Year |
Citation |
Score |
2022 |
Aryal P, Devkota SR, Jeevarajah D, Law R, Payne RJ, Bhusal RP, Stone MJ. Swapping N-terminal regions among tick evasins reveals cooperative interactions influencing chemokine binding and selectivity. The Journal of Biological Chemistry. 102382. PMID 35973511 DOI: 10.1016/j.jbc.2022.102382 |
0.314 |
|
2020 |
Franck C, Foster SR, Johansen-Leete J, Chowdhury S, Cielesh M, Bhusal RP, Mackay JP, Larance M, Stone MJ, Payne RJ. Semisynthesis of an evasin from tick saliva reveals a critical role of tyrosine sulfation for chemokine binding and inhibition. Proceedings of the National Academy of Sciences of the United States of America. PMID 32461364 DOI: 10.1073/Pnas.2000605117 |
0.427 |
|
2020 |
Johansen-Leete J, Passioura T, Foster S, Bhusal RP, Ford D, Liu M, Jongkees SAK, Suga H, Stone MJ, Payne RJ. Discovery of Potent Cyclic Sulfopeptide Chemokine Inhibitors via Reprogrammed Genetic Code mRNA Display. Journal of the American Chemical Society. PMID 32330017 DOI: 10.1021/Jacs.0C03152 |
0.369 |
|
2020 |
Huang C, Foster SR, Shah AD, Kleifeld O, Canals M, Schittenhelm RB, Stone MJ. Phosphoproteomic characterization of the signaling network resulting from activation of chemokine receptor CCR2. The Journal of Biological Chemistry. PMID 32241914 DOI: 10.1074/Jbc.Ra119.012026 |
0.376 |
|
2019 |
Bhusal RP, Foster SR, Stone MJ. Structural Basis of Chemokine and Receptor Interactions: Key Regulators of Leukocyte Recruitment in Inflammatory Responses. Protein Science : a Publication of the Protein Society. PMID 31605402 DOI: 10.1002/Pro.3744 |
0.349 |
|
2019 |
Sanchez J, Lane JR, Canals M, Stone MJ. Influence of Chemokine N-Terminal Modification on Biased Agonism at the Chemokine Receptor CCR1. International Journal of Molecular Sciences. 20. PMID 31096719 DOI: 10.3390/Ijms20102417 |
0.389 |
|
2018 |
Sanchez J, E Huma Z, Lane JR, Liu X, Bridgford JL, Payne RJ, Canals M, Stone MJ. Evaluation and extension of the two-site, two-step model for binding and activation of the chemokine receptor CCR1. The Journal of Biological Chemistry. PMID 30567735 DOI: 10.1074/Jbc.Ra118.006535 |
0.473 |
|
2018 |
Hayward J, Sanchez J, Perry A, Huang C, Valle MR, Canals M, Payne RJ, Stone MJ. Correction: Ticks from diverse genera encode chemokine-inhibitory evasin proteins. The Journal of Biological Chemistry. 293: 15888. PMID 30315086 DOI: 10.1074/Jbc.Aac118.005871 |
0.331 |
|
2017 |
Hayward J, Sanchez J, Perry A, Huang C, Rodriguez Valle M, Canals M, Payne RJ, Stone MJ. Ticks from diverse genera encode chemokine-inhibitory evasin proteins. The Journal of Biological Chemistry. PMID 28778927 DOI: 10.1074/Jbc.M117.807255 |
0.353 |
|
2017 |
Huma ZE, Sanchez J, Lim HD, Bridgford JL, Huang C, Parker BJ, Pazhamalil JG, Porebski BT, Pfleger KDG, Lane JR, Canals M, Stone MJ. Key determinants of selective binding and activation by the monocyte chemoattractant proteins at the chemokine receptor CCR2. Science Signaling. 10. PMID 28536301 DOI: 10.1126/Scisignal.Aai8529 |
0.405 |
|
2017 |
Payne RJ, Wang X, Sanchez J, Stone M. Sulfation of Human Cytomegalovirus Protein UL22A Enhances Binding to the Chemokine RANTES. Angewandte Chemie (International Ed. in English). PMID 28488292 DOI: 10.1002/Anie.201703059 |
0.412 |
|
2017 |
