| Year |
Citation |
Score |
| 2020 |
Ortega G, Mariottini D, Troina A, Dahlquist FW, Ricci F, Plaxco KW. Rational design to control the trade-off between receptor affinity and cooperativity. Proceedings of the National Academy of Sciences of the United States of America. PMID 32727893 DOI: 10.1073/Pnas.2006254117 |
0.494 |
|
| 2018 |
Kang D, Parolo C, Sun S, Ogden N, Dahlquist FW, Plaxco KW. Expanding the scope of protein-detecting electrochemical DNA "scaffold" sensors. Acs Sensors. PMID 29877078 DOI: 10.1021/Acssensors.8B00311 |
0.468 |
|
| 2017 |
Kang D, Sun S, Kurnik M, Morales DP, Dahlquist FW, Plaxco KW. A new architecture for reagentless, protein-based electro-chemical biosensors. Journal of the American Chemical Society. PMID 28789522 DOI: 10.1021/Jacs.7B05953 |
0.525 |
|
| 2015 |
Dahlquist FW. Flagellar Motor Architecture Biophysical Journal. 108: 42a. DOI: 10.1016/J.Bpj.2014.11.257 |
0.376 |
|
| 2014 |
Wang X, Vallurupalli P, Vu A, Lee K, Sun S, Bai WJ, Wu C, Zhou H, Shea JE, Kay LE, Dahlquist FW. The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activity. Biochemistry. 53: 855-61. PMID 24444349 DOI: 10.1021/Bi4012379 |
0.615 |
|
| 2013 |
Ortega DR, Mo G, Lee K, Zhou H, Baudry J, Dahlquist FW, Zhulin IB. Conformational coupling between receptor and kinase binding sites through a conserved salt bridge in a signaling complex scaffold protein. Plos Computational Biology. 9: e1003337. PMID 24244143 DOI: 10.1371/Journal.Pcbi.1003337 |
0.616 |
|
| 2013 |
Matje DM, Krivacic CT, Dahlquist FW, Reich NO. Distal structural elements coordinate a conserved base flipping network. Biochemistry. 52: 1669-76. PMID 23409802 DOI: 10.1021/Bi301284F |
0.326 |
|
| 2013 |
Matje DM, Zhou H, Smith DA, Neely RK, Dryden DT, Jones AC, Dahlquist FW, Reich NO. Enzyme-promoted base flipping controls DNA methylation fidelity. Biochemistry. 52: 1677-85. PMID 23409782 DOI: 10.1021/Bi3012912 |
0.369 |
|
| 2012 |
Wang X, Wu C, Vu A, Shea JE, Dahlquist FW. Computational and experimental analyses reveal the essential roles of interdomain linkers in the biological function of chemotaxis histidine kinase CheA. Journal of the American Chemical Society. 134: 16107-10. PMID 22992224 DOI: 10.1021/Ja3056694 |
0.593 |
|
| 2012 |
Vartanian AS, Paz A, Fortgang EA, Abramson J, Dahlquist FW. Structure of flagellar motor proteins in complex allows for insights into motor structure and switching. The Journal of Biological Chemistry. 287: 35779-83. PMID 22896702 DOI: 10.1074/Jbc.C112.378380 |
0.794 |
|
| 2012 |
Levenson R, Zhou H, Dahlquist FW. Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG. Biochemistry. 51: 5052-60. PMID 22670715 DOI: 10.1021/Bi3004582 |
0.447 |
|
| 2012 |
Wang X, Vu A, Lee K, Dahlquist FW. CheA-receptor interaction sites in bacterial chemotaxis. Journal of Molecular Biology. 422: 282-90. PMID 22659323 DOI: 10.1016/J.Jmb.2012.05.023 |
0.55 |
|
| 2012 |
Mo G, Zhou H, Kawamura T, Dahlquist FW. Solution structure of a complex of the histidine autokinase CheA with its substrate CheY. Biochemistry. 51: 3786-98. PMID 22494339 DOI: 10.1021/Bi300147M |
0.681 |
|
| 2012 |
Vu A, Wang X, Zhou H, Dahlquist FW. The receptor-CheW binding interface in bacterial chemotaxis. Journal of Molecular Biology. 415: 759-67. PMID 22155081 DOI: 10.1016/J.Jmb.2011.11.043 |
0.59 |
|
| 2011 |
Vu A, Hamel DJ, Zhou H, Dahlquist FW. The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima. Journal of Biomolecular Nmr. 51: 49-55. PMID 21947914 DOI: 10.1007/S10858-011-9540-2 |
0.782 |
|
| 2011 |
Kawamura T, Vartanian AS, Zhou H, Dahlquist FW. The design involved in PapI and Lrp regulation of the pap operon. Journal of Molecular Biology. 409: 311-32. PMID 21338611 DOI: 10.1016/J.Jmb.2011.01.058 |
0.774 |
|
| 2011 |
