| Year |
Citation |
Score |
| 2019 |
Sternke M, Tripp KW, Barrick D. Consensus sequence design as a general strategy to create hyperstable, biologically active proteins. Proceedings of the National Academy of Sciences of the United States of America. 116: 11275-11284. PMID 31110018 DOI: 10.1073/pnas.1816707116 |
0.795 |
|
| 2019 |
Petersen M, Fang R, Majumdar A, Barrick D. Interfaces of the Topoisomerase V (HhH)2Domains have Surprising Contributions to Thermodynamic Stability Biophysical Journal. 116: 338a. DOI: 10.1016/j.bpj.2018.11.1842 |
0.3 |
|
| 2018 |
Jenkins KA, Fossat MJ, Zhang S, Rai DK, Klein S, Gillilan R, White Z, Gerlich G, McCallum SA, Winter R, Gruner SM, Barrick D, Royer CA. The consequences of cavity creation on the folding landscape of a repeat protein depend upon context. Proceedings of the National Academy of Sciences of the United States of America. PMID 30104366 DOI: 10.1073/Pnas.1807379115 |
0.422 |
|
| 2018 |
Geiger-Schuller K, Sforza K, Yuhas M, Parmeggiani F, Baker D, Barrick D. Extreme stability in de novo-designed repeat arrays is determined by unusually stable short-range interactions. Proceedings of the National Academy of Sciences of the United States of America. PMID 29959204 DOI: 10.1073/Pnas.1800283115 |
0.458 |
|
| 2018 |
Zhang Y, Berghaus M, Klein S, Jenkins K, Zhang S, McCallum SA, Morgan J, Winter R, Barrick D, Royer CA. High Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine Rich Repeat Protein. Journal of Molecular Biology. PMID 29545082 DOI: 10.1016/J.Jmb.2018.03.005 |
0.407 |
|
| 2017 |
Sherry KP, Das RK, Pappu RV, Barrick D. Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor. Proceedings of the National Academy of Sciences of the United States of America. PMID 29078291 DOI: 10.1073/Pnas.1706083114 |
0.324 |
|
| 2017 |
Tripp KW, Sternke M, Majumdar A, Barrick D. Creating a homeodomain with high stability and DNA binding affinity by sequence averaging. Journal of the American Chemical Society. PMID 28326770 DOI: 10.1021/jacs.6b11323 |
0.796 |
|
| 2016 |
Geiger-Schuller K, Barrick D. Broken TALEs: Transcription Activator-like Effectors Populate Partly Folded States. Biophysical Journal. 111: 2395-2403. PMID 27926841 DOI: 10.1016/j.bpj.2016.10.013 |
0.392 |
|
| 2016 |
Fossat MJ, Dao TP, Jenkins K, Dellarole M, Yang Y, McCallum SA, Garcia AE, Barrick D, Roumestand C, Royer CA. High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape. Biophysical Journal. 111: 2368-2376. PMID 27926838 DOI: 10.1016/J.Bpj.2016.08.027 |
0.421 |
|
| 2016 |
Cunha ES, Hatem CL, Barrick D. Synergistic enhancement of cellulase pairs linked by consensus ankyrin repeats: determination of the roles of spacing, orientation and enzyme identity. Proteins. PMID 27071357 DOI: 10.1002/prot.25047 |
0.528 |
|
| 2016 |
Fossat MJ, Garcia A, Barrick D, Roumestand C, Royer CA. Exploring Folding Cooperativity of a Repeat Protein Folding by 2D-NMR Detected Pressure Perturbation Biophysical Journal. 110: 391a. DOI: 10.1016/J.Bpj.2015.11.2115 |
0.372 |
|
| 2015 |
Marold JD, Kavran JM, Bowman GD, Barrick D. A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins. Structure (London, England : 1993). 23: 2055-65. PMID 26439765 DOI: 10.1016/j.str.2015.07.022 |
0.427 |
|
| 2015 |
Sherry KP, Johnson SE, Hatem CL, Majumdar A, Barrick D. Effects of Linker Length and Transient Secondary Structure Elements in the Intrinsically Disordered Notch RAM Region on Notch Signaling. Journal of Molecular Biology. 427: 3587-3597. PMID 26344835 DOI: 10.1016/j.jmb.2015.09.001 |
0.367 |
|
| 2015 |
Dao TP, Majumdar A, Barrick D. Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability. Proceedings of the National Academy of Sciences of the United States of America. 112: E2298-306. PMID 25902505 DOI: 10.1073/pnas.1412165112 |
