| Year |
Citation |
Score |
| 2023 |
Nixon C, Lim SA, Sternke M, Barrick D, Harms M, Marqusee S. The importance of input sequence set to consensus-derived proteins and their relationship to reconstructed ancestral proteins. Biorxiv : the Preprint Server For Biology. PMID 37425932 DOI: 10.1101/2023.06.29.547063 |
0.301 |
|
| 2023 |
Shaw A, Craig JM, Amiri H, Kim J, Upton HE, Pimentel SC, Huang JR, Marqusee S, Gundlach JH, Collins K, Bustamante CJ. Secondary Structure Detection Through Direct Nanopore RNA Sequencing. Biorxiv : the Preprint Server For Biology. PMID 37066208 DOI: 10.1101/2023.04.05.535757 |
0.408 |
|
| 2023 |
Glasgow A, Hobbs HT, Perry ZR, Wells ML, Marqusee S, Kortemme T. Ligand-specific changes in conformational flexibility mediate long-range allostery in the lac repressor. Nature Communications. 14: 1179. PMID 36859492 DOI: 10.1038/s41467-023-36798-1 |
0.321 |
|
| 2022 |
Harman JL, Reardon PN, Costello SM, Warren GD, Phillips SR, Connor PJ, Marqusee S, Harms MJ. Evolution avoids a pathological stabilizing interaction in the immune protein S100A9. Proceedings of the National Academy of Sciences of the United States of America. 119: e2208029119. PMID 36194634 DOI: 10.1073/pnas.2208029119 |
0.35 |
|
| 2022 |
Hobbs HT, Shah NH, Shoemaker SR, Amacher JF, Marqusee S, Kuriyan J. Saturation mutagenesis of a predicted ancestral Syk-family kinase. Protein Science : a Publication of the Protein Society. 31: e4411. PMID 36173161 DOI: 10.1002/pro.4411 |
0.479 |
|
| 2022 |
Hidalgo F, Nocka LM, Shah NH, Gorday K, Latorraca NR, Bandaru P, Templeton S, Lee D, Karandur D, Pelton JG, Marqusee S, Wemmer D, Kuriyan J. A saturation-mutagenesis analysis of the interplay between stability and activation in Ras. Elife. 11. PMID 35272765 DOI: 10.7554/eLife.76595 |
0.463 |
|
| 2021 |
Hobbs HT, Shah NH, Badroos JM, Gee CL, Marqusee S, Kuriyan J. Differences in the dynamics of the tandem-SH2 modules of the Syk and ZAP-70 tyrosine kinases. Protein Science : a Publication of the Protein Society. PMID 34601763 DOI: 10.1002/pro.4199 |
0.506 |
|
| 2021 |
Carroll EC, Latorraca NR, Lindner JM, Maguire BC, Pelton JG, Marqusee S. Mechanistic basis for ubiquitin modulation of a protein energy landscape. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33723075 DOI: 10.1073/pnas.2025126118 |
0.323 |
|
| 2021 |
Nixon CF, Lim SA, Sailer ZR, Zheludev IN, Gee CL, Kelch BA, Harms MJ, Marqusee S. Exploring the Evolutionary History of Kinetic Stability in the α-Lytic Protease Family. Biochemistry. PMID 33433210 DOI: 10.1021/acs.biochem.0c00720 |
0.36 |
|
| 2020 |
Chen Z, Shaw A, Wilson H, Woringer M, Darzacq X, Marqusee S, Wang Q, Bustamante C. Single-molecule diffusometry reveals no catalysis-induced diffusion enhancement of alkaline phosphatase as proposed by FCS experiments. Proceedings of the National Academy of Sciences of the United States of America. PMID 32817484 DOI: 10.1073/Pnas.2006900117 |
0.471 |
|
| 2020 |
Jensen MK, Samelson AJ, Steward A, Clarke J, Marqusee S. The folding and unfolding behavior of ribonuclease H on the ribosome. The Journal of Biological Chemistry. PMID 32527724 DOI: 10.1074/Jbc.Ra120.013909 |
0.531 |
|
| 2020 |