Matje DM, Coughlin DF, Connolly BA, Dahlquist FW, Reich NO. Determinants of precatalytic conformational transitions in the DNA cytosine methyltransferase M.HhaI. Biochemistry. 50: 1465-73. PMID 21229971 DOI: 10.1021/Bi101446G |
0.305 |
|
| 2011 |
Kenrick S, Vartanian A, Dahlquist F. Revealing the Affinity of Individual and Combined Flig Domains for Flim in the Bacterial Flagellar Motor Switch Complex by CG-MALS Biophysical Journal. 100: 54a. DOI: 10.7490/F1000Research.1092808.1 |
0.776 |
|
| 2011 |
Vu A, Hamel D, Zhou H, Dahlquist F. Solution Structure of Histidine Phosphotransfer Domain of CheA Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Ld6/Pdb |
0.766 |
|
| 2011 |
Maeno A, Kitahara R, Dahlquist F, Yokoyama S, Mulder F, Akasaka K. 1H1348 Cavity hydration as a gateway to internal mobility : A high pressure ^<13>C and ^<15>N-NMR study of T4 lysozyme(Protein: Property 2,The 49th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 51: S49. DOI: 10.2142/Biophys.51.S49_1 |
0.3 |
|
| 2009 |
Zhou H, Purdy MM, Dahlquist FW, Reich NO. The recognition pathway for the DNA cytosine methyltransferase M.HhaI. Biochemistry. 48: 7807-16. PMID 19580326 DOI: 10.1021/Bi900502G |
0.316 |
|
| 2009 |
Hao S, Hamel D, Zhou H, Dahlquist FW. Structural basis for the localization of the chemotaxis phosphatase CheZ by CheAS. Journal of Bacteriology. 191: 5842-4. PMID 19502407 DOI: 10.1128/Jb.00323-09 |
0.742 |
|
| 2009 |
Dyer CM, Vartanian AS, Zhou H, Dahlquist FW. A molecular mechanism of bacterial flagellar motor switching. Journal of Molecular Biology. 388: 71-84. PMID 19358329 DOI: 10.1016/J.Jmb.2009.02.004 |
0.772 |
|
| 2008 |
Peterson DW, Zhou H, Dahlquist FW, Lew J. A soluble oligomer of tau associated with fiber formation analyzed by NMR. Biochemistry. 47: 7393-404. PMID 18558718 DOI: 10.1021/Bi702466A |
0.307 |
|
| 2007 |
Caballero-Manrique E, Bray JK, Deutschman WA, Dahlquist FW, Guenza MG. A theory of protein dynamics to predict NMR relaxation. Biophysical Journal. 93: 4128-40. PMID 17766356 DOI: 10.1529/Biophysj.107.111849 |
0.307 |
|
| 2007 |
Zhou H, Shatz W, Purdy MM, Fera N, Dahlquist FW, Reich NO. Long-range structural and dynamical changes induced by cofactor binding in DNA methyltransferase M.HhaI. Biochemistry. 46: 7261-8. PMID 17523600 DOI: 10.1021/Bi602662E |
0.408 |
|
| 2007 |
Cellitti J, Llinas M, Echols N, Shank EA, Gillespie B, Kwon E, Crowder SM, Dahlquist FW, Alber T, Marqusee S. Exploring subdomain cooperativity in T4 lysozyme I: structural and energetic studies of a circular permutant and protein fragment. Protein Science : a Publication of the Protein Society. 16: 842-51. PMID 17400926 DOI: 10.1110/Ps.062628607 |
0.808 |
|
| 2007 |
Kawamura T, Le LU, Zhou H, Dahlquist FW. Solution structure of Escherichia coli PapI, a key regulator of the pap pili phase variation. Journal of Molecular Biology. 365: 1130-42. PMID 17109885 DOI: 10.1016/J.Jmb.2006.10.066 |
0.492 |
|
| 2007 |
Maeno A, Kitahara R, Yokoyama S, Dahlquist FW, Mulder FAA, Akasaka K. 2P035 Detection of Cavity-based Fluctuations in a T4 Lysozyme Mutant. A Variable Pressure NMR Study(Proteins-structure and structure-function relationship,Poster Presentations) Seibutsu Butsuri. 47: S121. DOI: 10.2142/Biophys.47.S121_4 |
0.338 |
|
| 2006 |
Dyer CM, Dahlquist FW. Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM. Journal of Bacteriology. 188: 7354-63. PMID 17050923 DOI: 10.1128/Jb.00637-06 |
0.811 |
|
| 2006 |
Hamel DJ, Zhou H, Starich MR, Byrd RA, Dahlquist FW. Chemical-shift-perturbation mapping of the phosphotransfer and catalytic domain interaction in the histidine autokinase CheA from Thermotoga maritima. Biochemistry. 45: 9509-17. PMID 16878985 DOI: 10.1021/Bi060798K |
0.74 |
|
| 2006 |
Maeno A, Kitahara R, Dahlquist FW, Yokoyama S, Mulder FAA, Akasaka K. 2P057 Variable pressure NMR reveals role of cavity in protein dynamics(29. Protein structure and dynamics (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) Seibutsu Butsuri. 46: S310. DOI: 10.2142/Biophys.46.S310_1 |