Stone MJ, Hayward JA, Huang C, E Huma Z, Sanchez J. Mechanisms of Regulation of the Chemokine-Receptor Network. International Journal of Molecular Sciences. 18. PMID 28178200 DOI: 10.3390/Ijms18020342 |
0.381 |
|
2016 |
Isahak N, Sanchez J, Perrier S, Stone MJ, Payne RJ. Synthesis of polymers and nanoparticles bearing polystyrene sulfonate brushes for chemokine binding. Organic & Biomolecular Chemistry. PMID 27031327 DOI: 10.1039/C6Ob00270F |
0.344 |
|
2015 |
Stone MJ, Payne RJ. Homogeneous sulfopeptides and sulfoproteins: synthetic approaches and applications to characterize the effects of tyrosine sulfation on biochemical function. Accounts of Chemical Research. 48: 2251-61. PMID 26196117 DOI: 10.1021/Acs.Accounts.5B00255 |
0.429 |
|
2015 |
Ludeman JP, Nazari-Robati M, Wilkinson BL, Huang C, Payne RJ, Stone MJ. Phosphate modulates receptor sulfotyrosine recognition by the chemokine monocyte chemoattractant protein-1 (MCP-1/CCL2). Organic & Biomolecular Chemistry. 13: 2162-9. PMID 25536525 DOI: 10.1039/C4Ob02262A |
0.446 |
|
2014 |
Millard CJ, Ludeman JP, Canals M, Bridgford JL, Hinds MG, Clayton DJ, Christopoulos A, Payne RJ, Stone MJ. Structural basis of receptor sulfotyrosine recognition by a CC chemokine: the N-terminal region of CCR3 bound to CCL11/eotaxin-1. Structure (London, England : 1993). 22: 1571-81. PMID 25450766 DOI: 10.1016/J.Str.2014.08.023 |
0.447 |
|
2014 |
Liu X, Malins LR, Roche M, Sterjovski J, Duncan R, Garcia ML, Barnes NC, Anderson DA, Stone MJ, Gorry PR, Payne RJ. Site-selective solid-phase synthesis of a CCR5 sulfopeptide library to interrogate HIV binding and entry. Acs Chemical Biology. 9: 2074-81. PMID 24963694 DOI: 10.1021/Cb500337R |
0.389 |
|
2014 |
Ludeman JP, Stone MJ. The structural role of receptor tyrosine sulfation in chemokine recognition. British Journal of Pharmacology. 171: 1167-79. PMID 24116930 DOI: 10.1111/Bph.12455 |
0.437 |
|
2014 |
Tan JHY, Ludeman JP, Wedderburn J, Canals M, Hall P, Butler SJ, Taleski D, Christopoulos A, Hickey MJ, Payne RJ, Stone MJ. Erratum: Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1): (Journal of Biological Chemistry (2013) 288 (10024-10034)) Journal of Biological Chemistry. 289. DOI: 10.1074/Jbc.A112.447359 |
0.416 |
|
2014 |
Huma ZE, Ludeman JP, Wilkinson BL, Payne RJ, Stone MJ. NMR characterization of cooperativity: Fast ligand binding coupled to slow protein dimerization Chemical Science. 5: 2783-2788. DOI: 10.1039/C4Sc00131A |
0.396 |
|
2013 |
Diepenhorst NA, Gooley PR, Stone MJ, Bathgate RA. Development of a scaffold displaying exoloops of RXFP1. Italian Journal of Anatomy and Embryology = Archivio Italiano Di Anatomia Ed Embriologia. 118: 1-3. PMID 24640555 DOI: 10.13128/Ijae-13723 |
0.494 |
|
2013 |
Tan JH, Ludeman JP, Wedderburn J, Canals M, Hall P, Butler SJ, Taleski D, Christopoulos A, Hickey MJ, Payne RJ, Stone MJ. Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1). The Journal of Biological Chemistry. 288: 10024-34. PMID 23408426 DOI: 10.1074/Jbc.M112.447359 |
0.467 |
|
2012 |
Tan JH, Canals M, Ludeman JP, Wedderburn J, Boston C, Butler SJ, Carrick AM, Parody TR, Taleski D, Christopoulos A, Payne RJ, Stone MJ. Design and receptor interactions of obligate dimeric mutant of chemokine monocyte chemoattractant protein-1 (MCP-1). The Journal of Biological Chemistry. 287: 14692-702. PMID 22396538 DOI: 10.1074/Jbc.M111.334201 |
0.417 |
|
2012 |