Carroll EC, Greene ER, Martin A, Marqusee S. Site-specific ubiquitination affects protein energetics and proteasomal degradation. Nature Chemical Biology. PMID 32483380 DOI: 10.1038/S41589-020-0556-3 |
0.644 |
|
| 2020 |
Oltrogge LM, Chaijarasphong T, Chen AW, Bolin ER, Marqusee S, Savage DF. Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation. Nature Structural & Molecular Biology. 27: 281-287. PMID 32123388 DOI: 10.1038/S41594-020-0387-7 |
0.369 |
|
| 2020 |
Dall NR, Marqusee S. Using Circular Permutation to Probe the Role of Chain Connectivity in the Co-Translational Folding Process of Halotag Biophysical Journal. 118: 509a-510a. DOI: 10.1016/J.Bpj.2019.11.2807 |
0.317 |
|
| 2020 |
Carroll E, Greene ER, Martin A, Marqusee S. Ubiquitination Modulates a Protein Energy Landscape Site-Specifically with Consequences for Proteasomal Degradation Biophysical Journal. 118: 337a. DOI: 10.1016/J.Bpj.2019.11.1877 |
0.598 |
|
| 2019 |
Guinn EJ, Marqusee S. Using Single-Molecule Chemo-Mechanical Unfolding to Simultaneously Probe Multiple Structural Parameters in Protein Folding. Methods and Protocols. 2. PMID 31164612 DOI: 10.3390/mps2020032 |
0.435 |
|
| 2019 |
Truong HH, Marqusee S. Single-Molecule Force Spectroscopy and Molecular Dynamics Simulations Reveals Complex Folding Landscape and its Potential Role in Amyloid Fibril Formation in a PDZ Domain Biophysical Journal. 116: 38a. DOI: 10.1016/J.Bpj.2018.11.249 |
0.34 |
|
| 2019 |
Costello SM, Dall NR, Samelson AJ, Gupta S, Ralston CY, Marqusee S. Monitoring Protein Folding On and Off the Ribosome using X-Ray Footprinting Mass Spectrometry Biophysical Journal. 116: 339a. DOI: 10.1016/J.Bpj.2018.11.1846 |
0.331 |
|
| 2019 |
Nixon C, Lim SA, Harms M, Marqusee S. The Effect of Input Set to Consensus Derived Proteins and their Relationship to Ancestral Proteins Biophysical Journal. 116: 335a-336a. DOI: 10.1016/J.Bpj.2018.11.1828 |
0.403 |
|
| 2018 |
Guinn EJ, Tian P, Shin M, Best RB, Marqusee S. A small single-domain protein folds through the same pathway on and off the ribosome. Proceedings of the National Academy of Sciences of the United States of America. PMID 30409803 DOI: 10.1073/Pnas.1810517115 |
0.531 |
|
| 2018 |
Rosemond SN, Hamadani KM, Cate JHD, Marqusee S. Modulating long-range energetics via helix stabilization: a case study using T4 lysozyme. Protein Science : a Publication of the Protein Society. PMID 30284332 DOI: 10.1002/Pro.3521 |
0.463 |
|
| 2018 |
Lim SA, Bolin ER, Marqusee S. Tracing a protein's folding pathway over evolutionary time using ancestral sequence reconstruction and hydrogen exchange. Elife. 7. PMID 30204082 DOI: 10.7554/Elife.38369 |
0.503 |
|
| 2018 |
Samelson AJ, Bolin E, Costello SM, Sharma AK, O'Brien EP, Marqusee S. Kinetic and structural comparison of a protein's cotranslational folding and refolding pathways. Science Advances. 4: eaas9098. PMID 29854950 DOI: 10.1126/Sciadv.Aas9098 |
0.509 |
|
| 2018 |
Bolin E, Lim S, Marqusee S. Monitoring the Folding Pathway of a Protein Over Evolutionary Time using Hydrogen Exchange - Mass Spectrometry (HX-MS) Biophysical Journal. 114: 54a. DOI: 10.1016/J.Bpj.2017.11.350 |
0.337 |
|
| 2018 |
Carroll E, Marqusee S. Examining the Effect of Ubiquitination on the Energetics of Substrate Proteins Biophysical Journal. 114: 580a. DOI: 10.1016/J.Bpj.2017.11.3175 |
