Year |
Citation |
Score |
2020 |
Soto J, Moody CL, Alhoshani A, Cocco MJ. Hydrogen Exchange and NMR Dynamics Reveal Positions Stabilized by P53 Rescue Mutants N239Y and N235K Biophysical Journal. 118: 51a. DOI: 10.1016/J.Bpj.2019.11.460 |
0.697 |
|
2019 |
Cocco MJ, Soto J, Alhoshani A, Moody C. Hydrogen Exchange Reveals the Mechanism of Stabilization of P53 Rescue Mutants N235K and N239Y Biophysical Journal. 116: 340a. DOI: 10.1016/J.Bpj.2018.11.1853 |
0.689 |
|
2016 |
Cocco MJ, Alhoshani A, Vu V, Greene D. Structural Determinants and Binding Properties of the Neurite Outgrowth Inhibitor (NOGO) Biophysical Journal. 110: 192. DOI: 10.1016/J.Bpj.2015.11.1067 |
0.396 |
|
2015 |
Moro SL, Cocco MJ. (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. PMID 26154586 DOI: 10.1007/S12104-015-9626-Y |
0.378 |
|
2014 |
Feinstein HE, Tifrea D, Sun G, Popot JL, de la Maza LM, Cocco MJ. Long-term stability of a vaccine formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis. The Journal of Membrane Biology. 247: 1053-65. PMID 24942817 DOI: 10.1007/S00232-014-9693-5 |
0.352 |
|
2014 |
Alhoshani A, Vithayathil R, Bandong J, Chrunyk KM, Moreno GO, Weiss GA, Cocco MJ. Glutamate provides a key structural contact between reticulon-4 (Nogo-66) and phosphocholine. Biochimica Et Biophysica Acta. 1838: 2350-6. PMID 24863057 DOI: 10.1016/J.Bbamem.2014.05.021 |
0.42 |
|
2014 |
Alhoshani A, Vithayathil R, Weiss GA, Cocco MJ. Model of the Nogo: Nogo Receptor Complex Biophysical Journal. 106: 410a-411a. DOI: 10.1016/J.Bpj.2013.11.2311 |
0.383 |
|
2012 |
Feinstein HE, Zardeneta G, Popot J, de la Maza LM, Cocco MJ. Amphipols Stabilize a Membrane Protein Vaccine Against Chlamydia Biophysical Journal. 102: 268a. DOI: 10.1016/J.Bpj.2011.11.1475 |
0.355 |
|
2012 |
Alhoshani A, Maeda N, Schulz J, Milton S, Glabe C, Fan H, Cocco M. The Oncogenic Jaagsiekte Sheep Retrovirus Cytoplasmic Tail Adopts a Unique Conformation on a Phosphocholine Surface Biophysical Journal. 102: 267a-268a. DOI: 10.1016/J.Bpj.2011.11.1472 |
0.36 |
|
2011 |
Vithayathil R, Hooy RM, Cocco MJ, Weiss GA. The scope of phage display for membrane proteins. Journal of Molecular Biology. 414: 499-510. PMID 22037583 DOI: 10.1016/J.Jmb.2011.10.021 |
0.323 |
|
2011 |
Moody CL, Tretyachenko-Ladokhina V, Laue TM, Senear DF, Cocco MJ. Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface. Biochemistry. 50: 6622-32. PMID 21688840 DOI: 10.1021/Bi200205V |
0.716 |
|
2011 |
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, et al. Amphipols from A to Z. Annual Review of Biophysics. 40: 379-408. PMID 21545287 DOI: 10.1146/Annurev-Biophys-042910-155219 |
0.347 |
|
2010 |
Corbin-Lickfett KA, Souki SK, Cocco MJ, Sandri-Goldin RM. 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. PMID 20410270 DOI: 10.1128/Jvi.00509-10 |
0.387 |
|
2010 |
Vasudevan SV, Schulz J, Zhou C, Cocco MJ. Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface. Proceedings of the National Academy of Sciences of the United States of America. 107: 6847-51. PMID 20351248 DOI: 10.1073/Pnas.0911817107 |
0.659 |
|
2010 |
Corbin-Lickfett KA, Rojas S, Li L, Cocco MJ, Sandri-Goldin RM. 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. PMID 20015986 DOI: 10.1128/Jvi.01388-09 |
0.371 |
|
2010 |
Moody CL, Tretyachenko-Ladokhina V, Senear DF, Cocco MJ. Structure and Dynamics of the Cytidine Repressor DNA-Binding Domain Biophysical Journal. 98: 660a. DOI: 10.1016/J.Bpj.2009.12.3622 |
0.716 |
|
2010 |
Cocco MJ, Vasudevan S, Vithayathil R, Schulz J, Zhou C, Majumdar S, Weiss G. Protein Folding at the Membrane Interface: The Structure of Nogo-66 Biophysical Journal. 98: 625a. DOI: 10.1016/J.Bpj.2009.12.3423 |
0.367 |
|
2009 |
Corbin-Lickfett KA, Chen IH, Cocco MJ, Sandri-Goldin RM. The HSV-1 ICP27 RGG box specifically binds flexible, GC-rich sequences but not G-quartet structures. Nucleic Acids Research. 37: 7290-301. PMID 19783816 DOI: 10.1093/Nar/Gkp793 |