Barter EF, Stone MJ. Synergistic interactions between chemokine receptor elements in recognition of interleukin-8 by soluble receptor mimics. Biochemistry. 51: 1322-31. PMID 22242662 DOI: 10.1021/Bi201615Y |
0.66 |
|
2011 |
Zhu JZ, Millard CJ, Ludeman JP, Simpson LS, Clayton DJ, Payne RJ, Widlanski TS, Stone MJ. Tyrosine sulfation influences the chemokine binding selectivity of peptides derived from chemokine receptor CCR3. Biochemistry. 50: 1524-34. PMID 21235238 DOI: 10.1021/Bi101240V |
0.45 |
|
2009 |
Stone MJ, Chuang S, Hou X, Shoham M, Zhu JZ. Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins. New Biotechnology. 25: 299-317. PMID 19658209 DOI: 10.1016/J.Nbt.2009.03.011 |
0.438 |
|
2009 |
Simpson LS, Zhu JZ, Widlanski TS, Stone MJ. Regulation of chemokine recognition by site-specific tyrosine sulfation of receptor peptides. Chemistry & Biology. 16: 153-61. PMID 19246006 DOI: 10.1016/J.Chembiol.2008.12.007 |
0.427 |
|
2008 |
Jarymowycz VA, Stone MJ. Remote changes in the dynamics of the phosphotyrosine-binding domain of insulin receptor substrate-1 induced by phosphopeptide binding. Biochemistry. 47: 13371-82. PMID 19053277 DOI: 10.1021/Bi801096B |
0.76 |
|
2008 |
Richer SM, Stewart NK, Tomaszewski JW, Stone MJ, Oakley MG. NMR investigation of the binding between human profilin I and inositol 1,4,5-triphosphate, the soluble headgroup of phosphatidylinositol 4,5-bisphosphate. Biochemistry. 47: 13455-62. PMID 19035654 DOI: 10.1021/Bi801535F |
0.385 |
|
2008 |
Jarymowycz VA, Cortajarena AL, Regan L, Stone MJ. Comparison of the backbone dynamics of a natural and a consensus designed 3-TPR domain. Journal of Biomolecular Nmr. 41: 169-78. PMID 18566891 DOI: 10.1007/S10858-008-9250-6 |
0.75 |
|
2006 |
Cheng CY, Jarymowycz VA, Cortajarena AL, Regan L, Stone MJ. Repeat motions and backbone flexibility in designed proteins with different numbers of identical consensus tetratricopeptide repeats. Biochemistry. 45: 12175-83. PMID 17002317 DOI: 10.1021/Bi060819A |
0.754 |
|
2006 |
Jarymowycz VA, Krupinska E, Stone MJ. Comparison between the backbone dynamics of an 11-amino acid peptide sequence in alpha-helical and beta-hairpin structural contexts. Biochemistry. 45: 11179-89. PMID 16964979 DOI: 10.1021/Bi0608919 |
0.751 |
|
2006 |
Jarymowycz VA, Stone MJ. Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences. Chemical Reviews. 106: 1624-71. PMID 16683748 DOI: 10.1021/Cr040421P |
0.729 |
|
2005 |
Sharrow SD, Edmonds KA, Goodman MA, Novotny MV, Stone MJ. Thermodynamic consequences of disrupting a water-mediated hydrogen bond network in a protein:pheromone complex. Protein Science : a Publication of the Protein Society. 14: 249-56. PMID 15608125 DOI: 10.1110/Ps.04912605 |
0.34 |
|
2004 |
Datta-Mannan A, Stone MJ. Chemokine-binding specificity of soluble chemokine-receptor analogues: identification of interacting elements by chimera complementation. Biochemistry. 43: 14602-11. PMID 15544331 DOI: 10.1021/Bi048990E |
0.758 |
|
2004 |
Goehlert VA, Krupinska E, Regan L, Stone MJ. Analysis of side chain mobility among protein G B1 domain mutants with widely varying stabilities. Protein Science : a Publication of the Protein Society. 13: 3322-30. PMID 15537756 DOI: 10.1110/Ps.04926604 |
0.388 |
|
2004 |
Mayer MR, Parody TR, Datta-Mannan A, Stone MJ. Specificity determinants for chemokine recognition identified using eotaxin-MCP-1 chimeras. Febs Letters. 571: 166-70. PMID 15280036 DOI: 10.1016/J.Febslet.2004.06.079 |
