ORCID ID: https://orcid.org/0000-0003-4039-5863
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Soto J, Moro,SL, Cocco MJ* (2024) Dynamics of the Bypass Polymerase, DinB Homolog (Dbh) Frontiers Molecular Biosciences Structural Biology, 11-2024. https://doi.org/10.3389/fmolb.2024.1364068
Barros EP, Demir O, Soto, J, Cocco MJ, Amaro, RE (2021) Markov State Models and NMR Uncover an Overlooked Allosteric Loop in p53, Chem. Sci., 12:1891-1900. https://doi.org/10.1039/D0SC05053A
Tifrea DF, Pal S, le Bon C,Cocco MJ, Zoonens M, de la Maza LM (2020) Improved protection against Chlamydia muridarum using the native major outer membrane protein trapped in Resiquimod-carrying amphipols and effects in protection with addition of a Th1 (CpG-1826) and a Th2 (Montanide ISA 720) adjuvant. Vaccine, 38:4412-22. https://doi.org/10.1016/j.vaccine.2020.04.065
Tifrea, DF, Pal, S, Le Bon, C, Guisti, F, Popot, J-L, Cocco, MJ, Zoonens, M, de la Maza, LM (2018) Co-delivery of amphipol-conjugated adjuvant with antigen, and adjuvant combinations, enhance immune protection elicited by a membrane protein-based vaccine against a mucosal challenge with Chlamydia. Vaccine, 36:6640-9. https://doi.org/10.1016/j.vaccine.2018.09.055
Moro, S. and Cocco, MJ*. (2015) (1)H, (13)C, and (15)N backbone resonance assignments of the full-length 40 kDa S. acidocaldarius Y-family DNA polymerase, dinB homolog. Biomolecular NMR Assignments, 9: 441-5. https://doi.org/10.1007/s12104-015-9626-y
Feinstein, HE, Tifrea, DF, Popot, J-L, de la Maza, LM, Cocco, MJ*. (2014) Long-term stability of a vaccine formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis. J. Membrane Biology, 247:1053-65. https://doi.org/10.1007/s00232-014-9693-5
Alhoshani, A,Vithayathil R, Bandong J, Chrunyk, KM, Moreno, GO, Weiss, GA and Cocco, MJ*. (2014) Glutamate is a Key Structural Contact Between Nogo-66 and Phosphocholine. BBA – Biomembranes, 1838: 2350-6. https://doi.org/10.1016/j.bbamem.2014.05.021
Tifrea, DF, Pal, S, Cocco, MJ, Popot, J-L and de la Maza, LM. (2014) Increased immuno accessibility of MOMP epitopes in a vaccine formulated with amphipols may account for the very robust protection elicited against a vaginal challenge with C. muridarum. J. Immunology, 192: 5201-13. https://doi.org/10.4049/jimmunol.1303392
Vithayathil R, Hooy RM, Cocco MJ, Weiss GA. (2011) The Scope of phage display for membrane proteins. J. Mol. Biol. 414:499-510. https://doi.org/10.1016/j.jmb.2011.10.021
Popot JL, Althoff T, Bagnard D, Banères JL, Bazzacco P, Billon-Denis E, Catoire LJ, Champeil P, Charvolin D, Cocco MJ, Crémel G, Dahmane T, de la Maza LM, Ebel C, Gabel F, Giusti F, Gohon Y, Goormaghtigh E, Guittet E, Kleinschmidt JH, Kühlbrandt W, Le Bon C, Martinez KL, Picard M, Pucci B, Sachs JN, Tribet C, van Heijenoort C, Wien F, Zito F, Zoonens M. (2011) Amphipols from A to Z. Annu Rev Biophys. 2011 40:379-408. https://doi.org/10.1146/annurev-biophys-042910-155219
Moody, CL, Tretyachenko-Ladokhina, V, Laue, T., Senear, DF and Cocco, MJ* (2011) Multiple Conformations of the Cytidine Repressor DNA-Binding Domain Coalesce to One Upon Recognition of a Specific DNA Surface. Biochemistry, 50:6622-32. https://doi.org/10.1021/bi200205v
Tifrea, DF, Sun, G, Pal, S, Zardeneta1, G, Cocco, MJ, Popot, J-L, de la Maza, LM (2011) Amphipols stabilize the Chlamydia major outer membrane protein and enhance vaccine protection based on a membrane-protein formulation. Vaccine 29:4623-31. https://doi.org/10.1016/j.vaccine.2011.04.065
Corbin-Lickfett, KA, Souki, SK, Li, L, Cocco, MJ and Sandri-Goldin, RM. (2010) Three arginine residues within the RGG-box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export. Journal of Virology, 84:6367-76. https://doi.org/10.1128/jvi.00509-10