0.309 |
|
| 2005 |
Hamel DJ, Dahlquist FW. The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy. Journal of the American Chemical Society. 127: 9676-7. PMID 15998058 DOI: 10.1021/Ja052517M |
0.721 |
|
| 2005 |
Quezada CM, Hamel DJ, Gradinaru C, Bilwes AM, Dahlquist FW, Crane BR, Simon MI. Structural and chemical requirements for histidine phosphorylation by the chemotaxis kinase CheA. The Journal of Biological Chemistry. 280: 30581-5. PMID 15994328 DOI: 10.1074/Jbc.M505316200 |
0.726 |
|
| 2005 |
Kingston R, Hamel D, Dahlquist F, Matthews B. Measles virus P protein (amino acids 457-407) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr6568 |
0.696 |
|
| 2004 |
Dyer CM, Quillin ML, Campos A, Lu J, McEvoy MM, Hausrath AC, Westbrook EM, Matsumura P, Matthews BW, Dahlquist FW. Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide. Journal of Molecular Biology. 342: 1325-35. PMID 15351654 DOI: 10.1016/J.Jmb.2004.07.084 |
0.804 |
|
| 2004 |
Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW. Structural basis for the attachment of a paramyxoviral polymerase to its template. Proceedings of the National Academy of Sciences of the United States of America. 101: 8301-6. PMID 15159535 DOI: 10.1073/Pnas.0402690101 |
0.747 |
|
| 2003 |
Korzhnev DM, Orekhov VY, Dahlquist FW, Kay LE. Off-resonance R1rho relaxation outside of the fast exchange limit: an experimental study of a cavity mutant of T4 lysozyme. Journal of Biomolecular Nmr. 26: 39-48. PMID 12766401 DOI: 10.1023/A:1023039902737 |
0.343 |
|
| 2002 |
Griswold IJ, Dahlquist FW. The dynamic behavior of CheW from Thermotoga maritima in solution, as determined by nuclear magnetic resonance: implications for potential protein-protein interaction sites. Biophysical Chemistry. 101: 359-73. PMID 12488014 DOI: 10.1016/S0301-4622(02)00157-6 |
0.808 |
|
| 2002 |
Eldridge AM, Kang HS, Johnson E, Gunsalus R, Dahlquist FW. Effect of phosphorylation on the interdomain interaction of the response regulator, NarL. Biochemistry. 41: 15173-80. PMID 12484754 DOI: 10.1021/Bi026254+ |
0.807 |
|
| 2002 |
Griswold IJ, Dahlquist FW. Bigger is better: megadalton protein NMR in solution. Nature Structural Biology. 9: 567-8. PMID 12145644 DOI: 10.1038/Nsb0802-567 |
0.779 |
|
| 2002 |
Boukhvalova MS, Dahlquist FW, Stewart RC. CheW binding interactions with CheA and Tar. Importance for chemotaxis signaling in Escherichia coli. The Journal of Biological Chemistry. 277: 22251-9. PMID 11923283 DOI: 10.1074/Jbc.M110908200 |
0.776 |
|
| 2002 |
Mulder FA, Hon B, Mittermaier A, Dahlquist FW, Kay LE. Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 124: 1443-51. PMID 11841314 DOI: 10.1021/Ja0119806 |
0.709 |
|
| 2002 |
Griswold IJ, Zhou H, Matison M, Swanson RV, McIntosh LP, Simon MI, Dahlquist FW. The solution structure and interactions of CheW from Thermotoga maritima. Nature Structural Biology. 9: 121-5. PMID 11799399 DOI: 10.1038/Nsb753 |
0.809 |
|
| 2001 |
Mulder FA, Mittermaier A, Hon B, Dahlquist FW, Kay LE. Studying excited states of proteins by NMR spectroscopy. Nature Structural Biology. 8: 932-5. PMID 11685237 DOI: 10.1038/Nsb1101-932 |
0.72 |
|
| 2001 |
Skrynnikov NR, Mulder FA, Hon B, Dahlquist FW, Kay LE. Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 4556-66. PMID 11457242 DOI: 10.1021/Ja004179P |
0.721 |
|
| 2001 |
Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE. Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 967-75. PMID 11456632 DOI: 10.1021/Ja003447G |
0.734 |
|
| 2001 |
Goto NK, Skrynnikov NR, Dahlquist FW, Kay LE. What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR. Journal of Molecular Biology. 308: 745-64. PMID 11350172 DOI: 10.1006/Jmbi.2001.4614 |
0.4 |
|
| 2001 |