0.468 |
|
| 2015 |
Sherry K, Das R, Pappu R, Barrick D. Effects of Charge Interactions and Transient Secondary Structure Elements on the Function of the Disordered RAM Region of the Notch Receptor Biophysical Journal. 108: 193a-194a. DOI: 10.1016/J.Bpj.2014.11.1071 |
0.314 |
|
| 2014 |
Dao TP, Majumdar A, Barrick D. Capping motifs stabilize the leucine-rich repeat protein PP32 and rigidify adjacent repeats. Protein Science : a Publication of the Protein Society. 23: 801-11. PMID 24659532 DOI: 10.1002/pro.2462 |
0.421 |
|
| 2014 |
Aksel T, Barrick D. Direct observation of parallel folding pathways revealed using a symmetric repeat protein system Biophysical Journal. 107: 220-232. DOI: 10.1016/j.bpj.2014.04.058 |
0.424 |
|
| 2013 |
Cunha ES, Hatem CL, Barrick D. Insertion of endocellulase catalytic domains into thermostable consensus ankyrin scaffolds: effects on stability and cellulolytic activity. Applied and Environmental Microbiology. 79: 6684-96. PMID 23974146 DOI: 10.1128/AEM.02121-13 |
0.572 |
|
| 2013 |
Cunha E, Hatem CL, Barrick D. Natural and designed enzymes for cellulose degradation Advanced Biofuels and Bioproducts. 2147483647: 339-368. DOI: 10.1007/978-1-4614-3348-4_19 |
0.502 |
|
| 2012 |
Johnson SE, Barrick D. Dissecting and circumventing the requirement for RAM in CSL-dependent Notch signaling. Plos One. 7: e39093. PMID 22876274 DOI: 10.1371/Journal.Pone.0039093 |
0.46 |
|
| 2011 |
Allgood AG, Barrick D. Mapping the Deltex-binding surface on the notch ankyrin domain using analytical ultracentrifugation. Journal of Molecular Biology. 414: 243-59. PMID 22001695 DOI: 10.1016/J.Jmb.2011.09.050 |
0.714 |
|
| 2011 |
Vieux EF, Barrick D. Deletion of internal structured repeats increases the stability of a leucine-rich repeat protein, YopM Biophysical Chemistry. 159: 152-161. PMID 21764506 DOI: 10.1016/j.bpc.2011.06.004 |
0.499 |
|
| 2011 |
Rouget JB, Aksel T, Roche J, Saldana JL, Garcia AE, Barrick D, Royer CA. Size and sequence and the volume change of protein folding. Journal of the American Chemical Society. 133: 6020-7. PMID 21446709 DOI: 10.1021/Ja200228W |
0.434 |
|
| 2011 |
Aksel T, Majumdar A, Barrick D. The contribution of entropy, enthalpy, and hydrophobic desolvation to cooperativity in repeat-protein folding Structure. 19: 349-360. PMID 21397186 DOI: 10.1016/j.str.2010.12.018 |
0.461 |
|
| 2011 |
Sosnick TR, Barrick D. The folding of single domain proteins--have we reached a consensus? Current Opinion in Structural Biology. 21: 12-24. PMID 21144739 DOI: 10.1016/J.Bpj.2010.12.2223 |
0.347 |
|
| 2011 |
Das RK, Barrick D, Pappu RV. Conformational Fluctuations within the Intrinsically Disordered RAM Domain of the Notch Receptor are Governed by the Patterning of Charged Residues within the Primary Sequence Biophysical Journal. 100: 13a. DOI: 10.1016/J.Bpj.2010.12.282 |
0.417 |
|
| 2010 |
Johnson SE, Ilagan MX, Kopan R, Barrick D. Thermodynamic analysis of the CSL x Notch interaction: distribution of binding energy of the Notch RAM region to the CSL beta-trefoil domain and the mode of competition with the viral transactivator EBNA2. The Journal of Biological Chemistry. 285: 6681-92. PMID 20028974 DOI: 10.1074/jbc.M109.019968 |
0.345 |
|
| 2009 |
Kloss E, Barrick D. C-terminal deletion of leucine-rich repeats from YopM reveals a heterogeneous distribution of stability in a cooperatively folded protein Protein Science. 18: 1948-1960. PMID 19593816 DOI: 10.1002/Pro.205 |
0.82 |
|
| 2009 |
Aksel T, Barrick D. Chapter 4 Analysis of Repeat-Protein Folding Using Nearest-Neighbor Statistical Mechanical Models Methods in Enzymology. 455: 95-125. PMID 19289204 DOI: 10.1016/S0076-6879(08)04204-3 |
0.375 |
|
| 2009 |
