Year |
Citation |
Score |
2017 |
Qassab A, Liyanage R, Stites W. Methionine Sulfoxide Formation by Cigarette Smoke is Associated with the Degradation of Plasma Proteins Biophysical Journal. 112: 48a-49a. DOI: 10.1016/J.Bpj.2016.11.301 |
0.329 |
|
2017 |
Moudy MG, Stites W. Investigation of Methionine Sulfoxide Formation as a Regulator of Proteolysis Biophysical Journal. 112: 202a. DOI: 10.1016/J.Bpj.2016.11.1117 |
0.326 |
|
2013 |
Spencer D, Bertrand GM, Stites WE. The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model. Biophysical Chemistry. 180: 86-94. PMID 23892194 DOI: 10.1016/J.Bpc.2013.06.018 |
0.445 |
|
2013 |
Talla D, Stites WE. The fluorescence detected guanidine hydrochloride equilibrium denaturation of wild-type staphylococcal nuclease does not fit a three-state unfolding model. Biochimie. 95: 1386-93. PMID 23523929 DOI: 10.1016/J.Biochi.2013.03.003 |
0.449 |
|
2012 |
Liyanage R, Devarapalli N, Pyland DB, Puckett LM, Phan NH, Starch JA, Okimoto MR, Gidden J, Stites WE, Lay JO. Theory of the Protein Equilibrium Population Snapshot by H/D Exchange Electrospray Ionization Mass Spectrometry (PEPS-HDX-ESI-MS) Method used to obtain Protein Folding Energies/Rates and Selected Supporting Experimental Evidence. International Journal of Mass Spectrometry. 330: 63-70. PMID 23436981 DOI: 10.1016/J.Ijms.2012.10.010 |
0.423 |
|
2012 |
Saunders CC, Stites WE. An electrophoretic mobility shift assay for methionine sulfoxide in proteins. Analytical Biochemistry. 421: 767-9. PMID 22230286 DOI: 10.1016/J.Ab.2011.12.021 |
0.386 |
|
2011 |
Bell-Upp P, Robinson AC, Whitten ST, Wheeler EL, Lin J, Stites WE, E BG. Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins. Biophysical Chemistry. 159: 217-26. PMID 21802194 DOI: 10.1016/J.Bpc.2011.06.016 |
0.445 |
|
2009 |
Liyanage R, Devarapalli N, Puckett LM, Phan NH, Gidden J, Stites WE, Lay JO. Comparison of Two ESI MS Based H/D Exchange Methods for Extracting Protein Folding Energies. International Journal of Mass Spectrometry. 287: 96-104. PMID 22427739 DOI: 10.1016/J.Ijms.2008.10.017 |
0.38 |
|
2008 |
Kim YH, Stites WE. Effects of excluded volume upon protein stability in covalently cross-linked proteins with variable linker lengths. Biochemistry. 47: 8804-14. PMID 18656955 DOI: 10.1021/Bi800297J |
0.453 |
|
2008 |
Talla-Singh D, Stites WE. Refinement of noncalorimetric determination of the change in heat capacity, DeltaC(p), of protein unfolding and validation across a wide temperature range. Proteins. 71: 1607-16. PMID 18384147 DOI: 10.1002/Prot.22016 |
0.33 |
|
2007 |
Karp DA, Gittis AG, Stahley MR, Fitch CA, Stites WE, García-Moreno E B. High apparent dielectric constant inside a protein reflects structural reorganization coupled to the ionization of an internal Asp. Biophysical Journal. 92: 2041-53. PMID 17172297 DOI: 10.1529/Biophysj.106.090266 |
0.448 |
|
2007 |
Byrne MP, Stites WE. Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation. Biophysical Chemistry. 125: 490-6. PMID 17134819 DOI: 10.1016/J.Bpc.2006.10.014 |
0.385 |
|
2006 |
Qiu W, Kao YT, Zhang L, Yang Y, Wang L, Stites WE, Zhong D, Zewail AH. Protein surface hydration mapped by site-specific mutations. Proceedings of the National Academy of Sciences of the United States of America. 103: 13979-84. PMID 16968773 DOI: 10.1073/Pnas.0606235103 |
0.406 |
|
2004 |
Chen J, Stites WE. Replacement of staphylococcal nuclease hydrophobic core residues with those from thermophilic homologues indicates packing is improved in some thermostable proteins. Journal of Molecular Biology. 344: 271-80. PMID 15504416 DOI: 10.1016/J.Jmb.2004.09.008 |
0.657 |
|
2004 |
Chen J, Lu Z, Sakon J, Stites WE. Proteins with simplified hydrophobic cores compared to other packing mutants. Biophysical Chemistry. 110: 239-48. PMID 15228960 DOI: 10.1016/J.Bpc.2004.02.007 |
0.664 |
|
2003 |
Schwehm JM, Fitch CA, Dang BN, García-Moreno E B, Stites WE. Changes in stability upon charge reversal and neutralization substitution in staphylococcal nuclease are dominated by favorable electrostatic effects. Biochemistry. 42: 1118-28. PMID 12549934 DOI: 10.1021/Bi0266434 |
0.478 |
|
2002 |
Fitch CA, Karp DA, Lee KK, Stites WE, Lattman EE, García-Moreno E B. Experimental pK(a) values of buried residues: analysis with continuum methods and role of water penetration. Biophysical Journal. 82: 3289-304. PMID 12023252 DOI: 10.1016/S0006-3495(02)75670-1 |
0.358 |
|
2001 |
Chen J, Stites WE. Packing is a key selection factor in the evolution of protein hydrophobic cores. Biochemistry. 40: 15280-9. PMID 11735410 DOI: 10.1021/Bi011776V |