Giesen AW, Bae LC, Barrett CL, Chyba JA, Chaykovsky MM, Cheng MC, Murray JH, Oliver EJ, Sullivan SM, Brown JM, Dahlquist FW, Homans SW. Measurement of one-bond 1H-13C, couplings in backbone-labelled proteins. Journal of Biomolecular Nmr. 19: 255-60. PMID 11330812 DOI: 10.1023/A:1011298531256 |
0.309 |
|
| 2000 |
Mulder FA, Hon B, Muhandiram DR, Dahlquist FW, Kay LE. Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR. Biochemistry. 39: 12614-22. PMID 11027141 DOI: 10.1021/Bi001351T |
0.728 |
|
| 2000 |
Anderson JS, Forman MD, Modleski S, Dahlquist FW, Baxter SM. Cooperative ordering in homeodomain-DNA recognition: solution structure and dynamics of the MATa1 homeodomain. Biochemistry. 39: 10045-54. PMID 10955992 DOI: 10.1021/Bi000677Z |
0.35 |
|
| 2000 |
Halkides CJ, McEvoy MM, Casper E, Matsumura P, Volz K, Dahlquist FW. The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY. Biochemistry. 39: 5280-6. PMID 10819997 DOI: 10.1021/Bi9925524 |
0.377 |
|
| 2000 |
Barrick D, Dahlquist FW. Trans-substitution of the proximal hydrogen bond in myoglobin: I. Structural consequences of hydrogen bond deletion. Proteins. 39: 278-90. PMID 10813811 DOI: 10.1002/(Sici)1097-0134(20000601)39:4<278::Aid-Prot20>3.0.Co;2-T |
0.313 |
|
| 2000 |
Yang G, Cecconi C, Baase WA, Vetter IR, Breyer WA, Haack JA, Matthews BW, Dahlquist FW, Bustamante C. Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 97: 139-44. PMID 10618384 DOI: 10.1073/Pnas.97.1.139 |
0.324 |
|
| 1999 |
Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW. Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry. 38: 14451-60. PMID 10545167 DOI: 10.1021/Bi9915519 |
0.39 |
|
| 1999 |
Llinás M, Gillespie B, Dahlquist FW, Marqusee S. The energetics of T4 lysozyme reveal a hierarchy of conformations. Nature Structural Biology. 6: 1072-8. PMID 10542101 DOI: 10.1038/14956 |
0.781 |
|
| 1999 |
McEvoy MM, Bren A, Eisenbach M, Dahlquist FW. Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein fliM. Journal of Molecular Biology. 289: 1423-33. PMID 10373376 DOI: 10.1006/Jmbi.1999.2830 |
0.419 |
|
| 1999 |
Bertelsen EB, Zhou H, Lowry DF, Flynn GC, Dahlquist FW. Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution. Protein Science : a Publication of the Protein Society. 8: 343-54. PMID 10048327 DOI: 10.1110/Ps.8.2.343 |
0.421 |
|
| 1998 |
Blat Y, Gillespie B, Bren A, Dahlquist FW, Eisenbach M. Regulation of phosphatase activity in bacterial chemotaxis. Journal of Molecular Biology. 284: 1191-9. PMID 9837737 DOI: 10.1006/Jmbi.1998.2224 |
0.772 |
|
| 1998 |
Halkides CJ, Zhu X, Phillion DP, Matsumura P, Dahlquist FW. Synthesis and biochemical characterization of an analogue of CheY-phosphate, a signal transduction protein in bacterial chemotaxis. Biochemistry. 37: 13674-80. PMID 9753454 DOI: 10.1021/Bi9806293 |
0.424 |
|
| 1998 |
McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW. Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proceedings of the National Academy of Sciences of the United States of America. 95: 7333-8. PMID 9636149 DOI: 10.1073/Pnas.95.13.7333 |
0.428 |
|
| 1998 |
Usher KC, de la Cruz AF, Dahlquist FW, Swanson RV, Simon MI, Remington SJ. Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability. Protein Science : a Publication of the Protein Society. 7: 403-12. PMID 9521117 DOI: 10.1002/Pro.5560070221 |
0.373 |
|
| 1998 |
Daughdrill GW, Hanely LJ, Dahlquist FW. The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations. Biochemistry. 37: 1076-82. PMID 9454599 DOI: 10.1021/Bi971952T |
0.369 |
|
| 1997 |
McEvoy MM, Dahlquist FW. Phosphohistidines in bacterial signaling. Current Opinion in Structural Biology. 7: 793-7. PMID 9434897 DOI: 10.1016/S0959-440X(97)80148-0 |
0.38 |
|
| 1997 |
Liu T, Ryan M, Dahlquist FW, Griffith OH. Determination of pKa values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus by NMR spectroscopy and site-directed mutagenesis. Protein Science : a Publication of the Protein Society. 6: 1937-44. PMID 9300493 DOI: 10.1002/Pro.5560060914 |
