binding and circular permutation modify residue interaction network in DHFR. Year Published: 2007
Department of Biochemistry and Molecular Biology, Howard University College of Medicine, Washington, District of Columbia, United States of America.
15. Probing potential binding modes of the p53 tetramer to DNA based on the symmetries encoded in p53 response elements. Year Published: 2008
Basic Research Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA. mab@ncifcrf.gov
16. Probing potential binding modes of the p53 tetramer to DNA based on the symmetries encoded in p53 response elements. Year Published: 2008
Basic Research Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA. mab@ncifcrf.gov