A. Acharya

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Site-specific PEGylation of hemoglobin at Cys-93(beta): correlation between the colligative properties of the PEGylated protein and the length of the conjugated PEG chain.

P. K. Smith, B. Manjula, A. Tsai, 2003, Bioconjugate chemistry.

and Innate Variation in Nitric Oxide Production by Mononuclear Cells Variation in the Pulmonary Hypertensive Responsiveness of Broilers to Lipopolysaccharide

M. Gladwin, S. G. Shimada, J. Stitt, 2015 .

Antigenic domains of the streptococcal Pep M5 protein. Localization of epitopes crossreactive with type 6 M protein and identification of a hypervariable region of the M molecule

B. Manjula, A. Acharya, V. Fischetti, 1986, The Journal of experimental medicine.

Dihydroxypropylation of amino groups of proteins: use of glyceraldehyde as a reversible agent for reductive alkylation.

B. Manjula, A. Acharya, 1987, Biochemistry.

The complete amino acid sequence of a biologically active 197-residue fragment of M protein isolated from type 5 group A streptococci.

B. Manjula, A. Acharya, V. Fischetti, 1984, The Journal of biological chemistry.

Cross-linking of proteins by aldotriose: reaction of the carbonyl function of the keto amines generated in situ with amino groups.

B. Manjula, A. Acharya, Y. J. Cho, 1988, Biochemistry.

Application of reductive dihydroxypropylation of amino groups of proteins in primary structural studies: identification of phenylthiohydantoin derivative of epsilon-dihydroxypropyl-lysine residues by high-performance liquid chromatography.

B. Manjula, A. Acharya, L. Sussman, 1984, Journal of chromatography.

Reductive hydroxyethylation of hemoglobin A. Functional properties of hemoglobin A selectively hydroxyethylated or dihydroxypropylated at the alpha-amino groups.

A. Acharya, L. Sussman, 1983, The Journal of biological chemistry.

Aldimine to ketoamine isomerization (Amadori rearrangement) potential at the individual nonenzymic glycation sites of hemoglobin a: Preferential inhibition of glycation by nucleophiles at sites of low isomerization potential

A. Acharya, R. P. Roy, R. Roy, 1991, Journal of protein chemistry.

Amadori rearrangement potential of hemoglobin at its glycation sites is dependent on the three-dimensional structure of protein.

A. Acharya, P. Nacharaju, 1992, Biochemistry.

Reactivity of the amino groups of carbonmonoxyhemoglobin S with glyceraldehyde.

A. Acharya, J. Manning, 1980, The Journal of biological chemistry.

Nonreductive Modification of Proteins by Glyceraldehyde a

A. Acharya, B. Dorai, Youngnan J. Cho, 1989 .

Schiff base adducts of glyceraldehyde with hemoglobin. Differences in the Amadori rearrangement at the alpha-amino groups.

A. Acharya, J. Manning, L. Sussman, 1983, The Journal of biological chemistry.

The reversibility of the ketoamine linkages of aldoses with proteins.

A. Acharya, L. Sussman, A., 1984, The Journal of biological chemistry.

Amadori rearrangement of glyceraldehyde-hemoglobin Schiff base adducts. A new procedure for the determination of ketoamine adducts in proteins.

A. Acharya, J. Manning, 1980, The Journal of biological chemistry.

Complete amino acid sequence of streptococcal PepM49 protein, a nephritis-associated serotype. Conserved conformational design among sequentially distinct M protein serotypes.

B. Trus, B. Manjula, A. Acharya, 1988, The Journal of biological chemistry.

Semisynthesis of hemoglobin.

A. Acharya, R. Roy, 1994, Methods in enzymology.

HbS-Savaria: The Anti-polymerization Effect of a Single Mutation in Human α-chains

M. Prabhakaran, A. Acharya, R. Nagel, 2007 .

The influence of esterification of carboxyl groups of ribonuclease-A on its structure and immunological activity.

B. Manjula, A. Acharya, P. Vithayathil, 2009, International journal of peptide and protein research.

Chemistry of the “molecular trap” of protease-catalyzed splicing reaction of complementary segments of α-subunit of hemoglobin A

A. Acharya, G. Sahni, S. Khan, 1998, Journal of protein chemistry.

Deamidated active intermediates in the irreversible acid denaturation of ribonuclease-A.

B. Manjula, A. Acharya, P. Vithayathil, 2009, International journal of peptide and protein research.

On the reactivity of carboxyl groups of ribonuclease-A in anhydrous methanol.

A. Acharya, P. Vithayathil, 2009, International journal of peptide and protein research.

Helix formation in enzymically ligated peptides as a driving force for the synthetic reaction: example of alpha-globin semisynthetic reaction.

