H. Balaram

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Crystal structure of fully ligated adenylosuccinate synthetase from Plasmodium falciparum.

M. Murthy, K. Eaazhisai, R. Jayalakshmi, 2004, Journal of molecular biology.

Solution nuclear magnetic resonance structure of the GATase subunit and structural basis of the interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.

H. Balaram, Rustam Ali, Sanjeev Kumar, 2013, Biochemistry.

Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design.

H. Balaram, S. Ray, P. Balaram, 1997, Structure.

Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state.

S. Parthasarathy, M. Murthy, H. Balaram, 2002, Biochemistry.

Subunit interface mutation disrupting an aromatic cluster in Plasmodium falciparum triosephosphate isomerase: effect on dimer stability.

Hemalatha Balaram, H. Balaram, P. Balaram, 2002, Protein engineering.

Perspectives in drug design against malaria.

Hemalatha Balaram, Jayalakshmi Raman, H. Balaram, 2002, Current topics in medicinal chemistry.

Biochemical and physiological investigations on adenosine 5ʹ monophosphate deaminase from Plasmodium spp.

H. Balaram, Kota Arun Kumar, S. Dey, 2019, Molecular microbiology.

Proteolytic stability of β‐peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site

H. Balaram, P. Balaram, P. Pattanaik, 2003, FEBS letters.

Identification and characterization of a library of microheterogeneous cyclohexadepsipeptides from the fungus Isaria.

H. Balaram, P. Balaram, V. Sabareesh, 2007, Journal of natural products.

Mechanistic insights into the functioning of GMP synthetase: a two-subunit, allosterically regulated, ammonia tunnelling enzyme

H. Balaram, Sanjeev Kumar, Santosh Shivakumaraswamy, 2022, bioRxiv.

Structure of triosephosphate isomerase (TIM) from Methanocaldococcus jannaschii.

M. Murthy, P. Gayathri, H. Balaram, 2007, Acta crystallographica. Section D, Biological crystallography.

Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase

H. Balaram, P. Balaram, M. Banerjee, 2009, The FEBS journal.

Prediction of substrate specificity and preliminary kinetic characterization of the hypothetical protein PVX_123945 from Plasmodium vivax.

H. Balaram, B. Srinivasan, Arpit Shukla, 2015, Experimental parasitology.

Structure and catalytic regulation of Plasmodium falciparum IMP specific nucleotidase

H. Balaram, B. Srinivasan, Arpit Shukla, 2020, Nature Communications.

Revisiting the burden borne by fumarase: enzymatic hydration of an olefin

H. Balaram, P. Balaram, S. Balasubramanian, 2022, bioRxiv.

Mechanistic Insights into the Functioning of a Two-Subunit GMP Synthetase, an Allosterically Regulated, Ammonia Channeling Enzyme.

H. Balaram, Sanjeev Kumar, Santosh Shivakumaraswamy, 2022, Biochemistry.

Tertiary and Quaternary Structure Organization in GMP Synthetases: Implications for Catalysis

H. Balaram, F. Galisson, N. Aghajari, 2022, Biomolecules.

Nuclear Overhauser Effects and circular Dichroism as Probes of \beta.-turn Conformations in Acyclic and Cyclic Peptides with Pro-X Sequences

H. Balaram, P. Balaram, Anilesh Kumar, 1983 .

Peptide models for beta-turns. A circular dichroism study.

M. Crisma, H. Balaram, P. Balaram, 1984, International journal of peptide and protein research.

Alpha-helix and mixed 3(10)/alpha-helix in cocrystallized conformers of Boc-Aib-Val-Aib-Aib-Val-Val-Val-Aib-Val-Aib-OMe.

J. Flippen-Anderson, I. Karle, H. Balaram, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Comparison of the Effect of Five Guest Residues on the \beta-Sheet Conformation of Host ${(L-Val)}_n$ Oligopeptides

C. Toniolo, M. Crisma, H. Balaram, 1989 .

Stereochemistry of α‐aminoisobutyric acid peptides in solution: Conformations of decapeptides with a central triplet of contiguous L‐amino acids

H. Balaram, P. Balaram, M. Sukumar, 1986 .

Kinetic mechanism of Plasmodium falciparum hypoxanthine-guanine-xanthine phosphoribosyltransferase.