0.403 |
|
| 2018 |
Nixon C, Lim SA, Sailer Z, Harms M, Marqusee S. Using Ancestral Proteins to Probe the Thermodynamic and Kinetic Properties of the Alpha-Lytic Protease Family Biophysical Journal. 114: 580a. DOI: 10.1016/J.Bpj.2017.11.3173 |
0.334 |
|
| 2018 |
Hobbs HT, Shah N, Marqusee S, Kuriyan J. Dissecting the Divergent Functions and Dynamics of ZAP-70 and SYK Biophysical Journal. 114: 572a. DOI: 10.1016/J.Bpj.2017.11.3129 |
0.47 |
|
| 2018 |
Guinn E, Marqusee S. Probing the Effect of the Ribosome on the Protein Folding Pathway using Single-Molecule Chemo-Mechanical Folding Biophysical Journal. 114: 415a. DOI: 10.1016/J.Bpj.2017.11.2300 |
0.467 |
|
| 2018 |
Truong HH, Marqusee S. Probing Protein Folding Landscape by Using Combined Force Spectroscopy and Molecular Dynamics Simulations Biophysical Journal. 114: 412a. DOI: 10.1016/J.Bpj.2017.11.2284 |
0.39 |
|
| 2017 |
Lim SA, Marqusee S. The burst-phase folding intermediate of ribonuclease H changes conformation over evolutionary history. Biopolymers. PMID 29152711 DOI: 10.1002/Bip.23086 |
0.511 |
|
| 2017 |
Guinn E, Marqusee S. Exploring the denatured state ensemble by single-molecule chemo-mechanical unfolding: The effect of force, temperature and urea. Journal of Molecular Biology. PMID 28782558 DOI: 10.1016/J.Jmb.2017.07.022 |
0.47 |
|
| 2017 |
Hamadani KM, Howe J, Jensen MK, Wu P, Cate JHD, Marqusee S. An in-vitro tag-and-modify protein sample generation method for singlemolecule FRET. The Journal of Biological Chemistry. PMID 28754692 DOI: 10.1074/Jbc.M117.791723 |
0.344 |
|
| 2017 |
Marqusee S. Touring the Landscape: The View Depends on How and When You Look Biophysical Journal. 112: 178a-179a. DOI: 10.1016/J.Bpj.2016.11.988 |
0.476 |
|
| 2017 |
Hobbs HT, Marqusee S, Kuriyan J. The Effects of Protein Dynamics on Immune System Signaling Pathways Biophysical Journal. 112: 63a. DOI: 10.1016/J.Bpj.2016.11.380 |
0.576 |
|
| 2017 |
Truong HH, Guinn EJ, Marqusee S. Using Single Molecule Force Spectroscopy to Detect High-Energy Intermediates on Protein Folding Pathway Biophysical Journal. 112: 60a. DOI: 10.1016/j.bpj.2016.11.362 |
0.311 |
|
| 2017 |
Hamadani KM, Jensen M, Peng W, Cate JH, Marqusee S. An in Vitro Sample Generation Pipeline for High-Throughput Single-Molecule FRET Based Screening of Proteins Biophysical Journal. 112: 471a. DOI: 10.1016/J.Bpj.2016.11.2530 |
0.309 |
|
| 2017 |
Bolin E, An S, Marqusee S. Folding Pathways of Evolutionarily Related Proteins Probed by Hydrogen Exchange Mass Spectrometry Biophysical Journal. 112: 60a. DOI: 10.1016/J.Bpj.2015.11.1193 |
0.506 |
|
| 2016 |
Samelson AJ, Jensen MK, Soto RA, Cate JH, Marqusee S. Quantitative determination of ribosome nascent chain stability. Proceedings of the National Academy of Sciences of the United States of America. PMID 27821780 DOI: 10.1073/Pnas.1610272113 |
0.495 |
|
| 2016 |
Lim SA, Hart KM, Harms MJ, Marqusee S. Evolutionary trend toward kinetic stability in the folding trajectory of RNases H. Proceedings of the National Academy of Sciences of the United States of America. PMID 27799545 DOI: 10.1073/Pnas.1611781113 |
0.722 |
|
| 2016 |
