| Year |
Citation |
Score |
| 2023 |
Fenton M, Gregory E, Daughdrill G. Protein disorder and autoinhibition: The role of multivalency and effective concentration. Current Opinion in Structural Biology. 83: 102705. PMID 37778184 DOI: 10.1016/j.sbi.2023.102705 |
0.452 |
|
| 2022 |
Gregory E, Daughdrill GW. Sequence Properties of An Intramolecular Interaction That Inhibits p53 DNA Binding. Biomolecules. 12. PMID 36358908 DOI: 10.3390/biom12111558 |
0.379 |
|
| 2022 |
Fenton M, Borcherds W, Chen L, Anbanandam A, Levy R, Chen J, Daughdrill G. Two short linear motifs in the MDMX acidic domain bind overlapping sites on MDMX and p53. Journal of Molecular Biology. 167844. PMID 36181774 DOI: 10.1016/j.jmb.2022.167844 |
0.78 |
|
| 2022 |
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, ... ... Daughdrill GW, et al. Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nature Structural & Molecular Biology. 29: 781-790. PMID 35948766 DOI: 10.1038/s41594-022-00811-w |
0.753 |
|
| 2020 |
Sang P, Shi Y, Lu J, Chen L, Yang L, Borcherds W, Abdulkadir S, Li Q, Daughdrill G, Chen J, Cai J. Correction to α-Helix-Mimicking Sulfono-γ-AApeptide Inhibitors for p53-MDM2/MDMX Protein-Protein Interactions. Journal of Medicinal Chemistry. PMID 32822169 DOI: 10.1021/Acs.Jmedchem.0C01284 |
0.731 |
|
| 2020 |
Sang P, Shi Y, Higbee P, Wang M, Abdulkadir S, Lu J, Daughdrill GW, Chen J, Cai J. Rational Design and Synthesis of Right-Handed D-Sulfono-γ-AApeptide Helical Foldamers as Potent Inhibitors of Protein-Protein Interactions. The Journal of Organic Chemistry. PMID 32700908 DOI: 10.1021/Acs.Joc.0C00996 |
0.401 |
|
| 2020 |
Daughdrill GW. Disorder for Dummies: Functional Mutagenesis of Transient Helical Segments in Disordered Proteins. Methods in Molecular Biology (Clifton, N.J.). 2141: 3-20. PMID 32696350 DOI: 10.1007/978-1-0716-0524-0_1 |
0.55 |
|
| 2020 |
Li Q, Karim RM, Cheng M, Das M, Chen L, Zhang C, Lawrence HR, Daughdrill GW, Schonbrunn E, Ji H, Chen J. Inhibition of p53 DNA binding by a small molecule protects mice from radiation toxicity. Oncogene. PMID 32555331 DOI: 10.1038/S41388-020-1344-Y |
0.45 |
|
| 2020 |
Sang P, Shi Y, Lu J, Chen L, Yang L, Borcherds W, Abdulkadir S, Li Q, Daughdrill GW, Chen J, Cai J. α-Helix-Mimicking Sulfono-γ-AApeptide Inhibitors for p53-MDM2/MDMX Protein-Protein Interactions. Journal of Medicinal Chemistry. PMID 31971801 DOI: 10.1021/Acs.Jmedchem.9B00993 |
0.754 |
|
| 2020 |
Higbee PS, Daughdrill GW, Sang P, Cai J. Role of Transient Helicity and Heat Capacity in Coupled Folding and Binding of P53TAD to MDM2 and MDMX Biophysical Journal. 118: 52a. DOI: 10.1016/J.Bpj.2019.11.467 |
0.378 |
|
| 2020 |
Fenton MJ, Borcherds WM, Daughdrill GW, Chen L, Chen J. MDMX Acidic Domain Requires the WF Motif for the Initiation of the Secondary Interaction with the P53DBD Biophysical Journal. 118: 38a-39a. DOI: 10.1016/J.Bpj.2019.11.391 |
0.707 |
|
| 2020 |
Levy R, Borcherds WM, He F, Daughdrill GW, Chen J. Protein Disorder Regulates the DNA Binding Specificity of p53 Biophysical Journal. 118: 215a. DOI: 10.1016/J.Bpj.2019.11.1279 |
0.777 |
|
| 2020 |