B. Manjula, A. Acharya, R. P. Roy, 1992, Biochemistry.

Effects of S-Nitrosation and Cross-Linking of Hemoglobin on Hypoxic Pulmonary Vasoconstriction in Isolated Rat Lungs

M. Gladwin, B. Manjula, A. Acharya, 2002, Circulation research.

Product‐conformation‐driven ligation of peptides by V8 protease

A. Acharya, S. Srinivasulu, 2002, Protein science : a publication of the Protein Society.

On the mechanism of renaturation of proteins containing disulfide bonds.

A. Acharya, G. Andria, H. Taniuchi, 1977, Advances in experimental medicine and biology.

Symmetric interspecies hybrids of mouse and human hemoglobin: Molecular basis of their abnormal oxygen affinity

A. Acharya, R. Nagel, R. P. Roy, 1995, Journal of protein chemistry.

Reaction of glycolaldehyde with proteins: latent crosslinking potential of alpha-hydroxyaldehydes.

A. Acharya, J. Manning, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Selective carboxymethylation of the alpha-amino groups of hemoglobin. Effect on functional properties.

A. Acharya, W. Fantl, J. Manning, 1983, The Journal of biological chemistry.

Labeling of hemoglobin with pyridoxal phosphate.

A. Acharya, R. Benesch, J. Manning, 1982, The Journal of biological chemistry.

Pair-wise interactions of polymerization inhibitory contact site mutations of hemoglobin-S

B. Manjula, R. Upadhya, K. Perumalsamy, 2006, The protein journal.

Proteosynthetic activity of immobilized Staphylococcus aureus V8 protease: application in the semisynthesis of molecular variants of alpha-globin.

A. Acharya, G. Sahni, A. Mallia, 1991, Analytical biochemistry.

Interspecies hybrid HbS: complete neutralization of Val6(beta)-dependent polymerization of human beta-chain by pig alpha-chains.

D. P. Sun, B. Manjula, A. Malavalli, 2000, Journal of molecular biology.

Inhibition of βS-chain dependent polymerization by synergistic complementation of contact site perturbations of α-chain: application of semisynthetic chimeric α-chains

A. Malavalli, M. Prabhakaran, A. Acharya, 1999 .

Inhibition of Sickle β-Chain (βS)-dependent Polymerization by Nonhuman α-Chains

A. Acharya, R. Nagel, R. P. Roy, 1997, The Journal of Biological Chemistry.

Reaction of ribosomal sulfhydryl groups with 5,5'-dithiobis(2-nitrobenzoic acid).

A. Acharya, P. Moore, 1973, Journal of molecular biology.

Bissulfosuccinimidyl Esters of Aliphatic Dicarboxylic Acids: A New Class of ‘Affinity Directed’ ββ Crosslinkers of HbA

B. Manjula, A. Acharya, Paul K. Smith, 1994 .

Perturbation of the Intermolecular Contact Regions (Molecular Surface) of Hemoglobin S by Intramolecular, Low-O2-Affinity-Inducing Central Cavity Cross-Bridges

B. Manjula, A. Malavalli, J. Friedman, 2000, Journal of protein chemistry.

Semisynthetic hemoglobin A: reconstitution of functional tetramer from semisynthetic alpha-globin.

A. Acharya, G. Sahni, Y. J. Cho, 1989, Biochemistry.

Preparation of a two-disulfide bonded enzymically active derivative from hen egg lysozyme.

A. Acharya, H. Taniuchi, 2009, International journal of peptide and protein research.

Reduction and renaturation of hen egg lysozyme containing carboxymethylcysteine-6 and -127.

A. Acharya, H. Taniuchi, 1978, Biochemistry.

Extension Arm Facilitated PEGylation of Hemoglobin: Correlation of the Properties with the Extent of PEGylation

B. Manjula, A. Acharya, Dongxia Li, 2006, The protein journal.

Domain structure and molecular flexibility of streptococcal M proteinIn Situ probed by limited proteolysis

B. Manjula, A. Acharya, T. Fairwell, 1990, Journal of protein chemistry.

Influence of native disulfide bonds of globular proteins on their retention behavior on reverse phase supports

A. Acharya, 1986 .

Permissible discontinuity region of the alpha-chain of hemoglobin: noncovalent interaction of heme and the complementary fragments alpha 1-30 and alpha 31-141.

A. Acharya, R. Seetharam, K. Iyer, 1986, Biochemistry.

Cys-93-ββ-Succinimidophenyl Polyethylene Glycol 2000 Hemoglobin A

B. Manjula, A. Malavalli, J. Friedman, 2000, The Journal of Biological Chemistry.

Recombinant hemoglobin A produced in transgenic swine: structural equivalence with human hemoglobin A.

B. Chait, B. Manjula, A. Acharya, 1994, Artificial cells, blood substitutes, and immobilization biotechnology.

Activation of the low oxygen affinity-inducing potential of the Asn108(β)→Lys mutation of Hb-Presbyterian on intramolecular αα-fumaryl cross-bridging

B. Manjula, A. Malavalli, J. Friedman, 2001 .

Amidation of basic carboxyl groups of hemoglobin.

