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Number of items: 8.

Conference Paper

Kumar, A and Chandu, Dilip and Nandi, D (2004) Substrate specificity and role of PepN, a metallo-aminoendopeptidase from Escherichia coli. In: Annual Meeting of the American-Society-for-Biochemistry-and-Molecular-Biology/8th Congress of the International-Union-for-Biochemistry-and-Molecular-Biology, JUN 12-16, 2004, Boston, MA.

Journal Article

Chandu, Dilip and Wood, R and Anderson, TL and Satheesh, SK and Charlson, RJ (2009) Satellite-derived direct radiative effect of aerosols dependent on cloud cover. In: Nature Geoscience, 2 (3). pp. 181-184.

Nandi, Dipankar and Tahiliani, Pankaj and Kumar, Anujith and Chandu, Dilip (2006) The ubiquitin-proteasome system. In: Journal of Biosciences, 31 (1). pp. 137-155.

Tahiliani, P and Kumar, Mohan M and Chandu, Dilip and Kumar, A and Nagaraj, C and Nandi, D (2005) Gel Purified Lipl32: A Prospective Antigen for Detection of Leptospirosis. In: Journal of Postgraduate Medicine, 51 (3). pp. 164-168.

Chandu, Dilip and Nandi, Dipankar (2004) Comparative genomics and functional roles of the ATP-dependent proteases Lon and Clp during cytosolic protein degradation. In: Research in Microbiology, 155 . pp. 710-719.

Chandu, Dilip and Nandi, Dipankar (2003) PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress. In: Microbiology, 149 . pp. 3437-3447.

Chandu, Dilip and Kumar, Anujith and Nandi, Dipankar (2003) PepN, the Major Suc-LLVY-AMC-hydrolyzing Enzyme in Escherichia coli, Displays Functional Similarity with Downstream Processing Enzymes in Archaea and Eukarya:Implications in Cytosolic Protein Degradation. In: Journal of Biological Chemistry, 278 (8). pp. 5548-5556.

Chandu, Dilip and Nandi, Dipankar (2002) From proteins to peptides to amino acids: comparative genomics of enzymes involved in downstream events during cytosoliv protein degradation. In: Applied Genomics and proteomics, 1 (4). pp. 235-252.

This list was generated on Thu Oct 17 10:19:00 2019 IST.