0.744 |
|
2004 |
Parody TR, Stone MJ. High level expression, activation, and antagonism of CC chemokine receptors CCR2 and CCR3 in Chinese hamster ovary cells. Cytokine. 27: 38-46. PMID 15207250 DOI: 10.1016/J.Cyto.2004.03.013 |
0.358 |
|
2004 |
Krízová H, Zídek L, Stone MJ, Novotny MV, Sklenár V. Temperature-dependent spectral density analysis applied to monitoring backbone dynamics of major urinary protein-I complexed with the pheromone 2- sec-butyl-4,5-dihydrothiazole. Journal of Biomolecular Nmr. 28: 369-84. PMID 14872128 DOI: 10.1023/B:Jnmr.0000015404.61574.65 |
0.357 |
|
2003 |
Datta A, Stone MJ. Soluble mimics of a chemokine receptor: chemokine binding by receptor elements juxtaposed on a soluble scaffold. Protein Science : a Publication of the Protein Society. 12: 2482-91. PMID 14573861 DOI: 10.1110/Ps.03254303 |
0.448 |
|
2003 |
Mayer KL, Earley MR, Gupta S, Pichumani K, Regan L, Stone MJ. Covariation of backbone motion throughout a small protein domain. Nature Structural Biology. 10: 962-5. PMID 14528292 DOI: 10.1038/Nsb991 |
0.45 |
|
2003 |
Sharrow SD, Novotny MV, Stone MJ. Thermodynamic analysis of binding between mouse major urinary protein-I and the pheromone 2-sec-butyl-4,5-dihydrothiazole. Biochemistry. 42: 6302-9. PMID 12755635 DOI: 10.1021/Bi026423Q |
0.398 |
|
2003 |
Mayer KL, Stone MJ. Backbone dynamics of the CC-chemokine eotaxin-2 and comparison among the eotaxin group chemokines. Proteins. 50: 184-91. PMID 12486712 DOI: 10.1002/Prot.10238 |
0.505 |
|
2002 |
Sharrow SD, Vaughn JL, Zídek L, Novotny MV, Stone MJ. Pheromone binding by polymorphic mouse major urinary proteins. Protein Science : a Publication of the Protein Society. 11: 2247-56. PMID 12192080 DOI: 10.1110/Ps.0204202 |
0.363 |
|
2001 |
Ye J, Mayer KL, Mayer MR, Stone MJ. NMR solution structure and backbone dynamics of the CC chemokine eotaxin-3. Biochemistry. 40: 7820-31. PMID 11425309 DOI: 10.1021/Bi010252S |
0.726 |
|
2001 |
Stone MJ. NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding. Accounts of Chemical Research. 34: 379-88. PMID 11352716 DOI: 10.1021/Ar000079C |
0.405 |
|
2001 |
Mayer MR, Stone MJ. Identification of receptor binding and activation determinants in the N-terminal and N-loop regions of the CC chemokine eotaxin. The Journal of Biological Chemistry. 276: 13911-6. PMID 11297526 DOI: 10.1074/Jbc.M011202200 |
0.43 |
|
2001 |
Stone MJ, Gupta S, Snyder N, Regan L. Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants. Journal of the American Chemical Society. 123: 185-6. PMID 11273620 DOI: 10.1021/Ja003094L |
0.408 |
|
2000 |
Mayer KL, Stone MJ. NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2. Biochemistry. 39: 8382-8395. PMID 10913244 DOI: 10.1021/Bi000523J |
0.379 |
|
2000 |
Seewald MJ, Pichumani K, Stowell C, Tibbals BV, Regan L, Stone MJ. The role of backbone conformational heat capacity in protein stability: temperature dependent dynamics of the B1 domain of Streptococcal protein G. Protein Science : a Publication of the Protein Society. 9: 1177-93. PMID 10892810 DOI: 10.1110/Ps.9.6.1177 |
0.372 |
|
2000 |
Ye J, Kohli LL, Stone MJ. Characterization of binding between the chemokine eotaxin and peptides derived from the chemokine receptor CCR3. The Journal of Biological Chemistry. 275: 27250-7. PMID 10859315 DOI: 10.1074/Jbc.M003925200 |