H. Balaram, Sourav Roy, L. K. Nagappa, 2015, Molecular and biochemical parasitology.

Antimalarial Activities of Peptide Antibiotics Isolated from Fungi

H. Balaram, G. Nagaraj, M. S. Shivayogi, 2001, Antimicrobial Agents and Chemotherapy.

Product Release Pathways in Human and Plasmodium falciparum Phosphoribosyltransferase

Meher K. Prakash, Hemalatha Balaram, Tarak Karmakar, 2016, J. Chem. Inf. Model..

Structural and dynamical correlations in PfHGXPRT oligomers: A molecular dynamics simulation study

H. Balaram, S. Balasubramanian, T. Karmakar, 2016, Journal of biomolecular structure & dynamics.

Unusual stability of a multiply nicked form of Plasmodium falciparum triosephosphate isomerase.

H. Balaram, S. Ray, P. Balaram, 1999, Chemistry & biology.

Development and characterization of lysine based tripeptide analogues as inhibitors of Sir2 activity.

H. Balaram, Roli Mishra, S. Chandrasekaran, 2009, Bioorganic & medicinal chemistry.

Metabolic Fate of Fumarate, a Side Product of the Purine Salvage Pathway in the Intraerythrocytic Stages of Plasmodium falciparum*

H. Balaram, V. Jayaraman, V. Bulusu, 2011, The Journal of Biological Chemistry.

Multiple conformational states of a Pro-Pro peptide. Solid-state and solution conformations of Boc-Aib-Pro-Pro-NHMe

H. Balaram, P. Balaram, B. Prasad, 1983 .

Unusual substrate specificity of a chimeric hypoxanthine-guanine phosphoribosyltransferase containing segments from the Plasmodium falciparum and human enzymes.

H. Balaram, S. Sukumaran, K. Shivashankar, 2000, Biochemical and biophysical research communications.

Acyclic peptides as conformational models Crystal structure of Boc-Aib-Leu-Pro-NHMe± 2H2O

H. Balaram, B. Prasad, P. Balaram, 2009 .

Elucidation of the substrate specificity, kinetic and catalytic mechanism of adenylosuccinate lyase from Plasmodium falciparum.

H. Balaram, B. Srinivasan, V. Bulusu, 2009, Biochimica et biophysica acta.

Kinetic and biochemical characterization of Plasmodium falciparum GMP synthetase.

H. Balaram, J. Bhat, B. Shastri, 2008, The Biochemical journal.

Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site.

M. Murthy, P. Gayathri, H. Balaram, 2009, Acta crystallographica. Section D, Biological crystallography.

Structure of Plasmodium falciparum Triose-phosphate Isomerase-2-Phosphoglycerate Complex at 1.1-Å Resolution*

S. Parthasarathy, M. Murthy, K. Eaazhisai, 2003, Journal of Biological Chemistry.

Allosteric regulation and substrate activation in cytosolic nucleotidase II from Legionella pneumophila

G. Montelione, H. Balaram, T. Acton, 2014, The FEBS journal.

Biochemical and physiological investigations on adenosine 5’ monophosphate deaminase from Plasmodium spp.

H. Balaram, L. K. Nagappa, L. Nagappa, 2018, bioRxiv.

Toward Developing Intuitive Rules for Protein Variant Effect Prediction Using Deep Mutational Scanning Data

Hemalatha Balaram, C. K. Sruthi, Meher K. Prakash, 2020, ACS omega.

Visualizing Deep Mutational Scan Data

Meher K. Prakash, Hemalatha Balaram, C. K. Sruthi, 2018, bioRxiv.

Inhibition of Plasmodium falciparum Triose-phosphate Isomerase by Chemical Modification of an Interface Cysteine

H. Balaram, P. Balaram, G. Ravindra, 2002, The Journal of Biological Chemistry.

Application of HPLC to study the kinetics of a branched bi-enzyme system consisting of hypoxanthine-guanine phosphoribosyltransferase and xanthine oxidase--an important biochemical system to evaluate the efficiency of the anticancer drug 6-mercaptopurine in ALL cell line.