Vasudevan, SV, Schulz, J, Zhou, C and Cocco, MJ* (2010) Protein Folding at the Membrane Interface, the Structure of Nogo-66. Proceedings of the National Academy of Sciences, 107:6847-51.https://doi.org/10.1073/pnas.0911817107
Corbin-Lickfett, KA, Rojas, S, Li, L, Cocco, MJ and Sandri-Goldin, RM. (2010) ICP27 Phosphorylation Site Mutants Display Altered Functional Interactions with Cellular Export Factors Aly/REF and TAP/NXF1 but Are Able to Bind Herpes Simplex Virus 1 RNA. Journal of Virology, 84:2212-22. https://doi.org/10.1128/jvi.01388-09
Corbin-Lickfett, KA, Chen, I-HB, Cocco, MJ* and Sandri-Goldin, RM* (2009) The HSV-1 ICP27 RGG box specifically binds flexible, GC-rich sequences but not G-quartet structures. Nucleic Acids Research, 37:7290-301. https://doi.org/10.1093/nar/gkp793
Llenado, RA, Weeks, CS, Cocco, MJ and Ouellette, AJ (2009) Electropositive charge in α-Defensin Bactericidal Activity: Functional Effects of Arg→Lys Substitutions Vary with Peptide Primary Structure. Infection and Immunity, 77:5035-43. https://doi.org/10.1128/iai.00695-09
Sasaki, H, Arai, H, Cocco, MJ and White, SH (2008) pH-Dependence of Sphingosine Aggregation, Biophysical Journal, 96:2727-33. https://doi.org/10.1016/j.bpj.2008.12.3926
Vasudevan, S, Yuan, J, Ösapay, G, Tran, P, Tai, K, Liang, W, Kumar, V, Selsted, ME*, and Cocco, MJ*(2008) Synthesis, Structure and Activities of an Oral Mucosal Alpha-Defensin from Rhesus Macaque, Journal of Biological Chemistry, 283:35869-77. https://doi.org/10.1074/jbc.m806915200
Gehman, JD, Cocco, MJ and Grindley, ND (2008) Chemical Shift Mapping of gd resolvase Dimer and Activated Tetramer: Mechanistic Implications for DNA Strand Exchange. BBA – Proteins and Proteomics1784:2086-92. https://doi.org/10.1016/j.bbapap.2008.08.023
Liu D, Ren D, Huang, H, Dankberg, J, Rosenfeld, R, Cocco, MJ, Li, L, Brems, DN, and Remmele, RL (2008) Structure and Stability Changes of Human IgG1 Fc as a Consequence of Methionine Oxidation.Biochemistry 47: 5088-5100. https://doi.org/10.1021/bi702238b
LiuD, Cocco, MJ, Matsumura M, Ren D, Becker, B, Remmele, RL and Brems, DN (2007) Assignment of backbone (1)H, (13)C and (15)N resonances of human IgG1 Fc (51.4 kDa). Biomolecular NMR Assignments 1: 233-235. https://doi.org/10.1007/s12104-007-9065-5
Liu D, Cocco, MJ, Matsumura M, Ren D, Becker, B, Remmele, RL and Brems, DN (2007) Assignment of backbone resonances of the reduced human IgG1 CH3 domain. Biomolecular NMR Assignments 1: 93-94. https://doi.org/10.1007/s12104-007-9026-z
Sun, G, Pal, S, Sarcon, AK, Kim, S, Sugawara, E, Nikaido, H, Cocco, MJ, Ellena M. Peterson, EM, de la Maza, LM (2007) Structural and functional analyses of the major outer membrane protein of Chlamydia trachomatis. Journal of Biological Chemistry, 189: 6222-35. https://doi.org/10.1128/jb.00552-07
Levin, A., Coroneus, J., Cocco, MJ., and Weiss, G. (2006) “Exploring the Interaction between the Protein Kinase A Catalytic Subunit and Caveolin-1 Scaffolding with Shotgun Scanning, Oligomer Complementation, NMR, and Docking” Protein Science, 15: 478-86. https://doi.org/10.1110/ps.051911706
Weeks, C, Tanabe, H, Cuymmings, JE, Crampton, SP, Sheynis, T, Jelinek, R, Vanderlick, TK, Cocco, MJ, Ouellette, AJ. (2006) Matrix metalloproteinase-7 activation of mouse paneth cell Pro-alpha-defensins: Ser43*↓Ile44 proteolysis enables membrane disruptive activity. Journal of Biological Chemistry, 281: 28932-42. https://doi.org/10.1074/jbc.m602041200
Tretyachenko-Ladokhina, V, Cocco, MJ, Senear, DF, (2006) Flexibility and Adaptability in Binding of E. coli Cytidine Repressor to Different Operators Suggests a Role in Differential Gene Regulation. Journal of Molecular Biology, 362: 271-86. https://doi.org/10.1016/j.jmb.2006.06.085