Wheeler LC, Lim SA, Marqusee S, Harms MJ. The thermostability and specificity of ancient proteins. Current Opinion in Structural Biology. 38: 37-43. PMID 27288744 DOI: 10.1016/J.Sbi.2016.05.015 |
0.42 |
|
| 2016 |
Zhuravlev PI, Hinczewski M, Chakrabarti S, Marqusee S, Thirumalai D. Reply to Alberti: Are in vitro folding experiments relevant in vivo? Proceedings of the National Academy of Sciences of the United States of America. PMID 27226292 DOI: 10.1073/Pnas.1603395113 |
0.396 |
|
| 2016 |
Zhuravlev PI, Hinczewski M, Chakrabarti S, Marqusee S, Thirumalai D. Force-dependent switch in protein unfolding pathways and transition-state movements. Proceedings of the National Academy of Sciences of the United States of America. PMID 26818842 DOI: 10.1073/Pnas.1515730113 |
0.462 |
|
| 2016 |
Guinn EJ, Jagannathan B, Marqusee S. Using Single Molecule Chemo-Mechanical Unfolding to Probe the Effect of Environmental Conditions on the Protein Folding Pathway Biophysical Journal. 110: 393a. DOI: 10.1016/j.bpj.2015.11.2124 |
0.316 |
|
| 2016 |
Samelson A, Soto R, Jensen MK, Marqusee S. A New Tool to Measure Biophysical Properties of Ribosome Nascent Chains Biophysical Journal. 110: 392a. DOI: 10.1016/J.Bpj.2015.11.2119 |
0.497 |
|
| 2016 |
Jensen MK, Hamadani K, Samelson AJ, Cate JH, Marqusee S. The Effect of the Ribosome on Nascent Chain Energy Landscapes Biophysical Journal. 110: 392a. DOI: 10.1016/J.Bpj.2015.11.2118 |
0.519 |
|
| 2016 |
Lim SA, Bolin ER, Harms MJ, Hart KM, Thornton JW, Marqusee S. Ancestral Sequence Reconstruction Reveals the Evolutionary History of the Folding Pathway and Landscape of Ribonucleases H Biophysical Journal. 110: 391a. DOI: 10.1016/J.Bpj.2015.11.2111 |
0.697 |
|
| 2016 |
Wiener DM, Dill JW, Marqusee S. Mechanical Unfolding of E. Coli RNase H Reveals an Intermediate with a Force-Induced Shift in the Rate-Limiting Barrier Biophysical Journal. 110: 180a. DOI: 10.1016/J.Bpj.2015.11.1003 |
0.841 |
|
| 2016 |
Marqusee S. Sequence Constraints on Folding and Binding Biophysical Journal. 110: 3a. DOI: 10.1016/J.Bpj.2015.11.058 |
0.491 |
|
| 2015 |
Koulechova DA, Tripp KW, Horner G, Marqusee S. When the Scaffold Cannot Be Ignored: The Role of the Hydrophobic Core in Ligand Binding and Specificity. Journal of Molecular Biology. 427: 3316-26. PMID 26301601 DOI: 10.1016/J.Jmb.2015.08.014 |
0.803 |
|
| 2015 |
Petzold C, Marceau AH, Miller KH, Marqusee S, Keck JL. Interaction with Single-stranded DNA-binding Protein Stimulates Escherichia coli Ribonuclease HI Enzymatic Activity. The Journal of Biological Chemistry. 290: 14626-36. PMID 25903123 DOI: 10.1074/Jbc.M115.655134 |
0.798 |
|
| 2015 |
Guinn EJ, Jagannathan B, Marqusee S. Single-molecule chemo-mechanical unfolding reveals multiple transition state barriers in a small single-domain protein. Nature Communications. 6: 6861. PMID 25882479 DOI: 10.1038/Ncomms7861 |
0.547 |
|
| 2015 |
Rosen LE, Marqusee S. Autonomously folding protein fragments reveal differences in the energy landscapes of homologous RNases H. Plos One. 10: e0119640. PMID 25803034 DOI: 10.1371/journal.pone.0119640 |
0.438 |
|
| 2015 |
Bowman GR, Bolin ER, Hart KM, Maguire BC, Marqusee S. Discovery of multiple hidden allosteric sites by combining Markov state models and experiments. Proceedings of the National Academy of Sciences of the United States of America. 112: 2734-9. PMID 25730859 DOI: 10.1073/Pnas.1417811112 |