H. Balaram, M. Paul, A. Mukhopadhyay, 2007, Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.

A point mutation at the subunit interface of hypoxanthine–guanine–xanthine phosphoribosyltransferase impairs activity: role of oligomerization in catalysis

H. Balaram, I. Subbayya, 2002, FEBS letters.

Hypoxanthine guanine phosphoribosyltransferase distorts the purine ring of nucleotide substrates and perturbs the pKa of bound xanthosine monophosphate.

H. Balaram, Mrinalini Puranik, S. Gogia, 2011, Biochemistry.

Connecting Active‐Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme

M. Murthy, H. Balaram, P. Balaram, 2016, Chembiochem : a European journal of chemical biology.

Engineered dimer interface mutants of triosephosphate isomerase: the role of inter-subunit interactions in enzyme function and stability.

H. Balaram, P. Balaram, M. Banerjee, 2011, Protein engineering, design & selection : PEDS.

Synthetic peptides as inactivators of multimeric enzymes: inhibition of Plasmodium falciparum triosephosphate isomerase by interface peptides

H. Balaram, P. Balaram, K. Maithal, 2001, FEBS letters.

Peptide design: Influence of a guest Aib‐Pro segment on the stereochemistry of an Oligo‐Val sequence—solution conformations and crystal structure of Boc‐(Val)2‐Aib‐Pro‐(Val)3‐OMe

J. Flippen-Anderson, I. Karle, H. Balaram, 1990, Biopolymers.

Methanocaldococcus jannaschii adenylosuccinate synthetase: studies on temperature dependence of catalytic activity and structural stability.

H. Balaram, Sonali Mehrotra, 2008, Biochimica et biophysica acta.

A Histidine Aspartate Ionic Lock Gates the Iron Passage in Miniferritins from Mycobacterium smegmatis*

S. Vishveshwara, H. Balaram, M. Vijayan, 2014, The Journal of Biological Chemistry.

Structural and kinetic studies on adenylosuccinate lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzyme

M. Murthy, H. Balaram, Sanchari Banerjee, 2014, The FEBS journal.

1H, 13C, 15N assignment and secondary structure determination of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii

H. Balaram, Rustam Ali, Sanjeev Kumar, 2012, Biomolecular NMR assignments.

1H, 13C, 15N assignment and secondary structure determination of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii

H. Balaram, Rustam Ali, S. Sarma, 2011, Biomolecular NMR Assignments.

Role of loop dynamics in thermal stability of mesophilic and thermophilic adenylosuccinate synthetase: a molecular dynamics and normal mode analysis study.

H. Balaram, S. Vemparala, Sonali Mehrotra, 2011, Biochimica et biophysica acta.

Active site coupling in Plasmodium falciparum GMP synthetase is triggered by domain rotation

H. Balaram, B. Dijkstra, R. Haser, 2015, Nature Communications.

Leptospira interrogans triosephosphate isomerase: exploring the structural determinants of stability, high reaction rate and specificity

H. Balaram, V. Pareek, P. Krishnaswamy, 2020, bioRxiv.

Probing the influence of non-covalent contact networks identified by charge density analysis on the oxidoreductase BacC

T. N. Guru Row, H. Balaram, B. Gopal, 2017, Protein engineering, design & selection : PEDS.

Differential Distortion of Purine Substrates by Human and Plasmodium falciparum Hypoxanthine-Guanine Phosphoribosyltransferase to Catalyse the Formation of Mononucleotides.

H. Balaram, Mrinalini Puranik, S. Gogia, 2015, Chemphyschem : a European journal of chemical physics and physical chemistry.

Stage-specific profiling of Plasmodium falciparum proteases using an internally quenched multispecificity protease substrate.

H. Balaram, P. Balaram, P. Pattanaik, 2003, Biochemical and biophysical research communications.

Reversible binding of zinc in Plasmodium falciparum Sir2: structure and activity of the apoenzyme.

H. Balaram, S. Chakrabarty, 2010, Biochimica et biophysica acta.

Plasmodium falciparum hypoxanthine guanine phosphoribosyltransferase

R. Anand, H. Balaram, Jayalakshmi Raman, 2005, The FEBS journal.

Biochemical characterization of Plasmodium falciparum Sir2, a NAD+-dependent deacetylase.

H. Balaram, Y. K. Saikumari, M. P. Bopanna, 2008, Molecular and biochemical parasitology.

Metabolic enzymes as potential drug targets in Plasmodium falciparum.