Gregory-Lott E, Borcherds WM, He F, Zhou M, Daughdrill GW. Conformational Flexibility of p53 Transactivation Domain Controls DNA Binding Specificity and Promoter Selectivity Biophysical Journal. 118: 213a. DOI: 10.1016/J.Bpj.2019.11.1271 |
0.754 |
|
| 2019 |
He F, Borcherds W, Song T, Wei X, Das M, Chen L, Daughdrill GW, Chen J. Interaction between p53 N terminus and core domain regulates specific and nonspecific DNA binding. Proceedings of the National Academy of Sciences of the United States of America. PMID 30988205 DOI: 10.1073/Pnas.1903077116 |
0.767 |
|
| 2019 |
Sowemimo OT, Knox-Brown P, Borcherds W, Rindfleisch T, Thalhammer A, Daughdrill GW. Conserved Glycines Control Disorder and Function in the Cold-Regulated Protein, COR15A. Biomolecules. 9. PMID 30832369 DOI: 10.3390/biom9030084 |
0.718 |
|
| 2019 |
Levy R, Gregory E, Borcherds W, Daughdrill G. p53 Phosphomimetics Preserve Transient Secondary Structure but Reduce Binding to Mdm2 and MdmX. Biomolecules. 9. PMID 30832340 DOI: 10.3390/biom9030083 |
0.787 |
|
| 2019 |
Sowemimo O, Borcherds W, Knox-Brown P, Rindfleisch T, Thalhammer A, Daughdrill G. Evolution of Transient Helicity and Disorder in Late Embryogenesis Abundant Protein COR15A Biophysical Journal. 116: 473a. DOI: 10.1016/J.Bpj.2018.11.2553 |
0.737 |
|
| 2018 |
Borcherds WM, Daughdrill GW. Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins. Methods in Enzymology. 611: 101-136. PMID 30471686 DOI: 10.1016/Bs.Mie.2018.09.011 |
0.786 |
|
| 2018 |
Poosapati A, Gregory E, Borcherds WM, Chemes LB, Daughdrill GW. Uncoupling the folding and binding of an intrinsically disordered protein. Journal of Molecular Biology. PMID 29890118 DOI: 10.1016/J.Jmb.2018.05.045 |
0.759 |
|
| 2017 |
Borcherds W, Becker A, Chen L, Chen J, Chemes LB, Daughdrill GW. Optimal Affinity Enhancement by a Conserved Flexible Linker Controls p53 Mimicry in MdmX. Biophysical Journal. PMID 28487147 DOI: 10.1016/J.Bpj.2017.04.017 |
0.775 |
|
| 2017 |
Crabtree MD, Borcherds W, Poosapati A, Shammas SL, Daughdrill GW, Clarke J. Conserved helix-flanking prolines modulate IDP:target affinity by altering the lifetime of the bound complex. Biochemistry. PMID 28425697 DOI: 10.1021/Acs.Biochem.7B00179 |
0.775 |
|
| 2016 |
Wei X, Wu S, Song T, Chen L, Gao M, Borcherds W, Daughdrill GW, Chen J. Secondary interaction between MDMX and p53 core domain inhibits p53 DNA binding. Proceedings of the National Academy of Sciences of the United States of America. PMID 27114532 DOI: 10.1073/Pnas.1603838113 |
0.771 |
|
| 2015 |
Ytreberg FM, Borcherds W, Wu H, Daughdrill GW. Using chemical shifts to generate structural ensembles for intrinsically disordered proteins with converged distributions of secondary structure. Intrinsically Disordered Proteins. 3: e984565. PMID 28232883 DOI: 10.1016/J.Bpj.2014.11.1256 |
0.771 |
|
| 2015 |
Chen L, Borcherds W, Wu S, Becker A, Schonbrunn E, Daughdrill GW, Chen J. Autoinhibition of MDMX by intramolecular p53 mimicry. Proceedings of the National Academy of Sciences of the United States of America. 112: 4624-9. PMID 25825738 DOI: 10.1073/Pnas.1420833112 |
0.762 |
|
| 2014 |
