PUBLICATIONS from the Maillard Lab
Chau AK, Bracken K, Bai L, Pham D, Good LL, Maillard RA. (2023) Conformational changes in protein kinase A along its activation cycle are rooted in the folding energetics of cyclic-nucleotide binding domains. J Biol Chem. 299: 104790
Foroutannejad S, Good LL, Lin C, Carter ZI, Tadesse MG, Lucius AL, Crane BR, Maillard RA. (2023) The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments. Nat Commun 14, 1057
Bai L, Malmosi M, Good LL, Maillard RA. (2022) Using Optical Tweezers to Monitor Allosteric Signals Through Changes in Folding Energy Landscapes. Methods Mol Biol. 2478: 483-510
Hao Y, Maillard RA. (2022) Using Optical Tweezers to Dissect Allosteric Communication Networks in Protein Kinases. Methods Mol Biol. 2394: 485-498
Gárate F, Dokas S, Lanfranco M, Canavan C, Wang I, Correia JJ, Maillard RA. (2021) cAMP is an allosteric modulator of DNA binding-specificity in cAMP receptor protein from Mycobacterium tuberculosis. J Biol Chem. 296: 100480
Rivera, M., Hao, Y., Maillard RA.*, Baez M.* (2020) Mechanical unfolding of a knotted protein unveils the kinetic and thermodynamic consequences of threading a polypeptide. Sci Rep 10, 9562
*Co-corresponding authors
Hao Y, England JP, Bellucci L, Paci E, Hodges HC, Taylor SS, Maillard RA. (2019) Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains. Nat Commun 10, 3984
England JP, Hao Y, Bai L, Glick V, Hodges HC, Taylor SS, Maillard RA. (2018) Switching of the folding- energy landscape governs the allosteric activation of protein kinase A. Proc Natl Acad Sci U S A 115 (32): E7478-E7485
Hao Y, Canavan C, Taylor SS, Maillard RA. (2017) Integrated Method to Attach DNA Handles and Functionally Select Proteins to Study Folding and Protein-Ligand Interactions with Optical Tweezers. Scientific Reports 7 (1): 10843
Selected Editor’s Choice on Optical Trapping and Manipulation (link here)
Lanfranco MF, Gárate F, Engdahl AJ, Maillard RA. (2017) Asymmetric configurations in a reengineered homodimer reveal multiple subunit communication pathways in protein allostery. J Biol Chem. 292 (15): 6086-6093
Selected Editor’s Pick, Herbert Tabor Young Investigator Awardee (links here and here) and highlighted in F1000
Maillard RA*, Liu T, Beasley DW, Barrett AD, Hilser V. and Lee JC*. (2014) Thermodynamic Mechanism for the Resistance to Antibody Neutralization in Flaviviruses. JACS (136): 10315-10324
* Co-corresponding authors
PUBLICATIONS in Single Molecule Biophysics (as a postdoc)
Bustamante CJ, Kaiser CM, Maillard RA, Goldman DH, Wilson CA. (2014) Mechanisms of cellular proteostasis: insights from single-molecule approaches. Annu Rev Biophys 43: 119-40
Sen M*, Maillard RA*, Nyquist K*, Rodriguez-Aliaga P, Pressé S, Martin A, Bustamante C. (2013) The ClpXP protease unfolds substrates using a constant rate of pulling but different gears. Cell 155 (3): 636-646
* Authors contributed equally to this work.
Maillard RA, Chistol G, Sen M, Righini M, Tan J, Kaiser CM, Hodges C, Martin A, Bustamante C. (2011) ClpX(P) generates mechanical force to unfold and translocate its protein substrates. Cell 29 (3): 459-469
PUBLICATIONS in Protein Allostery (as a graduate student)
Yu S, Maillard RA, Gibenko AV, Lee JC. (2012) The N-terminal capping propensities of the D-helix modulate the allosteric activation of the Escherichia coli cAMP receptor protein. J. Biol. Chem. 287 (47): 39402-39411
Zhang S, Evgeniy I, Maillard R, Gromowski G, Volk D, Schein C, Huang C, Gorenstein D, Lee JC, Barrett AD, Beasley DW. (2010) Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III. Virology 403 (1): 85-91
Maillard RA, Jordan M, Beasley DW, Barrett AD, Lee JC. (2008) Long range communication in the envelope protein domain III and its effect on the resistance of West Nile virus to antibody-mediated neutralization. J. Biol. Chem. 283 (1): 613-622
Galletto R, Maillard R, Jezewska MJ and Bujalowski W. (2004) Global conformation of the Escherichia coli replication factor DnaC protein in absence and presence of nucleotide cofactors. Biochemistry 43 (34): 10988-11001
Galletto R, Jezewska MJ, Maillard R and Bujalowski W. (2005) The nucleotide-binding site of the Escherichia coli DnaC protein: molecular topography of DnaC protein-nucleotide cofactor complexes. Cell Biochemistry and Biophysics 43 (3): 331-353
© 2023 Maillard Lab.
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