Year |
Citation |
Score |
2023 |
Cina NP, Frank DW, Klug CS. Residues within the LptC transmembrane helix are critical for Escherichia coli LptB FG ATPase regulation. Protein Science : a Publication of the Protein Society. e4879. PMID 38131105 DOI: 10.1002/pro.4879 |
0.362 |
|
2023 |
Schultz KM, Schneider JR, Fischer MA, Cina NP, Riegert MO, Frank DW, Klug CS. Binding and transport of LPS occurs through the coordinated combination of an array of sites across the entire E. coli LPS transport protein LptA. Protein Science : a Publication of the Protein Society. e4724. PMID 37417889 DOI: 10.1002/pro.4724 |
0.353 |
|
2022 |
Schultz KM, Klug CS. Use of Site-Directed Spin Labeling EPR Spectroscopy to Study Protein-LPS Interactions. Methods in Molecular Biology (Clifton, N.J.). 2548: 83-96. PMID 36151493 DOI: 10.1007/978-1-0716-2581-1_6 |
0.372 |
|
2022 |
Perry-Hauser NA, Bennett Hopkins J, Zhuo Y, Zheng C, Perez I, Schultz KM, Vishnivetskiy SA, Kaya AI, Sharma P, Dalby KN, Young Chung K, Klug CS, Gurevich VV, Iverson TM. The two non-visual arrestins engage ERK2 differently. Journal of Molecular Biology. 167465. PMID 35077767 DOI: 10.1016/j.jmb.2022.167465 |
0.311 |
|
2020 |
Chen Q, Zhuo Y, Sharma P, Perez I, Francis DJ, Chakravarthy S, Vishnivetskiy SA, Berndt S, Hanson SM, Zhan X, Brooks EK, Altenbach C, Hubbell WL, Klug CS, Iverson TM, et al. An eight amino acid segment controls oligomerization and preferred conformation of the two non-visual arrestins. Journal of Molecular Biology. 166790. PMID 33387531 DOI: 10.1016/j.jmb.2020.166790 |
0.622 |
|
2020 |
Zhuo Y, Klug C, Marchese A. Identifying β‐arrestin1 conformational states by a non‐GPCR binding partner The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.07155 |
0.387 |
|
2018 |
Schultz KM, Fischer MA, Noey EL, Klug CS. Disruption of the E. coli LptC dimerization interface and characterization of lipopolysaccharide and LptA binding to monomeric LptC. Protein Science : a Publication of the Protein Society. PMID 29672978 DOI: 10.1002/Pro.3429 |
0.413 |
|
2017 |
Schultz KM, Klug CS. Characterization of and lipopolysaccharide binding to the E. coli LptC protein dimer. Protein Science : a Publication of the Protein Society. PMID 29024084 DOI: 10.1002/Pro.3322 |
0.434 |
|
2017 |
Schultz KM, Lundquist TJ, Klug CS. Lipopolysaccharide (LPS) binding to the periplasmic protein LptA. Protein Science : a Publication of the Protein Society. PMID 28419595 DOI: 10.1002/Pro.3177 |
0.3 |
|
2017 |
Schultz KM, Lundquist TJ, Fischer MA, Klug CS. LPS Binding to LptA Biophysical Journal. 112: 446a. DOI: 10.1016/J.Bpj.2016.11.2390 |
0.357 |
|
2016 |
Petrou VI, Herrera CM, Schultz KM, Clarke OB, Vendome J, Tomasek D, Banerjee S, Rajashankar KR, Belcher Dufrisne M, Kloss B, Kloppmann E, Rost B, Klug CS, Trent MS, Shapiro L, et al. Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation. Science (New York, N.Y.). 351: 608-12. PMID 26912703 DOI: 10.1126/Science.Aad1172 |
0.383 |
|
2016 |
Petrou VI, Herrera CM, Schultz KM, Clarke OB, Vendome J, Tomasek D, Banerjee S, Rajashankar KR, Kloss B, Kloppmann E, Rost B, Klug CS, Trent MS, Shapiro L, Mancia F. ArnT: Structure and Mechanism of the Aminoarabinose Transferase Responsible for Resistance to Polymyxin-Class Antibiotics Biophysical Journal. 110: 38a. DOI: 10.1016/J.Bpj.2015.11.274 |
0.362 |
|
2015 |
Alvarez FJ, Orelle C, Huang Y, Bajaj R, Everly RM, Klug CS, Davidson AL. Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter. Molecular Microbiology. PMID 26268698 DOI: 10.1111/mmi.13165 |
0.427 |
|
2015 |
Petrou VI, Clarke OB, Schultz KM, Tomasek D, Kloss B, Banerjee S, Rajashankar KR, Klug CS, Shapiro L, Mancia F. Crystal Structure of the Bacterial Aminoarabinose Transferase ArnT Biophysical Journal. 108: 253a. DOI: 10.1016/J.Bpj.2014.11.1400 |