A. Acharya, M. J. Rao, 1994, Methods in enzymology.

Inhibition of deoxyhemoglobin S polymerization by glyceraldehyde.

A. Acharya, J. Manning, W. Jones, 1984, Analytical biochemistry.

Characterization of the particles produced by exposure of ribosomal subunits to urea.

A. Acharya, P. Moore, J. Langer, 1975, Biochimica et biophysica acta.

Selectivity in the modification of the alpha-amino groups of hemoglobin on reductive alkylation with aliphatic carbonyl compounds. Influence of derivatization on the polymerization of hemoglobin S.

A. Acharya, J. Manning, L. Sussman, 1985, The Journal of biological chemistry.

Reversible Dihydroxypropylation of Amino Groups in Proteins: Application in Primary Structural Studies of Streptococcal M-Proteins

B. Manjula, A. Acharya, V. Fischetti, 1987 .

Probing the Hemoglobin Central Cavity by Direct Quantification of Effector Binding Using Fluorescence Lifetime Methods*

J. Friedman, A. Acharya, D. Gottfried, 1997, The Journal of Biological Chemistry.

Biogenerics and biobetters v/s chemical based drugs - comparative discourse

A. Acharya, R. Basnet, A. Nagappa, 2018 .

Influence of trifluoroacetic acid on retention times of histidine-containing tryptic peptides in reverse phase HPLC.

B. Manjula, A. Acharya, V. Fischetti, 2009, International journal of peptide and protein research.

Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation

A. Acharya, H. Taniuchi, 1982, Molecular and Cellular Biochemistry.

Electrostatic modification at the amino termini of hemoglobin A.

A. Acharya, D. J. Bobelis, S. P. White, 1994, The Journal of biological chemistry.

Activation of the low oxygen affinity-inducing potential of the Asn108(beta)-->Lys mutation of Hb-Presbyterian on intramolecular alpha alpha-fumaryl cross-bridging.

B. Manjula, A. Malavalli, M. Prabhakaran, 2001, Protein Engineering.

Intramolecular cross-linking of oxy hemoglobin by bis sulfosuccinimidyl suberate and sebacate: generation of cross-linked hemoglobin with reduced oxygen affinity.

P. K. Smith, B. Manjula, A. Malavalli, 1995, Artificial cells, blood substitutes, and immobilization biotechnology.

Probing the diphosphoglycerate binding pocket of HbA and HbPresbyterian (beta 108Asn --> Lys).

B. Manjula, A. Malavalli, J. Friedman, 1999, Biochemistry.

Correct assembly of human normal adult hemoglobin when expressed in transgenic swine: chemical, conformational and functional equivalence with the human-derived protein.

D. P. Sun, B. Manjula, A. Malavalli, 1998, Protein engineering.

Influence of the chemical nature of side chain at beta 108 of hemoglobin A on the modulation of the oxygen affinity by chloride ions. Low oxygen affinity variants of human hemoglobin expressed in transgenic pigs: hemoglobins Presbyterian and Yoshizuka.

B. Manjula, A. Acharya, K. Sundarapandiyan, 1994, The Journal of biological chemistry.

Reactivity of Glu-22(beta) of hemoglobin S for amidation with glucosamine.

A. Acharya, R. Seetharam, 1985, Biochemistry.

Reductive hydroxyethylation of the α-amino groups of amidated hemoglobin S

A. Acharya, R. Seetharam, L. Sussman, 1985 .

Molecular basis of the inhibition of beta s-chain-dependent polymerization by mouse alpha-chain. Semisynthesis of chimeras of human and mouse alpha-chains.

A. Acharya, R. Nagel, R. P. Roy, 1993, The Journal of biological chemistry.

Basic carboxyl groups of hemoglobin S: Influence of oxy-deoxy conformation on the chemical reactivity of Glu-43(β)

A. Acharya, M. J. Rao, 1991, Journal of protein chemistry.

Selective amidation of carboxyl groups of the intermolecular contact regions of hemoglobin S: Structural aspects

A. Acharya, L. Khandke, 1989, Journal of protein chemistry.

Molecular Aspects of the High Oxygen Afinity of Non-Hypertensive Hexa Pegylated Hemoglobin, [(SP-PEG5K)6-Hb]

C. Ho, B. Manjula, A. Acharya, 2007, Artificial cells, blood substitutes, and immobilization biotechnology.

Contribution of the gamma-carboxyl group of Glu-43(beta) to the alkaline Bohr effect of hemoglobin A.

A. Acharya, M. J. Rao, 1992, Biochemistry.

Covalent semisynthesis of α-chain of hemoglobin: Protease-catalyzed transpeptidation at the permissible discontinuity site

A. Acharya, G. Sahni, Youngnan J. Cho, 1988 .