Barrick D. What have we learned from the studies of two-state folders, and what are the unanswered questions about two-state protein folding? Physical Biology. 6. PMID 19208936 DOI: 10.1088/1478-3975/6/1/015001 |
0.367 |
|
| 2009 |
Street TO, Barrick D. Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape Protein Science. 18: 58-68. PMID 19177351 DOI: 10.1002/pro.9 |
0.458 |
|
| 2008 |
Kloss E, Barrick D. Thermodynamics, Kinetics, and Salt dependence of Folding of YopM, a Large Leucine-rich Repeat Protein Journal of Molecular Biology. 383: 1195-1209. PMID 18793647 DOI: 10.1016/J.Jmb.2008.08.069 |
0.819 |
|
| 2008 |
Courtemanche N, Barrick D. The Leucine-Rich Repeat Domain of Internalin B Folds along a Polarized N-Terminal Pathway Structure. 16: 705-714. PMID 18462675 DOI: 10.1016/j.str.2008.02.015 |
0.425 |
|
| 2008 |
Tripp KW, Barrick D. Rerouting the folding pathway of the Notch ankyrin domain by reshaping the energy landscape Journal of the American Chemical Society. 130: 5681-5688. PMID 18396879 DOI: 10.1021/ja0763201 |
0.807 |
|
| 2008 |
Bertagna A, Toptygin D, Brand L, Barrick D. The effects of conformational heterogeneity on the binding of the Notch intracellular domain to effector proteins: a case of biologically tuned disorder. Biochemical Society Transactions. 36: 157-66. PMID 18363556 DOI: 10.1042/Bst0360157 |
0.416 |
|
| 2008 |
Barrick D, Ferreiro DU, Komives EA. Folding landscapes of ankyrin repeat proteins: experiments meet theory. Current Opinion in Structural Biology. 18: 27-34. PMID 18243686 DOI: 10.1016/J.Sbi.2007.12.004 |
0.667 |
|
| 2008 |
Courtemanche N, Barrick D. Folding thermodynamics and kinetics of the leucine-rich repeat domain of the virulence factor Internalin B Protein Science. 17: 43-53. PMID 18156467 DOI: 10.1110/ps.073166608 |
0.447 |
|
| 2008 |
Street TO, Courtemanche N, Barrick D. Protein Folding and Stability Using Denaturants Methods in Cell Biology. 84: 295-325. PMID 17964936 DOI: 10.1016/S0091-679X(07)84011-8 |
0.436 |
|
| 2008 |
Kloss E, Courtemanche N, Barrick D. Repeat-protein folding: New insights into origins of cooperativity, stability, and topology Archives of Biochemistry and Biophysics. 469: 83-99. PMID 17963718 DOI: 10.1016/J.Abb.2007.08.034 |
0.811 |
|
| 2007 |
Street TO, Bradley CM, Barrick D. Predicting coupling limits from an experimentally determined energy landscape. Proceedings of the National Academy of Sciences of the United States of America. 104: 4907-12. PMID 17360387 DOI: 10.1073/pnas.0608756104 |
0.708 |
|
| 2007 |
Lubman OY, Ilagan MX, Kopan R, Barrick D. Quantitative dissection of the Notch:CSL interaction: insights into the Notch-mediated transcriptional switch. Journal of Molecular Biology. 365: 577-89. PMID 17070841 DOI: 10.1016/J.Jmb.2006.09.071 |
0.4 |
|
| 2007 |
Tripp KW, Barrick D. Enhancing the Stability and Folding Rate of a Repeat Protein through the Addition of Consensus Repeats Journal of Molecular Biology. 365: 1187-1200. PMID 17067634 DOI: 10.1016/j.jmb.2006.09.092 |
0.831 |
|
| 2006 |
Bradley CM, Barrick D. The notch ankyrin domain folds via a discrete, centralized pathway. Structure (London, England : 1993). 14: 1303-12. PMID 16905104 DOI: 10.1016/J.Str.2006.06.013 |
0.733 |
|
| 2006 |
Street TO, Rose GD, Barrick D. The Role of Introns in Repeat Protein Gene Formation Journal of Molecular Biology. 360: 258-266. PMID 16781737 DOI: 10.1016/J.Jmb.2006.05.024 |
0.324 |
|
| 2005 |
Zweifel ME, Leahy DJ, Barrick D. Structure and Notch receptor binding of the tandem WWE domain of Deltex. Structure (London, England : 1993). 13: 1599-611. PMID 16271883 DOI: 10.1016/J.Str.2005.07.015 |
0.809 |
|
| 2005 |
Street TO, Bradley CM, Barrick D. An improved experimental system for determining small folding entropy changes resulting from proline to alanine substitutions. Protein Science : a Publication of the Protein Society. 14: 2429-35. PMID 16131666 DOI: 10.1110/ps.051505705 |