0.396 |
|
2014 |
Zhuo Y, Vishnivetskiy SA, Zhan X, Gurevich VV, Klug CS. Identification of receptor binding-induced conformational changes in non-visual arrestins. The Journal of Biological Chemistry. 289: 20991-1002. PMID 24867953 DOI: 10.1074/Jbc.M114.560680 |
0.352 |
|
2014 |
Chen Q, Zhuo Y, Kim M, Hanson SM, Francis DJ, Vishnivetskiy SA, Altenbach C, Klug CS, Hubbell WL, Gurevich VV. Self-association of arrestin family members. Handbook of Experimental Pharmacology. 219: 205-23. PMID 24292832 DOI: 10.1007/978-3-642-41199-1_11 |
0.543 |
|
2013 |
Dellisanti CD, Ghosh B, Hanson SM, Raspanti JM, Grant VA, Diarra GM, Schuh AM, Satyshur K, Klug CS, Czajkowski C. Site-directed spin labeling reveals pentameric ligand-gated ion channel gating motions. Plos Biology. 11: e1001714. PMID 24260024 DOI: 10.1371/Journal.Pbio.1001714 |
0.3 |
|
2013 |
Schultz KM, Feix JB, Klug CS. Disruption of LptA oligomerization and affinity of the LptA-LptC interaction. Protein Science : a Publication of the Protein Society. 22: 1639-45. PMID 24123237 DOI: 10.1002/Pro.2369 |
0.415 |
|
2013 |
Bajaj R, Park MI, Paul LN, Klug CS, Davidson AL. Structural Mechanism of Action of Binding Protein Independent Mutant MalG511 of Escherichia Coli Maltose Transporter Biophysical Journal. 104: 111a. DOI: 10.1016/J.Bpj.2012.11.646 |
0.378 |
|
2012 |
Francis DJ, Hubbell WL, Klug CS. Probing Protein Secondary Structure using EPR: Investigating a Dynamic Region of Visual Arrestin. Applied Magnetic Resonance. 43: 405-419. PMID 25419051 DOI: 10.1007/S00723-012-0369-Y |
0.615 |
|
2012 |
Merten JA, Schultz KM, Klug CS. Concentration-dependent oligomerization and oligomeric arrangement of LptA. Protein Science : a Publication of the Protein Society. 21: 211-8. PMID 22109962 DOI: 10.1002/Pro.2004 |
0.358 |
|
2011 |
Vishnivetskiy SA, Gimenez LE, Francis DJ, Hanson SM, Hubbell WL, Klug CS, Gurevich VV. Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins. The Journal of Biological Chemistry. 286: 24288-99. PMID 21471193 DOI: 10.1074/Jbc.M110.213835 |
0.631 |
|
2011 |
Schultz KM, Merten JA, Klug CS. Characterization of the E506Q and H537A dysfunctional mutants in the E. coli ABC transporter MsbA. Biochemistry. 50: 3599-608. PMID 21462989 DOI: 10.1021/Bi101666P |
0.399 |
|
2011 |
Schultz KM, Merten JA, Klug CS. Effects of the L511P and D512G mutations on the Escherichia coli ABC transporter MsbA. Biochemistry. 50: 2594-602. PMID 21344946 DOI: 10.1021/Bi1018418 |
0.346 |
|
2011 |
Joan F, Alvarez D, Orelle C, Klug CS, Davidson A. Both Lobes of Maltose Binding Protein are Engaged in Stabilization of the Semi-Open State of the Malk Dimer in the Maltose ABC Transporter Biophysical Journal. 100: 134a. DOI: 10.1016/j.bpj.2010.12.937 |
0.329 |
|
2010 |
Vishnivetskiy SA, Francis D, Van Eps N, Kim M, Hanson SM, Klug CS, Hubbell WL, Gurevich VV. The role of arrestin alpha-helix I in receptor binding. Journal of Molecular Biology. 395: 42-54. PMID 19883657 DOI: 10.1016/J.Jmb.2009.10.058 |
0.644 |
|
2009 |
Impellitteri NA, Merten JA, Bretscher LE, Klug CS. Identification of Functionally Important Sites within the Cysteine-Free Inner Membrane Transferase Protein ArnT Biophysical Journal. 96: 327a-328a. DOI: 10.1016/j.bpj.2008.12.1647 |
0.34 |
|
2008 |
Westfahl KM, Merten JA, Buchaklian AH, Klug CS. Functionally important ATP binding and hydrolysis sites in Escherichia coli MsbA. Biochemistry. 47: 13878-86. PMID 19053284 DOI: 10.1021/Bi801745U |
0.766 |
|
2008 |
Bretscher LE, Buchaklian AH, Klug CS. Spin-labeled lipid A. Analytical Biochemistry. 382: 129-31. PMID 18760259 DOI: 10.1016/J.Ab.2008.08.001 |
0.732 |
|
2008 |
Orelle C, Ayvaz T, Everly RM, Klug CS, Davidson AL. Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter. Proceedings of the National Academy of Sciences of the United States of America. 105: 12837-42. PMID 18725638 DOI: 10.1073/pnas.0803799105 |