Borcherds W, Theillet FX, Katzer A, Finzel A, Mishall KM, Powell AT, Wu H, Manieri W, Dieterich C, Selenko P, Loewer A, Daughdrill GW. Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells. Nature Chemical Biology. 10: 1000-2. PMID 25362358 DOI: 10.1038/nchembio.1668 |
0.778 |
|
| 2014 |
van der Lee R, Buljan M, Lang B, Weatheritt RJ, Daughdrill GW, Dunker AK, Fuxreiter M, Gough J, Gsponer J, Jones DT, Kim PM, Kriwacki RW, Oldfield CJ, Pappu RV, Tompa P, et al. Classification of intrinsically disordered regions and proteins. Chemical Reviews. 114: 6589-631. PMID 24773235 DOI: 10.1021/Cr400525M |
0.369 |
|
| 2014 |
Lee C, Kalmar L, Xue B, Tompa P, Daughdrill GW, Uversky VN, Han KH. Contribution of proline to the pre-structuring tendency of transient helical secondary structure elements in intrinsically disordered proteins. Biochimica Et Biophysica Acta. 1840: 993-1003. PMID 24211251 DOI: 10.1016/J.Bbagen.2013.10.042 |
0.501 |
|
| 2013 |
Theillet FX, Kalmar L, Tompa P, Han KH, Selenko P, Dunker AK, Daughdrill GW, Uversky VN. The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins. Intrinsically Disordered Proteins. 1: e24360. PMID 28516008 DOI: 10.4161/idp.24360 |
0.389 |
|
| 2013 |
Kennedy JA, Daughdrill GW, Schmidt KH. A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1. Nucleic Acids Research. 41: 10215-27. PMID 24038467 DOI: 10.1093/Nar/Gkt817 |
0.499 |
|
| 2013 |
Zhan YA, Wu H, Powell AT, Daughdrill GW, Ytreberg FM. Impact of the K24N mutation on the transactivation domain of p53 and its binding to murine double-minute clone 2. Proteins. 81: 1738-47. PMID 23609977 DOI: 10.1002/Prot.24310 |
0.526 |
|
| 2013 |
Borcherds W, Kashtanov S, Wu H, Daughdrill GW. Structural divergence is more extensive than sequence divergence for a family of intrinsically disordered proteins. Proteins. 81: 1686-98. PMID 23606624 DOI: 10.1002/Prot.24303 |
0.799 |
|
| 2013 |
Borcherds WM, Kashtanov S, Daughdrill GW. Structural Divergence Exceeds Sequence Divergence for a Family of Intrinsically Disordered Proteins Biophysical Journal. 104: 54a. DOI: 10.1016/J.Bpj.2012.11.339 |
0.8 |
|
| 2013 |
Barrett A, Wu H, Kashtanov S, Daughdrill G. Structural Basis for Ternary Complex Formation between Tau, Hsp90, and FKBP51 Biophysical Journal. 104: 387a-388a. DOI: 10.1016/J.Bpj.2012.11.2162 |
0.412 |
|
| 2013 |
Ytreberg FM, Kashtanov S, Borcherds W, Wu H, Daughdrill GW. De Novo Generation of Bound Structures for an Intrinsically Disordered Protein using Only Alpha Carbon Chemical Shifts Biophysical Journal. 104: 191a. DOI: 10.1016/J.Bpj.2012.11.1075 |
0.763 |
|
| 2012 |
Kashtanov S, Borcherds W, Wu H, Daughdrill GW, Ytreberg FM. Using chemical shifts to assess transient secondary structure and generate ensemble structures of intrinsically disordered proteins. Methods in Molecular Biology (Clifton, N.J.). 895: 139-52. PMID 22760318 DOI: 10.1007/978-1-61779-927-3_11 |
0.722 |
|
| 2012 |
Doi K, Li R, Sung SS, Wu H, Liu Y, Manieri W, Krishnegowda G, Awwad A, Dewey A, Liu X, Amin S, Cheng C, Qin Y, Schonbrunn E, Daughdrill G, et al. Discovery of marinopyrrole A (maritoclax) as a selective Mcl-1 antagonist that overcomes ABT-737 resistance by binding to and targeting Mcl-1 for proteasomal degradation. The Journal of Biological Chemistry. 287: 10224-35. PMID 22311987 DOI: 10.1074/Jbc.M111.334532 |