0.742 |
|
2000 |
Goodman JL, Pagel MD, Stone MJ. Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters. Journal of Molecular Biology. 295: 963-78. PMID 10656804 DOI: 10.1006/Jmbi.1999.3419 |
0.428 |
|
1999 |
Ye J, Mayer KL, Stone MJ. Backbone dynamics of the human CC-chemokine eotaxin. Journal of Biomolecular Nmr. 15: 115-24. PMID 10605085 DOI: 10.1023/A:1008376728947 |
0.73 |
|
1999 |
Zidek L, Novotny MV, Stone MJ. Increased protein backbone conformational entropy upon hydrophobic ligand binding Nature Structural Biology. 6: 1118-1121. PMID 10581552 DOI: 10.1038/70057 |
0.414 |
|
1999 |
Žídek L, Stone MJ, Lato SM, Pagel MD, Miao Z, Ellington AD, Novotny MV. NMR mapping of the recombinant mouse major urinary protein I binding site occupied by the pheromone 2-sec-buty1-4,5-dihydrothiazole Biochemistry. 38: 9850-9861. PMID 10433691 DOI: 10.1021/Bi990497T |
0.447 |
|
1998 |
Saint-Jean AP, Phillips KR, Creighton DJ, Stone MJ. Active monomeric and dimeric forms of Pseudomonas putida glyoxalase I: evidence for 3D domain swapping. Biochemistry. 37: 10345-53. PMID 9671502 DOI: 10.1021/Bi980868Q |
0.344 |
|
1995 |
Jennings PA, Stone MJ, Wright PE. Overexpression of myoglobin and assignment of its amide, C alpha and C beta resonances. Journal of Biomolecular Nmr. 6: 271-6. PMID 8520219 DOI: 10.1007/Bf00197808 |
0.346 |
|
1995 |
Stone MJ, Ruf W, Miles DJ, Edgington TS, Wright PE. Recombinant soluble human tissue factor secreted by Saccharomyces cerevisiae and refolded from Escherichia coli inclusion bodies: glycosylation of mutants, activity and physical characterization. The Biochemical Journal. 605-14. PMID 7654202 DOI: 10.1042/Bj3100605 |
0.366 |
|
1994 |
Ruf W, Schullek JR, Stone MJ, Edgington TS. Mutational mapping of functional residues in tissue factor: identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain. Biochemistry. 33: 1565-72. PMID 8312277 DOI: 10.1021/Bi00172A037 |
0.43 |
|
1993 |
Stone MJ, Chandrasekhar K, Holmgren A, Wright PE, Dyson HJ. Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurements. Biochemistry. 32: 426-35. PMID 8422352 DOI: 10.1021/bi00053a007 |
0.316 |
|
1992 |
Stone MJ, Nedderman AN, Williams DH, Lin PK, Brown DM. Molecular basis for methoxyamine initiated mutagenesis. 1H nuclear magnetic resonance studies of base-modified oligodeoxynucleotides. Journal of Molecular Biology. 222: 711-23. PMID 1660932 DOI: 10.1016/0022-2836(91)90507-3 |
0.315 |
|
1992 |
Stone MJ, Fairbrother WJ, Palmer AG, Reizer J, Saier MH, Wright PE. Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from 15N NMR relaxation measurements. Biochemistry. 31: 4394-406. PMID 1316146 DOI: 10.1021/Bi00133A003 |
0.432 |
|
1991 |
Stone MJ, Dyk MSV, Booth PM, Williams DH. An approach to a synthetic carboxylate-binding pocket based on β-avoparcin Journal of the Chemical Society-Perkin Transactions 1. 1629-1635. DOI: 10.1039/P19910001629 |
0.304 |
|
1990 |
Williams DH, Stone MJ, Mortishire-Smith RJ, Hauck PR. Molecular recognition by secondary metabolites. Biochemical Pharmacology. 40: 27-34. PMID 2372307 DOI: 10.1016/0006-2952(90)90174-J |
0.372 |
|
1989 |
Williams DH, Stone MJ, Hauck PR, Rahman SK. Why are secondary metabolites (natural products) biosynthesized? Journal of Natural Products. 52: 1189-208. PMID 2693613 DOI: 10.1021/Np50066A001 |
0.302 |
|
Show low-probability matches. |