Kamtekar, S, Ho, RS, Cocco, MJ, Li, W, Wenwieser, SVCT, Boocock, MR, Grindley, NDF, Steitz, TA, (2006) Implications of Structure of Synaptic Tetramers of gd Resolvase for the Mechanism of Recombination. Proceedings of the National Academy of Sciences, 103: 10642-7. https://doi.org/10.1073/pnas.0604062103
Tanabe, H, Ouellette, AJ, Cocco, MJ and Robinson, WE. (2004) Differential Effects on Human Immunodificiency Virus Type 1 Replication by -Defensins of Comparable Bactericidal Activities. Journal of Virology, 78: 11622-31. https://doi.org/10.1128/jvi.78.21.11622-11631.2004
Cortajarena, AL, Kajander, T, Pan, W, Cocco, MJ, and Regan, L. (2004) Protein Design to Understand Peptide Ligand Recognition by Tetratricopeptide Repeat Proteins. Protein Design Engineering and Selection, 17: 399-409. https://doi.org/10.1093/protein/gzh047
Cocco, MJ*, Hanakahi, L, Huber, MD, and Maizels, N. (2003) Distamysin Binds G4 DNA and Maps the Interaction Surface of Nucleolin RGG Domain Recognition. Nucleic Acids Research. 31: 2944-2951; *corresponding author. https://doi.org/10.1093/nar/gkg392
Main, E, Xoing, Y, Cocco, MJ, D’Andrea, L and Regan, L. (2003) Design of Stable a-Helical Arrays from an Idealized TPR Motif. Structure 11: 497-508. https://doi.org/10.1016/s0969-2126(03)00076-5
Cocco, MJ1, Ramirez-Alvarado, M1 and Regan, L. (2003) Mutations in the B1 Domain of Protein G that Delay the Onset of Amyloid Fibril Formation in Vitro. Protein Science 12: 567-576; 1co-first authors. https://doi.org/10.1110/ps.0227403
Li H, Cocco MJ, Steitz TA, and Engelman DM. (2001) Conversion of Phospholamban Into a Soluble Pentameric Helical Bundle. Biochemistry 40: 6636-6645. https://doi.org/10.1021/bi0026573
Zhou, FX, Cocco, MJ, Russ, WP, Brunger, AT, and DM Engelman, DM. (2000) Interhelical Hydrogen Bonding Drives Strong Interactions in Membrane Proteins. Nature Struct. Biol. 7: 154-160. https://doi.org/10.1038/72430
Basu, S, Szewczak, AA, Cocco, MJ, Strobel, SA. (2000) Direct Detection of Monovalent Metal Ion Binding to a DNA G-quartet by 205Tl NMR. J. Am. Chem. Soc. 122: 3240-3241. https://doi.org/10.1021/ja993614g
Lecomte, JTJ, Kao, YH, and Cocco, MJ. (1996) The Native State of Apomyoglobin Described by Proton NMR Spectroscopy: The A-B-G-H Interface of Wild-Type Sperm Whale Apomyoglobin. Proteins: Structure, Function and Genetics 25: 267-285. https://doi.org/10.1002/(sici)1097-0134(199607)25:3%3C267::aid-prot1%3E3.0.co;2-d
Wynn, R, Cocco, MJ, and Richards, FM. (1995) Mixed Disulfide Intermediates During the Reduction of Disulfides by Eschericia coli Thioredoxin. Biochemistry 34: 11807-11813. https://doi.org/10.1021/bi00037a019
Cocco, MJ and Lecomte, JTJ. (1994) The Native State of Apomyoglobin Described by Proton NMR Spectroscopy: Interaction with the Paramagnetic Probe HyTEMPO and the Fluorescent Dye ANS. Protein Science 3: 267-281. https://doi.org/10.1002/pro.5560030211
Cocco, MJ, Barrick, D, Taylor, SV, and Lecomte, JTJ. (1992) Histidine 82 Influences Heme Orientational Isomerization in Sperm Whale Myoglobin. Long-Range Effect due to Mutation of a Conserved Residue. J. Am. Chem. Soc. 114: 11000-11001. https://doi.org/10.1021/ja00053a069
Cocco, MJ, Kao, YH, Phillips, AT and Lecomte, JTJ. (1992) Structural Comparison of Apomyoglobin and Metaquomyoglobin: pH Titration of Histidines by NMR Spectroscopy. Biochemistry 31: 6481-6491. https://doi.org/10.1021/bi00143a018
Cocco, MJ and Lecomte, JTJ. (1990) Characterization of Hydrophobic Cores in Apomyoglobin: A Proton NMR Spectroscopy Study. Biochemistry 29: 11067-11072. https://doi.org/10.1021/bi00502a008
Lecomte, JTJ and Cocco, MJ. (1990) Structural Features of the Protoporphyrin-Apomyoglobin Complex: A Proton NMR Spectroscopy Study. Biochemistry 29: 11057-11067. https://doi.org/10.1021/bi00502a007