0.316 |
|
| 2012 |
Daughdrill GW, Kashtanov S, Stancik A, Hill SE, Helms G, Muschol M, Receveur-Bréchot V, Ytreberg FM. Understanding the structural ensembles of a highly extended disordered protein. Molecular Biosystems. 8: 308-19. PMID 21979461 DOI: 10.1039/C1Mb05243H |
0.557 |
|
| 2012 |
Borcherds WM, Daughdrill GW, Mishall K, Wu H. Crossing the Entropic Barrier to Coupled Folding and Binding Biophysical Journal. 102: 62a-63a. DOI: 10.1016/J.Bpj.2011.11.372 |
0.778 |
|
| 2012 |
Narayanaswami P, Daughdrill GW. Secondary Structure and Dynamics of a Family of Disordered Proteins Protein and Peptide Folding, Misfolding, and Non-Folding. 221-238. DOI: 10.1002/9781118183373.ch8 |
0.323 |
|
| 2011 |
Daughdrill GW, Borcherds WM, Wu H. Disorder predictors also predict backbone dynamics for a family of disordered proteins. Plos One. 6: e29207. PMID 22195023 DOI: 10.1371/Journal.Pone.0029207 |
0.726 |
|
| 2011 |
Brown CJ, Johnson AK, Dunker AK, Daughdrill GW. Evolution and disorder. Current Opinion in Structural Biology. 21: 441-6. PMID 21482101 DOI: 10.1016/J.Sbi.2011.02.005 |
0.471 |
|
| 2011 |
Daughdrill GW. Protein dynamics: bridging the gap. Nature Chemical Biology. 7: 193-4. PMID 21423160 DOI: 10.1038/Nchembio.544 |
0.544 |
|
| 2011 |
Pine AT, Mishall KM, Borcherds WM, Wu H, Daughdrill GW. Structural Basis for the Dynamic Behavior of a Family of Disordered Proteins Biophysical Journal. 100: 59a-60a. DOI: 10.1016/J.Bpj.2010.12.522 |
0.801 |
|
| 2011 |
Kennedy JA, Daughdrill G, Schmidt K. Structural and Functional Characterization of a RecQ-Like Helicase in S. cerevisiae with a 647 Residue Disordered Region Biophysical Journal. 100: 59a. DOI: 10.1016/J.Bpj.2010.12.520 |
0.515 |
|
| 2011 |
Borcherds WM, Wu H, Pine AT, Mishall KM, Daughdrill GW. Evolution of Structure and Dynamics for a Family of Disordered Proteins Biophysical Journal. 100: 519a. DOI: 10.1016/J.Bpj.2010.12.3036 |
0.776 |
|
| 2011 |
Brown CJ, Daughdrill GW, Dunker AK. Intrinsically Disordered Proteins Evolve Differently from Ordered (Structured) Proteins Biophysical Journal. 100: 519a. DOI: 10.1016/J.Bpj.2010.12.3034 |
0.497 |
|
| 2010 |
Gely S, Lowry DF, Bernard C, Jensen MR, Blackledge M, Costanzo S, Bourhis JM, Darbon H, Daughdrill G, Longhi S. Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein. Journal of Molecular Recognition : Jmr. 23: 435-47. PMID 20058326 DOI: 10.1002/Jmr.1010 |
0.511 |
|
| 2010 |
Brown CJ, Johnson AK, Daughdrill GW. Comparing models of evolution for ordered and disordered proteins. Molecular Biology and Evolution. 27: 609-21. PMID 19923193 DOI: 10.1093/Molbev/Msp277 |
0.481 |
|
| 2010 |
Daughdrill GW. Determining Structural Ensembles for Intrinsically Disordered Proteins Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation. 107-129. DOI: 10.1002/9780470602614.ch5 |
0.356 |
|
| 2009 |
Daughdrill G, Lowry D, Hausrath A. A Robust Approach for Analyzing a Heterogeneous Structural Ensemble Biophysical Journal. 96: 3-8. DOI: 10.1016/J.Bpj.2008.12.1593 |
0.434 |
|
| 2008 |
