Madan Lab - Publications

Protein Mechanisms & Allostery Laboratory

Understanding Life's Chemistry, One Protein at a Time

Link to lab publications:

GOOGLE SCHOLAR: https://scholar.google.co.in/citations?user=PnM5oyUAAAAJ&hl=en

RESEARCH GATE: https://www.researchgate.net/profile/Lalima-K-Madan

Overview of our research using figures from selected publications:

Fig 2. Protein Tyrosine Phosphatases as negative and positive regulators of phosphorylation based signaling.

Adv Cancer Res 2021;152:263-303. PMID: 34353440 PMCID: PMC10544742

Fig 6. Community network at the activation segment of the 7 kinase:peptide complexes. The community network at activation segment is seen to vary in the 7 kinase:peptide complexes in accordance with the signatures of their molecular recognition.

Proc Natl Acad Sci U S A 2019 Jul 23;116(30):15052-15061. PMID: 31285328 PMCID: PMC6660753

Fig 2. The conserved kinase core harbors a hydrophobic motif known as the regulatory or R-spine. An assembled R-spine is the signature of the “active” kinase conformation. This assembly and disassembly of the R-spine in accordance with effects like activation loop phosphorylation and kinase dimerization forms a conformation-based allosteric descriptor of protein kinase activation.

IUBMB Life 2019 Jun;71(6):685-696. PMID: 31063633 PMCID: PMC6690483

Fig 4. Dynamics of pseudosubstrate binding at the PKA active-site cleft. (A) Pseudosubstrate peptide interacting residues at the PKA active-site cleft. (B) Stability of apo, binary (protein:nucleotide), and ternary (protein:nucleotide:pseudosubstrate) states of wtPKA and Y204A mutant as seen by differentialscanning fluorimetry.

Proc Natl Acad Sci U S A 2017 Feb 7;114(6):E931-E940. PMID: 28115705 PMCID: PMC5307475

Figure 4. Phosphatase assays and time course measurements on PTP10D a. Michealis-Menten kinetics for the phosphatase activity of PTP10D and the F76L mutant with various substrates. b. Time course measurements to ascertain the life time of the phosphatase reaction as catalyzed by PTP10D and the F76L mutant.

Biochemistry 2011 Nov 22;50(46):10114-25. PMID: 22007620 PMCID: PMC3667199

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