0.38 |
|
| 1997 |
Feher VA, Zapf JW, Hoch JA, Whiteley JM, McIntosh LP, Rance M, Skelton NJ, Dahlquist FW, Cavanagh J. High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition. Biochemistry. 36: 10015-25. PMID 9254596 DOI: 10.1021/Bi970816L |
0.427 |
|
| 1997 |
Wilkens S, Dunn SD, Chandler J, Dahlquist FW, Capaldi RA. Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase. Nature Structural Biology. 4: 198-201. PMID 9164460 DOI: 10.1038/Nsb0397-198 |
0.343 |
|
| 1997 |
Hall DA, Maus DC, Gerfen GJ, Inati SJ, Becerra LR, Dahlquist FW, Griffin RG. Polarization-enhanced NMR spectroscopy of biomolecules in frozen solution. Science (New York, N.Y.). 276: 930-2. PMID 9139651 DOI: 10.1126/Science.276.5314.930 |
0.478 |
|
| 1997 |
Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW. The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. Nature Structural Biology. 4: 285-91. PMID 9095196 DOI: 10.1038/Nsb0497-285 |
0.416 |
|
| 1997 |
Zhou H, Dahlquist FW. Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR. Biochemistry. 36: 699-710. PMID 9020767 DOI: 10.1021/Bi961663P |
0.419 |
|
| 1997 |
Barrick D, Ho NT, Simplaceanu V, Dahlquist FW, Ho C. A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin. Nature Structural Biology. 4: 78-83. PMID 8989328 DOI: 10.1038/Nsb0197-78 |
0.367 |
|
| 1997 |
McEvoy MM, de la Cruz AF, Dahlquist FW. Large modular proteins by NMR. Nature Structural Biology. 4: 9. PMID 8989314 DOI: 10.1038/Nsb0197-9 |
0.358 |
|
| 1996 |
Feher VA, Baldwin EP, Dahlquist FW. Access of ligands to cavities within the core of a protein is rapid. Nature Structural Biology. 3: 516-21. PMID 8646537 DOI: 10.1038/Nsb0696-516 |
0.375 |
|
| 1996 |
McEvoy MM, Muhandiram DR, Kay LE, Dahlquist FW. Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. Biochemistry. 35: 5633-40. PMID 8639521 DOI: 10.1021/Bi952707H |
0.466 |
|
| 1996 |
Zhou H, McEvoy MM, Lowry DF, Swanson RV, Simon MI, Dahlquist FW. Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker. Biochemistry. 35: 433-43. PMID 8555213 DOI: 10.1021/Bi951960E |
0.395 |
|
| 1995 |
Feher VA, Zapf JW, Hoch JA, Dahlquist FW, Whiteley JM, Cavanagh J. 1H, 15N, and 13C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of the Bacillus subtilis response regulator, Spo0F, determined by heteronuclear high-resolution NMR. Protein Science : a Publication of the Protein Society. 4: 1801-14. PMID 8528078 DOI: 10.1002/Pro.5560040915 |
0.427 |
|
| 1995 |
Fischer MW, Majumdar A, Dahlquist FW, Zuiderweg ER. 15N, 13C, and 1H NMR assignments and secondary structure for T4-lysozyme. Journal of Magnetic Resonance. Series B. 108: 143-54. PMID 7648012 DOI: 10.1006/Jmrb.1995.1115 |
0.351 |
|
| 1995 |
Wilkens S, Dahlquist FW, McIntosh LP, Donaldson LW, Capaldi RA. Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nature Structural Biology. 2: 961-7. PMID 7583669 DOI: 10.1038/Nsb1195-961 |
0.384 |
|
| 1995 |
McEvoy MM, Zhou H, Roth AF, Lowry DF, Morrison TB, Kay LE, Dahlquist FW. Nuclear magnetic resonance assignments and global fold of a CheY-binding domain in CheA, the chemotaxis-specific kinase of Escherichia coli. Biochemistry. 34: 13871-80. PMID 7577981 DOI: 10.1021/Bi00042A019 |
0.395 |
|
| 1995 |
Zhou H, Lowry DF, Swanson RV, Simon MI, Dahlquist FW. NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics. Biochemistry. 34: 13858-70. PMID 7577980 DOI: 10.1021/Bi00042A018 |
0.427 |
|
| 1995 |
Swanson RV, Lowry DF, Matsumura P, McEvoy MM, Simon MI, Dahlquist FW. Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface. Nature Structural Biology. 2: 906-10. PMID 7552716 DOI: 10.1038/Nsb1095-906 |
0.426 |
|
| 1994 |
Cavanagh J, Zapf J, Hoch JA, Feher V, Dahlquist FW, Whiteley JM. Aspartyl phosphates in the regulatory control of bacterial response. Amino Acids. 6: 131-40. PMID 24190783 DOI: 10.1007/Bf00805841 |