Lowry DF, Hausrath AC, Daughdrill GW. A robust approach for analyzing a heterogeneous structural ensemble. Proteins. 73: 918-28. PMID 18536020 DOI: 10.1002/Prot.22117 |
0.441 |
|
| 2008 |
Lowry DF, Stancik A, Shrestha RM, Daughdrill GW. Modeling the accessible conformations of the intrinsically unstructured transactivation domain of p53. Proteins. 71: 587-98. PMID 17972286 DOI: 10.1002/Prot.21721 |
0.541 |
|
| 2008 |
Daughdrill GW, Pielak GJ, Uversky VN, Cortese MS, Dunker AK. Natively Disordered Proteins Protein Folding Handbook. 1: 275-357. DOI: 10.1002/9783527619498.Ch41 |
0.361 |
|
| 2007 |
Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. Journal of Molecular Evolution. 65: 277-88. PMID 17721672 DOI: 10.1007/S00239-007-9011-2 |
0.399 |
|
| 2007 |
Vise P, Baral B, Stancik A, Lowry DF, Daughdrill GW. Identifying long-range structure in the intrinsically unstructured transactivation domain of p53. Proteins. 67: 526-30. PMID 17335006 DOI: 10.1002/Prot.21364 |
0.567 |
|
| 2005 |
Olson KE, Narayanaswami P, Vise PD, Lowry DF, Wold MS, Daughdrill GW. Secondary structure and dynamics of an intrinsically unstructured linker domain. Journal of Biomolecular Structure & Dynamics. 23: 113-24. PMID 16060685 DOI: 10.1080/07391102.2005.10507052 |
0.453 |
|
| 2005 |
Vise PD, Baral B, Latos AJ, Daughdrill GW. NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain. Nucleic Acids Research. 33: 2061-77. PMID 15824059 DOI: 10.1093/Nar/Gki336 |
0.514 |
|
| 2003 |
Daughdrill GW, Buchko GW, Botuyan MV, Arrowsmith C, Wold MS, Kennedy MA, Lowry DF. Chemical shift changes provide evidence for overlapping single-stranded DNA- and XPA-binding sites on the 70 kDa subunit of human replication protein A. Nucleic Acids Research. 31: 4176-83. PMID 12853635 DOI: 10.1093/Nar/Gkg451 |
0.513 |
|
| 2002 |
Iwahara J, Iwahara M, Daughdrill GW, Ford J, Clubb RT. The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA. The Embo Journal. 21: 1197-209. PMID 11867548 DOI: 10.1093/Emboj/21.5.1197 |
0.362 |
|
| 2001 |
Daughdrill GW, Ackerman J, Isern NG, Botuyan MV, Arrowsmith C, Wold MS, Lowry DF. The weak interdomain coupling observed in the 70 kDa subunit of human replication protein A is unaffected by ssDNA binding. Nucleic Acids Research. 29: 3270-6. PMID 11470885 DOI: 10.1093/Nar/29.15.3270 |
0.513 |
|
| 1999 |
Buchko GW, Daughdrill GW, de Lorimier R, Rao B K, Isern NG, Lingbeck JM, Taylor JS, Wold MS, Gochin M, Spicer LD, Lowry DF, Kennedy MA. Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies. Biochemistry. 38: 15116-28. PMID 10563794 DOI: 10.1021/Bi991755P |
0.45 |
|
| 1999 |
Jacobs DM, Lipton AS, Isern NG, Daughdrill GW, Lowry DF, Gomes X, Wold MS. Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker. Journal of Biomolecular Nmr. 14: 321-31. PMID 10526407 DOI: 10.1023/A:1008373009786 |
0.395 |
|
| 1998 |
Rupert PB, Daughdrill GW, Bowerman B, Matthews BW. A new DNA-binding motif in the Skn-1 binding domain-DNA complex. Nature Structural Biology. 5: 484-91. PMID 9628487 DOI: 10.1038/Nsb0698-484 |
0.327 |
|
| 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 |
0.378 |
|
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