0.687 |
|
| 2005 |
Mello CC, Bradley CM, Tripp KW, Barrick D. Experimental characterization of the folding kinetics of the notch ankyrin domain. Journal of Molecular Biology. 352: 266-81. PMID 16095609 DOI: 10.1016/J.Jmb.2005.07.026 |
0.802 |
|
| 2005 |
Bradley CM, Barrick D. Effect of multiple prolyl isomerization reactions on the stability and folding kinetics of the notch ankyrin domain: experiment and theory. Journal of Molecular Biology. 352: 253-65. PMID 16054647 DOI: 10.1016/J.Jmb.2005.06.041 |
0.679 |
|
| 2004 |
Tripp KW, Barrick D. The tolerance of a modular protein to duplication and deletion of internal repeats Journal of Molecular Biology. 344: 169-178. PMID 15504409 DOI: 10.1016/j.jmb.2004.09.038 |
0.81 |
|
| 2004 |
Mello CC, Barrick D. An experimentally determined protein folding energy landscape. Proceedings of the National Academy of Sciences of the United States of America. 101: 14102-7. PMID 15377792 DOI: 10.1073/pnas.0403386101 |
0.356 |
|
| 2004 |
Bertagna AM, Barrick D. Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region Proceedings of the National Academy of Sciences of the United States of America. 101: 12514-12519. PMID 15314218 DOI: 10.1073/pnas.0404760101 |
0.321 |
|
| 2003 |
Zweifel ME, Leahy DJ, Hughson FM, Barrick D. Structure and stability of the ankyrin domain of the Drosophila Notch receptor. Protein Science : a Publication of the Protein Society. 12: 2622-32. PMID 14573873 DOI: 10.1110/Ps.03279003 |
0.816 |
|
| 2003 |
Mello CC, Barrick D. Measuring the stability of partly folded proteins using TMAO. Protein Science : a Publication of the Protein Society. 12: 1522-9. PMID 12824497 DOI: 10.1110/ps.0372903 |
0.459 |
|
| 2003 |
Tripp KW, Barrick D. Folding by consensus Structure. 11: 486-487. PMID 12737814 DOI: 10.1016/S0969-2126(03)00078-9 |
0.797 |
|
| 2002 |
Zweifel ME, Barrick D. Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curves. Biophysical Chemistry. 101: 221-37. PMID 12488003 DOI: 10.1016/S0301-4622(02)00181-3 |
0.771 |
|
| 2002 |
Bradley CM, Barrick D. Limits of cooperativity in a structurally modular protein: response of the Notch ankyrin domain to analogous alanine substitutions in each repeat. Journal of Molecular Biology. 324: 373-86. PMID 12441114 DOI: 10.1016/S0022-2836(02)00945-2 |
0.77 |
|
| 2002 |
Barrick D, Hughson FM. Irreversible assembly of membrane fusion machines. Nature Structural Biology. 9: 78-80. PMID 11813007 DOI: 10.1038/Nsb0202-78 |
0.576 |
|
| 2001 |
Zweifel ME, Barrick D. Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding. Biochemistry. 40: 14357-67. PMID 11724547 DOI: 10.1021/Bi011436+ |
0.833 |
|
| 2001 |
Zweifel ME, Barrick D. Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 1. Solution conformational and hydrodynamic properties. Biochemistry. 40: 14344-56. PMID 11724546 DOI: 10.1021/Bi011435H |
0.81 |
|
| 1995 |
Scholtz JM, Barrick D, York EJ, Stewart JM, Baldwin RL. Urea unfolding of peptide helices as a model for interpreting protein unfolding. Proceedings of the National Academy of Sciences of the United States of America. 92: 185-9. PMID 7816813 DOI: 10.1073/Pnas.92.1.185 |
0.695 |
|
| 1994 |
Barrick D, Hughson FM, Baldwin RL. Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin. Journal of Molecular Biology. 237: 588-601. PMID 8158639 DOI: 10.1006/Jmbi.1994.1257 |
0.72 |
|
| 1993 |
Barrick D, Baldwin RL. Three-state analysis of sperm whale apomyoglobin folding Biochemistry. 32: 3790-3796. PMID 8466917 DOI: 10.1021/Bi00065A035 |
0.509 |
|
| 1993 |
Barrick D, Baldwin RL. The molten globule intermediate of apomyoglobin and the process of protein folding Protein Science. 2: 869-876. PMID 8318892 DOI: 10.1002/Pro.5560020601 |
0.547 |
|
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