B. Shenoy

发表

A. G. Rao, L. Katwa, M. Rao, 2007, Journal of Biosciences.

Electric fields in active sites: substrate switching from null to strong fields in thiol- and selenol-subtilisins.

D. Hilvert, D. Dinakarpandian, D. McRee, 1999, Biochemistry.

Purification of polyphosphate and ATP glucose phosphotransferase from Mycobacterium tuberculosis H37Ra: evidence that poly(P) and ATP glucokinase activities are catalyzed by the same enzyme.

N. Phillips, P. Hsieh, B. Shenoy, 1993, Protein expression and purification.

Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study.

P. Carey, F. Sönnichsen, B. Shenoy, 1997, Biochemistry.

Chemical modification of the functional arginine residues of carbon monoxide dehydrogenase from Clostridium thermoaceticum.

T. Shanmugasundaram, H. Wood, B. Shenoy, 1989, Biochemistry.

Studies on plant gums. Role of calcium in polysaccharide-protein interaction in the neem (Azadirachta indica) gum

T. N. Pattabiraman, B. Shenoy, B. R. Nayak, 1979, Journal of Biosciences.

Arginine-239 in the beta subunit is at or near the active site of bovine pyruvate dehydrogenase.

T. Roche, M. Patel, L. Korotchkina, 1995, Biochimica et biophysica acta.

Hyperoxaluria Is Reduced and Nephrocalcinosis Prevented with an Oxalate-Degrading Enzyme in Mice with Hyperoxaluria

E. Salido, A. Margolin, C. Langman, 2008, American Journal of Nephrology.

Purification and properties of diaminopimelate decarboxylase ofMicrococcus glutamicus

M. Rao, B. Shenoy, M. Lakshman, 1981, Journal of Biosciences.

The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis.

H. Wood, Y. Xie, D. Samols, 1992, The Journal of biological chemistry.

Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli

H. Wood, N. Phillips, D. Samols, 1993, Journal of bacteriology.

Structure and stability of glucoamylase II fromAspergillus niger: A circular dichroism study

A. G. Rao, M. Rao, B. Shenoy, 1984, Journal of Biosciences.

Identification and characterization of a factor which is essential for assembly of transcarboxylase.

Y. Xie, D. Sha, D. Samols, 1993, Biochemistry.

Primary structure of the 5 S subunit of transcarboxylase as deduced from the genomic DNA sequence

H. Wood, C. Thornton, D. Samols, 1993, FEBS letters.

Involvement of tryptophan(s) at the active site of polyphosphate/ATP glucokinase from Mycobacterium tuberculosis.

N. Phillips, P. Hsieh, B. Shenoy, 1993, Biochemistry.

Identification of the Tryptophan Residue in the Thiamin Pyrophosphate Binding Site of Mammalian Pyruvate Dehydrogenase (*)

T. Roche, M. Patel, B. Shenoy, 1995, The Journal of Biological Chemistry.

Injectable controlled release formulations incorporating protein crystals.

A. Margolin, Mark X Yang, S. Basu, 2004, Journal of controlled release : official journal of the Controlled Release Society.

Cell selective induction and transcriptional activation of immediate early genes by hypoxia

N. Prabhakar, N. Cherniack, M. Simonson, 1995, Brain Research.

Isolation and characterization of a novel haemoprotein b-559 from Bengal gram (Cicer arietinum).

A. Borthakur, C. S. Ramadoss, B. Shenoy, 1987, The Biochemical journal.

Crystalline monoclonal antibodies for subcutaneous delivery

Sergey Pechenov, A. Margolin, Mark X Yang, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Aspartokinase of a lysine producing mutant ofMicrococcus glutamicus

M. Rao, B. Shenoy, M. Lakshman, 1981, Journal of Biosciences.

Cloning, Expression, and Characterization of Polyphosphate Glucokinase from Mycobacterium tuberculosis(*)

D. Samols, B. Shenoy, Pei-chung Hsieh, 1996, The Journal of Biological Chemistry.

High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii.

P. Carey, F. Sönnichsen, B. Shenoy, 2000, Biochemistry.

Effect of mutations at Met‐88 and Met‐90 on the biotination of Lys‐89 of the apo 1.3S subunit of transcarboxylase

H. Wood, B. Shenoy, G. K. Kumar, 1988, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Purification and properties of the synthetase catalyzing the biotination of the aposubunit of transcarboxylase from Propionibacterium shermanii

H. Wood, B. Shenoy, 1988, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii

P. Carey, F. Sönnichsen, S. Rothemund, 1998, Protein science : a publication of the Protein Society.

Effect of chemical modification on struture and activity of glucoamylase fromAspergillus candidus andRhizopus species

A. G. Rao, M. Rao, B. Shenoy, 1987, Journal of Biosciences.

Cross-linked protein crystals for vaccine delivery.

B. Shenoy, A. Margolin, B. Shenoy, 1999, Proceedings of the National Academy of Sciences of the United States of America.