0.695 |
|
2001 |
Chen J, Stites WE. Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease. Biochemistry. 40: 14012-9. PMID 11705393 DOI: 10.1021/Bi011269D |
0.67 |
|
2001 |
Chen J, Stites WE. Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles. Biochemistry. 40: 14004-11. PMID 11705392 DOI: 10.1021/Bi011268L |
0.639 |
|
2001 |
Holder JB, Bennett AF, Chen J, Spencer DS, Byrne MP, Stites WE. Energetics of side chain packing in staphylococcal nuclease assessed by exchange of valines, isoleucines, and leucines. Biochemistry. 40: 13998-4003. PMID 11705391 DOI: 10.1021/Bi011267T |
0.656 |
|
2001 |
Kim YH, Berry AH, Spencer DS, Stites WE. Comparing the effect on protein stability of methionine oxidation versus mutagenesis: steps toward engineering oxidative resistance in proteins. Protein Engineering. 14: 343-7. PMID 11438757 DOI: 10.1093/Protein/14.5.343 |
0.436 |
|
2000 |
Chen J, Lu Z, Sakon J, Stites WE. Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability. Journal of Molecular Biology. 303: 125-30. PMID 11023780 DOI: 10.1006/Jmbi.2000.4140 |
0.688 |
|
2000 |
Dwyer JJ, Gittis AG, Karp DA, Lattman EE, Spencer DS, Stites WE, García-Moreno E B. High apparent dielectric constants in the interior of a protein reflect water penetration. Biophysical Journal. 79: 1610-20. PMID 10969021 DOI: 10.1016/S0006-3495(00)76411-3 |
0.427 |
|
1998 |
Schwehm JM, Stites WE. Application of automated methods for determination of protein conformational stability Methods in Enzymology. 295: 150-170. PMID 9750218 DOI: 10.1016/S0076-6879(98)95039-X |
0.37 |
|
1998 |
Schwehm JM, Kristyanne ES, Biggers CC, Stites WE. Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease Biochemistry. 37: 6939-6948. PMID 9578580 DOI: 10.1021/Bi9725069 |
0.576 |
|
1997 |
Stites WE. Proteinminus signProtein Interactions: Interface Structure, Binding Thermodynamics, and Mutational Analysis. Chemical Reviews. 97: 1233-1250. PMID 11851449 DOI: 10.1021/Cr960387H |
0.361 |
|
1997 |
García-Moreno B, Dwyer JJ, Gittis AG, Lattman EE, Spencer DS, Stites WE. Experimental measurement of the effective dielectric in the hydrophobic core of a protein. Biophysical Chemistry. 64: 211-24. PMID 9127946 DOI: 10.1016/S0301-4622(96)02238-7 |
0.506 |
|
1997 |
Stites WE. Protein-protein interactions: Interface structure, binding thermodynamics, and mutational analysis Chemical Reviews. 97: 1233-1250. |
0.392 |
|
1996 |
Byrne MP, Broomfield CA, Stites WE. Mustard gas crosslinking of proteins through preferential alkylation of cysteines Journal of Protein Chemistry. 15: 131-136. PMID 8924198 DOI: 10.1007/Bf01887394 |
0.438 |
|
1996 |
Spencer DS, Stites WE. The M32L substitution of staphylococcal nuclease: Disagreement between theoretical prediction and experimental protein stability Journal of Molecular Biology. 257: 497-499. PMID 8648619 DOI: 10.1006/Jmbi.1996.0180 |
0.494 |
|
1995 |
Byrne MP, Stites WE. Chemically crosslinked protein dimers: Stability and denaturation effects Protein Science. 4: 2545-2558. PMID 8580845 DOI: 10.1002/Pro.5560041211 |
0.516 |
|
1995 |
Byrne MP, Manuel RL, Lowe LG, Stites WE. Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease Biochemistry. 34: 13949-13960. PMID 7577991 |
0.304 |
|
1995 |
Stites WE, Pranata J. Empirical evaluation of the influence of side chains on the conformational entropy of the polypeptide backbone Proteins: Structure, Function and Genetics. 22: 132-140. PMID 7567961 DOI: 10.1002/Prot.340220206 |
0.431 |
|
1994 |
Stites WE, Meeker AK, Shortle D. Evidence for strained interactions between side-chains and the polypeptide backbone Journal of Molecular Biology. 235: 27-32. PMID 8289248 DOI: 10.1016/S0022-2836(05)80008-7 |
0.454 |
|
1993 |
Gittis AG, Stites WE, Lattman EE. The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. Journal of Molecular Biology. 232: 718-24. PMID 8355268 DOI: 10.1006/Jmbi.1993.1425 |
0.417 |
|
1992 |
James E, Wu PG, Stites W, Brand L. Compact denatured state of a staphylococcal nuclease mutant by guanidinium as determined by resonance energy transfer Biochemistry. 31: 10217-10225. PMID 1420143 |
0.379 |
|
1991 |
Stites WE, Gittis AG, Lattman EE, Shortle D. In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core. Journal of Molecular Biology. 221: 7-14. PMID 1920420 DOI: 10.1016/0022-2836(91)80195-Z |
0.557 |
|
1990 |
Shortle D, Stites WE, Meeker AK. Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease Biochemistry. 29: 8033-8041. PMID 2261461 DOI: 10.1021/Bi00487A007 |
0.557 |
|
Show low-probability matches. |