0.418 |
|
2008 |
Hanson SM, Dawson ES, Francis DJ, Van Eps N, Klug CS, Hubbell WL, Meiler J, Gurevich VV. A model for the solution structure of the rod arrestin tetramer. Structure (London, England : 1993). 16: 924-34. PMID 18547524 DOI: 10.1016/J.Str.2008.03.006 |
0.6 |
|
2008 |
Klug CS, Feix JB. Methods and applications of site-directed spin labeling EPR spectroscopy. Methods in Cell Biology. 84: 617-58. PMID 17964945 DOI: 10.1016/S0091-679X(07)84020-9 |
0.351 |
|
2007 |
Hanson SM, Cleghorn WM, Francis DJ, Vishnivetskiy SA, Raman D, Song X, Nair KS, Slepak VZ, Klug CS, Gurevich VV. Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity. Journal of Molecular Biology. 368: 375-87. PMID 17359998 DOI: 10.1016/J.Jmb.2007.02.053 |
0.627 |
|
2007 |
Hanson SM, Van Eps N, Francis DJ, Altenbach C, Vishnivetskiy SA, Arshavsky VY, Klug CS, Hubbell WL, Gurevich VV. Structure and function of the visual arrestin oligomer. The Embo Journal. 26: 1726-36. PMID 17332750 DOI: 10.1038/Sj.Emboj.7601614 |
0.622 |
|
2007 |
Cleghorn WM, Hanson SM, Francis DJ, Vishnivetskiy SA, Raman D, Song X, Klug CS, Gurevich VV. Arrestin‐dependent mobilization of signaling proteins to the cytoskeleton The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A613-C |
0.529 |
|
2006 |
Wu N, Hanson SM, Francis DJ, Vishnivetskiy SA, Thibonnier M, Klug CS, Shoham M, Gurevich VV. Arrestin binding to calmodulin: a direct interaction between two ubiquitous signaling proteins. Journal of Molecular Biology. 364: 955-63. PMID 17054984 DOI: 10.1016/J.Jmb.2006.09.075 |
0.643 |
|
2006 |
Buchaklian AH, Klug CS. Characterization of the LSGGQ and H motifs from the Escherichia coli lipid A transporter MsbA. Biochemistry. 45: 12539-46. PMID 17029409 DOI: 10.1021/Bi060830A |
0.768 |
|
2006 |
Hanson SM, Francis DJ, Vishnivetskiy SA, Kolobova EA, Hubbell WL, Klug CS, Gurevich VV. Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 103: 4900-5. PMID 16547131 DOI: 10.1073/Pnas.0600733103 |
0.629 |
|
2006 |
Hanson SM, Francis DJ, Vishnivetskiy SA, Klug CS, Gurevich VV. Visual arrestin binding to microtubules involves a distinct conformational change. The Journal of Biological Chemistry. 281: 9765-72. PMID 16461350 DOI: 10.1074/Jbc.M510738200 |
0.664 |
|
2005 |
Buchaklian AH, Klug CS. Characterization of the Walker A motif of MsbA using site-directed spin labeling electron paramagnetic resonance spectroscopy. Biochemistry. 44: 5503-9. PMID 15807544 DOI: 10.1021/Bi047568V |
0.777 |
|
2004 |
Buchaklian AH, Funk AL, Klug CS. Resting state conformation of the MsbA homodimer as studied by site-directed spin labeling. Biochemistry. 43: 8600-6. PMID 15222771 DOI: 10.1021/Bi0497751 |
0.761 |
|
2004 |
Austermuhle MI, Hall JA, Klug CS, Davidson AL. Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport. The Journal of Biological Chemistry. 279: 28243-50. PMID 15117946 DOI: 10.1074/jbc.M403508200 |
0.451 |
|
1998 |
Klug CS, Eaton SS, Eaton GR, Feix JB. Ligand-induced conformational change in the ferric enterobactin receptor FepA as studied by site-directed spin labeling and time-domain ESR. Biochemistry. 37: 9016-23. PMID 9636045 DOI: 10.1021/Bi980144E |
0.353 |
|
1997 |
Klug CS, Su W, Feix JB. Mapping of the residues involved in a proposed beta-strand located in the ferric enterobactin receptor FepA using site-directed spin-labeling. Biochemistry. 36: 13027-33. PMID 9335564 DOI: 10.1021/bi971232m |
0.315 |
|
1995 |
Klug CS, Su W, Liu J, Klebba PE, Feix JB. Denaturant unfolding of the ferric enterobactin receptor and ligand-induced stabilization studied by site-directed spin labeling. Biochemistry. 34: 14230-6. PMID 7578022 DOI: 10.1021/bi00043a030 |
0.377 |
|
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