0.356 |
|
| 1994 |
Moy FJ, Lowry DF, Matsumura P, Dahlquist FW, Krywko JE, Domaille PJ. Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy. Biochemistry. 33: 10731-42. PMID 8075074 DOI: 10.1021/Bi00201A022 |
0.408 |
|
| 1994 |
Yamazaki T, Lee W, Revington M, Mattiello DL, Dahlquist FW, Arrowsmith CH, Kay LE. An HNCA pulse scheme for the backbone assignment of 15N,13C,2H-labeled proteins: Application to a 37-kDa Trp repressor-DNA complex Journal of the American Chemical Society. 116: 6464-6465. DOI: 10.1021/Ja00093A069 |
0.305 |
|
| 1993 |
Heinz DW, Baase WA, Dahlquist FW, Matthews BW. How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme. Nature. 361: 561-4. PMID 8429913 DOI: 10.1038/361561A0 |
0.346 |
|
| 1993 |
Flynn GC, Beckers CJ, Baase WA, Dahlquist FW. Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones. Proceedings of the National Academy of Sciences of the United States of America. 90: 10826-30. PMID 7902573 DOI: 10.1073/Pnas.90.22.10826 |
0.311 |
|
| 1992 |
Lu J, Dahlquist FW. Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR. Biochemistry. 31: 4749-56. PMID 1591236 DOI: 10.1021/Bi00135A002 |
0.408 |
|
| 1992 |
Lu J, Baase WA, Muchmore DC, Dahlquist FW. Protein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded states. Biochemistry. 31: 7765-72. PMID 1510962 DOI: 10.1021/Bi00149A004 |
0.359 |
|
| 1992 |
Gegner JA, Graham DR, Roth AF, Dahlquist FW. Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway. Cell. 70: 975-82. PMID 1326408 DOI: 10.1016/0092-8674(92)90247-A |
0.337 |
|
| 1991 |
Gegner JA, Dahlquist FW. Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA. Proceedings of the National Academy of Sciences of the United States of America. 88: 750-4. PMID 1992467 DOI: 10.1073/Pnas.88.3.750 |
0.386 |
|
| 1991 |
Dao-pin S, Anderson DE, Baase WA, Dahlquist FW, Matthews BW. Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. Biochemistry. 30: 11521-9. PMID 1747370 DOI: 10.1021/Bi00113A006 |
0.357 |
|
| 1990 |
Oas TG, McIntosh LP, O'Shea EK, Dahlquist FW, Kim PS. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry. 29: 2891-4. PMID 2337572 DOI: 10.1021/Bi00464A001 |
0.708 |
|
| 1990 |
McIntosh LP, Wand AJ, Lowry DF, Redfield AG, Dahlquist FW. Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme. Biochemistry. 29: 6341-62. PMID 2207079 DOI: 10.1021/Bi00479A003 |
0.337 |
|
| 1990 |
Stewart RC, Roth AF, Dahlquist FW. Mutations that affect control of the methylesterase activity of CheB, a component of the chemotaxis adaptation system in Escherichia coli. Journal of Bacteriology. 172: 3388-99. PMID 2188960 DOI: 10.1128/Jb.172.6.3388-3399.1990 |
0.321 |
|
| 1990 |
McIntosh LP, Dahlquist FW. Biosynthetic incorporation of 15N and 13C for assignment and interpretation of nuclear magnetic resonance spectra of proteins. Quarterly Reviews of Biophysics. 23: 1-38. PMID 2188278 DOI: 10.1017/S0033583500005400 |
0.399 |
|
| 1990 |
Zuiderweg ERP, McIntosh LP, Dahlquist FW, Fesik SW. Three-dimensional 13C-resolved proton NOE spectroscopy of uniformly 13C-labeled proteins for the NMR assignment and structure determination of larger molecules Journal of Magnetic Resonance (1969). 86: 210-216. DOI: 10.1016/0022-2364(90)90228-2 |
0.391 |
|
| 1989 |
Weaver LH, Gray TM, Grütter MG, Anderson DE, Wozniak JA, Dahlquist FW, Matthews BW. High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His. Biochemistry. 28: 3793-7. PMID 2665808 DOI: 10.1021/Bi00435A025 |
0.378 |
|
| 1989 |
Russell CB, Stewart RC, Dahlquist FW. Control of transducer methylation levels in Escherichia coli: investigation of components essential for modulation of methylation and demethylation reactions. Journal of Bacteriology. 171: 3609-18. PMID 2661528 DOI: 10.1128/Jb.171.7.3609-3618.1989 |
0.345 |
|
| 1989 |