H. Balaram, S. Ray, P. Balaram, 1997, The Indian journal of medical research.

Crosstalk between purine nucleotide metabolism and mitochondrial pathways in Plasmodium falciparum

H. Balaram, V. Jayaraman, V. Bulusu, 2012 .

Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site‐specific mutagenesis – distal effects on dimer stability

M. Murthy, H. Balaram, P. Balaram, 2011, The FEBS journal.

Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli.

R. Jayalakshmi, K. Sumathy, H. Balaram, 2002, Protein expression and purification.

Cloning of the triosephosphate isomerase gene of Plasmodium falciparum and expression in Escherichia coli.

H. Balaram, Vidya P Kumar, J. Ranie, 1993, Molecular and biochemical parasitology.

Biochemical characterization and essentiality of Plasmodium fumarate hydratase

H. Balaram, V. Jayaraman, Arpitha Suryavanshi, 2017, The Journal of Biological Chemistry.

Slow ligand-induced conformational switch increases the catalytic rate in Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase.

H. Balaram, S. Balasubramanian, T. Karmakar, 2015, Molecular bioSystems.

Stability studies on the product-activated enzyme

R. Anand, H. Balaram, S. Selvi, 2005 .

A non-active site mutation in human hypoxanthine guanine phosphoribosyltransferase expands substrate specificity.

R. Anand, K. Sumathy, H. Balaram, 2004, Archives of biochemistry and biophysics.

Unusual fluorescence of W168 in Plasmodium falciparum triosephosphate isomerase, probed by single-tryptophan mutants.

H. Balaram, P. Balaram, P. Pattanaik, 2003, European journal of biochemistry.

Unique kinetic mechanism of Plasmodium falciparum adenylosuccinate synthetase.

R. Anand, H. Balaram, Jayalakshmi Raman, 2004, Molecular and biochemical parasitology.

Structural basis for the hyperthermostability of an archaeal glutaminase induced by post-translational succinimide formation

H. Balaram, P. Balaram, S. Balasubramanian, 2021, bioRxiv.

Structural biology of plasmodial proteins.

M. Murthy, P. Gayathri, H. Balaram, 2007, Current opinion in structural biology.

Probing the role of highly conserved residues in triosephosphate isomerase – analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzyme

M. Murthy, H. Balaram, D. Bandyopadhyay, 2015, The FEBS journal.

Ammonia channeling in Plasmodium falciparum GMP synthetase: investigation by NMR spectroscopy and biochemical assays.

H. Balaram, Kallol Gupta, S. Sarma, 2011, Biochemistry.

Mutational analysis of cysteine 328 and cysteine 368 at the interface of Plasmodium falciparum adenylosuccinate synthetase.

R. Anand, H. Balaram, Jayalakshmi Raman, 2012, Biochimica et biophysica acta.

Substrate‐induced conformational changes in Plasmodium falciparum guanosine monophosphate synthetase

H. Balaram, J. Bhat, Roopa Venkatachala, 2011, The FEBS journal.

Adenine metabolism in Plasmodium falciparum.

H. Balaram, V. Bulusu, M. P. Bopanna, 2010, Experimental parasitology.

Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state.

S. Parthasarathy, M. Murthy, H. Balaram, 2002, Acta crystallographica. Section D, Biological crystallography.

Evidence for multiple active states of Plasmodium falciparum hypoxanthine-guanine-xanthine phosphoribosyltransferase.

H. Balaram, I. N. Sujay Subbayya, 2000, Biochemical and biophysical research communications.

Conformational transitions in a Pro-Pro peptide on dissolution of single crystals.

H. Balaram, P. Balaram, B. V. Enkatara Prasad, 1982, Biochemical and biophysical research communications.

Type II β‐turn conformation of pivaloyl‐L‐prolyl‐α‐aminoisobutyryl‐N‐methylamide: Theoretical, spectroscopic, and X‐ray studies

H. Balaram, P. Balaram, B. Prasad, 1982 .

Simultaneous observation of positive and negative nuclear Overhauser effects in oligopeptides due to segmental motion.