0.384 |
|
2008 |
Gehman JD, Cocco MJ, Grindley ND. Chemical shift mapping of gammadelta resolvase dimer and activated tetramer: mechanistic implications for DNA strand exchange. Biochimica Et Biophysica Acta. 1784: 2086-92. PMID 18840551 DOI: 10.1016/J.Bbapap.2008.08.023 |
0.463 |
|
2007 |
Sun G, Pal S, Sarcon AK, Kim S, Sugawara E, Nikaido H, Cocco MJ, Peterson EM, De La Maza LM. Structural and functional analyses of the major outer membrane protein of Chlamydia trachomatis Journal of Bacteriology. 189: 6222-6235. PMID 17601785 DOI: 10.1128/Jb.00552-07 |
0.37 |
|
2006 |
Tretyachenko-Ladokhina V, Cocco MJ, Senear DF. 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. PMID 16919681 DOI: 10.1016/J.Jmb.2006.06.085 |
0.434 |
|
2006 |
Kamtekar S, Ho RS, Cocco MJ, Li W, Wenwieser SV, Boocock MR, Grindley ND, Steitz TA. Implications of structures of synaptic tetramers of gamma delta resolvase for the mechanism of recombination. Proceedings of the National Academy of Sciences of the United States of America. 103: 10642-7. PMID 16807292 DOI: 10.1073/Pnas.0604062103 |
0.434 |
|
2006 |
Levin AM, Coroneus JG, Cocco MJ, Weiss GA. Exploring the interaction between the protein kinase A catalytic subunit and caveolin-1 scaffolding domain with shotgun scanning, oligomer complementation, NMR, and docking. Protein Science : a Publication of the Protein Society. 15: 478-86. PMID 16452625 DOI: 10.1110/Ps.051911706 |
0.429 |
|
2004 |
Cortajarena AL, Kajander T, Pan W, Cocco MJ, Regan L. Protein design to understand peptide ligand recognition by tetratricopeptide repeat proteins. Protein Engineering, Design & Selection : Peds. 17: 399-409. PMID 15166314 DOI: 10.1093/Protein/Gzh047 |
0.32 |
|
2003 |
Cocco MJ, Hanakahi LA, Huber MD, Maizels N. Specific interactions of distamycin with G-quadruplex DNA. Nucleic Acids Research. 31: 2944-51. PMID 12771220 DOI: 10.1093/Nar/Gkg392 |
0.369 |
|
2003 |
Main ER, Xiong Y, Cocco MJ, D'Andrea L, Regan L. Design of stable alpha-helical arrays from an idealized TPR motif. Structure (London, England : 1993). 11: 497-508. PMID 12737816 DOI: 10.1016/S0969-2126(03)00076-5 |
0.375 |
|
2001 |
Li H, Cocco MJ, Steitz TA, Engelman DM. Conversion of phospholamban into a soluble pentameric helical bundle. Biochemistry. 40: 6636-45. PMID 11380258 DOI: 10.1021/Bi0026573 |
0.377 |
|
2000 |
Zhou FX, Cocco MJ, Russ WP, Brunger AT, Engelman DM. Interhelical hydrogen bonding drives strong interactions in membrane proteins. Nature Structural Biology. 7: 154-60. PMID 10655619 DOI: 10.1038/72430 |
0.385 |
|
1996 |
Lecomte JTJ, Kao YH, Cocco MJ. 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. PMID 8844864 DOI: 10.1002/(Sici)1097-0134(199607)25:3<267::Aid-Prot1>3.0.Co;2-D |
0.388 |
|
1995 |
Wynn R, Cocco MJ, Richards FM. Mixed disulfide intermediates during the reduction of disulfides by Escherichia coli thioredoxin. Biochemistry. 34: 11807-13. PMID 7547914 DOI: 10.1021/Bi00037A019 |
0.305 |
|
1994 |
Cocco MJ, Lecomte JTJ. 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. PMID 8003963 DOI: 10.1002/Pro.5560030211 |
0.416 |
|
1992 |
Cocco MJ, Kao YH, Phillips AT, Lecomte JTJ. Structural comparison of apomyoglobin and metaquomyoglobin: pH titration of histidines by NMR spectroscopy Biochemistry. 31: 6481-6491. PMID 1633160 DOI: 10.1021/Bi00143A018 |
0.401 |
|
1990 |
Cocco MJ, Lecomte JTJ. Characterization of hydrophobic cores in apomyoglobin: A proton NMR spectroscopy study Biochemistry. 29: 11067-11072. PMID 2176892 DOI: 10.1021/Bi00502A008 |
0.384 |
|
1990 |
Lecomte JTJ, Cocco MJ. Structural features of the protoporphyrin-apomyoglobin complex: A proton NMR spectroscopy study Biochemistry. 29: 11057-11067. PMID 2176891 DOI: 10.1021/Bi00502A007 |
0.399 |
|
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