Oas TG, Hartzell CJ, Drobny GP, Dahlquist FW. Selective NMR detection of 13C15N dipole pairs in solid samples Journal of Magnetic Resonance (1969). 81: 395-399. DOI: 10.1016/0022-2364(89)90072-3 |
0.59 |
|
| 1988 |
Stewart RC, Dahlquist FW. N-terminal half of CheB is involved in methylesterase response to negative chemotactic stimuli in Escherichia coli. Journal of Bacteriology. 170: 5728-38. PMID 3056911 DOI: 10.1128/Jb.170.12.5728-5738.1988 |
0.327 |
|
| 1987 |
McIntosh LP, Dahlquist FW, Redfield AG. Proton NMR and NOE structural and dynamic studies of larger proteins and nucleic acids aided by isotope labels: T4 lysozyme. Journal of Biomolecular Structure & Dynamics. 5: 21-34. PMID 3271466 DOI: 10.1080/07391102.1987.10506372 |
0.338 |
|
| 1987 |
McIntosh LP, Griffey RH, Muchmore DC, Nielson CP, Redfield AG, Dahlquist FW. Proton NMR measurements of bacteriophage T4 lysozyme aided by 15N isotopic labeling: structural and dynamic studies of larger proteins. Proceedings of the National Academy of Sciences of the United States of America. 84: 1244-8. PMID 3029773 DOI: 10.1073/Pnas.84.5.1244 |
0.356 |
|
| 1987 |
Oas TG, Hartzell CJ, Dahlquist FW, Drobny GP. The amide 15N chemical shift tensors of four peptides determined from 13C dipole-coupled chemical shift powder patterns Journal of the American Chemical Society. 109: 5962-5966. DOI: 10.1021/Ja00254A011 |
0.61 |
|
| 1987 |
Oas TG, Hartzell CJ, McMahon TJ, Drobny GP, Dahlquist FW. The carbonyl 13C chemical shift tensors of five peptides determined from 15N dipole-coupled chemical shift powder patterns Journal of the American Chemical Society. 109: 5956-5962. DOI: 10.1021/Ja00254A010 |
0.574 |
|
| 1987 |
GRIFFEY RH, REDFIELD AG, MCINTOSH LP, OAS TG, DAHLQUIST FW. ChemInform Abstract: Assignment of Proton Amide Resonances of T4 Lysozyme by 13C and 15N Multiple Isotopic Labeling. Cheminform. 18. DOI: 10.1002/chin.198711040 |
0.582 |
|
| 1986 |
Griffey RH, Redfield AG, McIntosh LP, Oas TG, Dahlquist FW. Assignment of proton amide resonances of T4 lysozyme by carbon-13 and nitrogen-15 multiple isotopic labeling Journal of the American Chemical Society. 108: 6816-6817. DOI: 10.1021/Ja00281A066 |
0.602 |
|
| 1986 |
Griffey RH, Redfield AG, McIntosh LP, Oas TG, Dahlquist FW. Assignment of proton amide resonances of T4 lysozyme by 13C and 15N multiple isotopic labeling Journal of the American Chemical Society. 108: 6816-6817. |
0.582 |
|
| 1985 |
Paddy MR, Dahlquist FW, Dratz EA, Deese AJ. Simultaneous observation of order and dynamics at several defined positions in a single acyl chain using 2H NMR of single acyl chain perdeuterated phosphatidylcholines. Biochemistry. 24: 5988-95. PMID 4084502 DOI: 10.1021/Bi00342A045 |
0.301 |
|
| 1985 |
Wilson ML, Dahlquist FW. Membrane protein conformational change dependent on the hydrophobic environment. Biochemistry. 24: 1920-8. PMID 3893541 |
0.301 |
|
| 1985 |
Griffey RH, Redfield AG, Loomis RE, Dahlquist FW. Nuclear magnetic resonance observation and dynamics of specific amide protons in T4 lysozyme. Biochemistry. 24: 817-22. PMID 3888265 DOI: 10.1021/Bi00325A001 |
0.368 |
|
| 1983 |
Kehry MR, Wilson ML, Dahlquist FW. A simple quantitative method for the determination of 3-fluorotyrosine substitution in proteins. Analytical Biochemistry. 131: 236-41. PMID 6614455 DOI: 10.1016/0003-2697(83)90160-4 |
0.305 |
|
| 1982 |
Huskins KR, Bernhard SA, Dahlquist FW. Halibut muscle 3-phosphoglycerate kinase. Chemical and physical properties of the enzyme and its substrate complexes Biochemistry. 21: 4180-4188. PMID 6982068 DOI: 10.1021/Bi00260A041 |
0.318 |
|
| 1981 |
Paddy MR, Dahlquist FW, Davis JH, Bloom M. Dynamical and temperature-dependent effects of lipid-protein interactions. Application of deuterium nuclear magnetic resonance and electron paramagnetic resonance spectroscopy to the same reconstitutions of cytochrome c oxidase. Biochemistry. 20: 3152-62. PMID 6264951 DOI: 10.1021/Bi00514A026 |