H. Balaram, P. Balaram, S. Raghothama, 1988, Biochemical and biophysical research communications.

Helices on Interdomain Interface Couple Catalysis in the ATPPase Domain with Allostery in Plasmodium falciparum GMP Synthetase

H. Balaram, N. Aghajari, L. Ballut, 2020, Chembiochem : a European journal of chemical biology.

Interactions of helices on interdomain interface couple the chemistry of intermediate formation with allostery in Plasmodium falciparum GMP synthetase

H. Balaram, N. Aghajari, L. Ballut, 2019, bioRxiv.

Revisiting the Mechanism of the Triosephosphate Isomerase Reaction: The Role of the Fully Conserved Glutamic Acid 97 Residue

H. Balaram, P. Balaram, M. Murthy, 2011, Chembiochem : a European journal of chemical biology.

Synthetic peptide models for protein secondary structures. Beta-sheet formation in acyclic cystine peptides.

H. Balaram, P. Balaram, K. Uma, 2009, International journal of peptide and protein research.

Structures of Pivaloyl-L-prolyl-N-methyl-D- phenylalaninamide and Pivaloyl-L-prolyl-N-methyl-D-valinamide

C. Toniolo, H. Balaram, P. Balaram, 1988 .

Unexpected functional implication of a stable succinimide in the structural stability of Methanocaldococcus jannaschii glutaminase

H. Balaram, P. Balaram, Kallol Gupta, 2016, Nature Communications.

Mechanism of growth inhibition of intraerythrocytic stages of Plasmodium falciparum by 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR).

H. Balaram, S. Thakur, V. Bulusu, 2011, Molecular and biochemical parasitology.

Kinetic characterization of adenylosuccinate synthetase from the thermophilic archaea Methanocaldococcus jannaschii.

H. Balaram, Sonali Mehrotra, 2007, Biochemistry.

Exquisite Modulation of the Active Site of Methanocaldococcus jannaschii Adenylosuccinate Synthetase in Forward Reaction Complexes.

H. Balaram, Mrinalini Puranik, Vishakha Karnawat, 2016, Biochemistry.

Studies on active site mutants of P. falciparum adenylosuccinate synthetase: insights into enzyme catalysis and activation.

H. Balaram, Sonali Mehrotra, B. N. Mylarappa, 2010, Biochimica et biophysica acta.

ISN1 Nucleotidases and HAD Superfamily Protein Fold: In silico Sequence and Structure Analysis

Bharath Srinivasan, Hemalatha Balaram, H. Balaram, 2007, Silico Biol..

Structures of unliganded and inhibitor complexes of W168F, a Loop6 hinge mutant of Plasmodium falciparum triosephosphate isomerase: observation of an intermediate position of loop6.

M. Murthy, K. Eaazhisai, H. Balaram, 2004, Journal of molecular biology.

Role of W181 in modulating kinetic properties of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase

H. Balaram, S. Balasubramanian, T. Karmakar, 2016, Proteins.

Biochemical characterization and essentiality of Plasmodium fumarate hydratase

H. Balaram, V. Jayaraman, Arpitha Suryavanshi, 2017, Journal of Biological Chemistry.

Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii.

H. Balaram, P. Balaram, Kallol Gupta, 2011, Rapid communications in mass spectrometry : RCM.

Peptide models for b-turns.A circular dichroism study

G. Fasman, M. Crisma, H. Balaram, 2009 .

Product Release Pathways in Human and Plasmodium falciparum Phosphoribosyltransferase

H. Balaram, M. Prakash, S. Balasubramanian, 2016, Journal of Chemical Information and Modeling.

Phosphoglycolate phosphatase is a metabolic proofreading enzyme essential for cellular function in Plasmodium berghei

H. Balaram, T. Govindaraju, P. Satha, 2019, The Journal of Biological Chemistry.

Metabolic proof-reading in Plasmodium berghei: essentiality of phosphoglycolate phosphatase

H. Balaram, T. Govindaraju, P. Satha, 2018, bioRxiv.

Peptide design: Influence of a guest Aib‐Pro segment on the stereochemistry of an Oligo‐Val sequence—solution conformations and crystal structure of Boc‐(Val)2‐Aib‐Pro‐(Val)3‐OMe

J. Flippen-Anderson, H. Balaram, K. Uma, 1990, Biopolymers.

Amino Acid Chirality: Stereospecific Conversion and Physiological Implications

H. Balaram, K. Sanyal, Kuladeep Das, 2024, ACS omega.