0.337 |
|
| 1980 |
Swanson PE, Paddy MR, Dahlquist FW, Storm DR. Characterization of octapeptin-membrane interactions using spin-labeled octapeptin Biochemistry. 19: 3307-3314. PMID 6250564 DOI: 10.1021/Bi00555A032 |
0.519 |
|
| 1974 |
Lovely P, Dahlquist FW, Macnab R, Koshland DE. An instrument for recording the motions of microorganisms in chemical gradients Review of Scientific Instruments. 45: 683-686. PMID 4596820 DOI: 10.1063/1.1686713 |
0.573 |
|
| 1972 |
Dahlquist FW, Lovely P, Koshland DE. Quantitative analysis of bacterial migration in chemotaxis Nature: New Biology. 236: 120-123. PMID 4554379 |
0.328 |
|
| 1969 |
Raftery MA, Rand-Meir T, Dahlquist FW, Parsons SM, Borders CL, Wolcott RG, Beranek W, Jao L. Separation of glycosaminoglycan saccharide and glycoside mixtures by gel filtration. Analytical Biochemistry. 30: 427-35. PMID 5821304 |
0.641 |
|
| 1969 |
Dahlquist FW, Borders CL, Jacobson G, Raftery MA. The stereospecificity of human, hen, and papaya lysozymes. Biochemistry. 8: 694-700. PMID 5815782 DOI: 10.1021/Bi00830A035 |
0.635 |
|
| 1969 |
Dahlquist FW, Raftery MA. Some properties of contiguous binding subsites on lysozyme as determined by proton magnetic resonance spectroscopy. Biochemistry. 8: 713-25. PMID 5793721 |
0.465 |
|
| 1969 |
Parsons SM, Jao L, Dahlquist FW, Borders CL, Racs J, Groff T, Raftery MA. The nature of amino acid side chains which are critical for the activity of lysozyme. Biochemistry. 8: 700-12. PMID 5793720 |
0.66 |
|
| 1969 |
Dahlquist FW, Rand-Meir T, Raftery MA. Application of secondary alpha-deuterium kinetic isotope effects to studies of enzyme catalysis. Glycoside hydrolysis by lysozyme and beta-glucosidase. Biochemistry. 8: 4214-21. PMID 5388150 |
0.389 |
|
| 1969 |
Rand-Meir T, Dahlquist FW, Raftery MA. Use of synthetic substrates to study binding and catalysis by lysozyme. Biochemistry. 8: 4206-14. PMID 5346398 |
0.458 |
|
| 1969 |
Raftery MA, Dahlquist FW, Parsons SM, Wolcott RG. The use of nuclear magnetic resonance to describe relative modes of binding to lysozyme of homologous inhibitors and related substrates. Proceedings of the National Academy of Sciences of the United States of America. 62: 44-51. PMID 5253664 |
0.478 |
|
| 1969 |
Raftery MA, Dahlquist FW. The chemistry of lysozyme. Fortschritte Der Chemie Organischer Naturstoffe = Progress in the Chemistry of Organic Natural Products. ProgrèS Dans La Chimie Des Substances Organiques Naturelles. 27: 340-81. PMID 4908211 |
0.383 |
|
| 1968 |
Dahlquist FW, Raftery MA. A nuclear magnetic resonance study of enzyme-inhibitor association. The use of pH and temperature effects to probe the binding environments. Biochemistry. 7: 3277-80. PMID 5684349 |
0.437 |
|
| 1968 |
Dahlquist FW, Raftery MA. A nuclear magnetic resonance study of association equilibria and enzyme-boud environments of N-acetyl-D-glucosamine anomers and lysozyme. Biochemistry. 7: 3269-76. PMID 5684348 |
0.416 |
|
| 1968 |
Raftery MA, Dahlquist FW, Chan SI, Parsons SM. A proton magnetic resonance study of the association of lysozyme with monosaccharide inhibitors. The Journal of Biological Chemistry. 243: 4175-80. PMID 5679957 |
0.408 |
|
| 1968 |
Dahlquist FW, Rand-Meir T, Raftery MA. Demonstration of carbonium ion intermediate during lysozyme catalysis. Proceedings of the National Academy of Sciences of the United States of America. 61: 1194-8. PMID 5249805 |
0.374 |
|
| 1967 |
Dahlquist FW, Raftery M. Specificity of cleavage of chitotriose by lysozyme [41] Nature. 213: 625-626. DOI: 10.1038/213625a0 |
0.409 |
|
| 1966 |
Dahlquist FW, Jao L, Raftery M. On the binding of chitin oligosaccharides to lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 56: 26-30. PMID 5229853 |
0.474 |
|
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