0.615 |
|
| 2015 |
Riedel C, Gabizon R, Wilson CA, Hamadani K, Tsekouras K, Marqusee S, Pressé S, Bustamante C. The heat released during catalytic turnover enhances the diffusion of an enzyme. Nature. 517: 227-30. PMID 25487146 DOI: 10.1038/Nature14043 |
0.66 |
|
| 2015 |
Rosen LE, Kathuria SV, Matthews CR, Bilsel O, Marqusee S. Non-native structure appears in microseconds during the folding of E. coli RNase H. Journal of Molecular Biology. 427: 443-53. PMID 25311861 DOI: 10.1016/J.Jmb.2014.10.003 |
0.499 |
|
| 2014 |
Hart KM, Harms MJ, Schmidt BH, Elya C, Thornton JW, Marqusee S. Thermodynamic system drift in protein evolution. Plos Biology. 12: e1001994. PMID 25386647 DOI: 10.1371/Journal.Pbio.1001994 |
0.7 |
|
| 2014 |
Rosen LE, Connell KB, Marqusee S. Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule. Proceedings of the National Academy of Sciences of the United States of America. 111: 14746-51. PMID 25258414 DOI: 10.1073/Pnas.1410630111 |
0.841 |
|
| 2014 |
Pressé S, Peterson J, Lee J, Elms P, MacCallum JL, Marqusee S, Bustamante C, Dill K. Single molecule conformational memory extraction: p5ab RNA hairpin. The Journal of Physical Chemistry. B. 118: 6597-603. PMID 24898871 DOI: 10.1021/Jp500611F |
0.788 |
|
| 2014 |
Jha SK, Marqusee S. Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride. Proceedings of the National Academy of Sciences of the United States of America. 111: 4856-61. PMID 24639503 DOI: 10.1073/Pnas.1315453111 |
0.475 |
|
| 2014 |
Riedel C, Wilson CW, Hamadani K, Tsekouras K, Marqusee S, Presse S, Bustamante C. The Heat Released by a Chemical Reaction Locally Enhanced the Enzyme Diffusion Biophysical Journal. 106: 668a. DOI: 10.1016/J.Bpj.2013.11.3701 |
0.489 |
|
| 2014 |
Bolin E, Maguire B, Bowman G, Marqusee S. Thiol Labeling Reveals Presence of Cryptic Binding Sites in β-Lactamase Biophysical Journal. 106: 658a. DOI: 10.1016/J.Bpj.2013.11.3642 |
0.352 |
|
| 2014 |
An S, Hart KM, Marqusee S. Exploring the Energy Landscape through Ancestral Proteins Biophysical Journal. 106: 657a. DOI: 10.1016/J.Bpj.2013.11.3638 |
0.692 |
|
| 2014 |
Bowman GR, Geissler PL, Marqusee S. Finding Hidden Allosteric Sites in Proteins Biophysical Journal. 106: 647a. DOI: 10.1016/J.Bpj.2013.11.3581 |
0.366 |
|
| 2014 |
Jagannathan B, Marqusee S. Exploring the Complex Energy Landscape of Protein Unfolding Under Force Biophysical Journal. 106: 470a. DOI: 10.1016/J.Bpj.2013.11.2659 |
0.448 |
|
| 2014 |
Leachman SM, Wilson CA, Marqusee S, Bustamante C. Protein-Folding Studies using Hybrid TIRF SmFRET-Magnetic Tweezers Biophysical Journal. 106: 469a-470a. DOI: 10.1016/J.Bpj.2013.11.2657 |
0.712 |
|
| 2014 |
Rosemond SN, Hamadani KH, Cate JH, Marqusee S. Context-Dependent Folding: Sequence-Encoded Strategies for Stabilizing a Protein Subdomain in Isolation Biophysical Journal. 106: 469a. DOI: 10.1016/J.Bpj.2013.11.2654 |
0.454 |
|
| 2014 |
Rosen LE, Kathuria S, Connell K, Bilsel O, Matthews CR, Marqusee S. Observing and Characterizing Early Folding Intermediates of E.Coli Rnase H using Kinetic and Equilibrium Approaches Biophysical Journal. 106: 246a. DOI: 10.1016/J.Bpj.2013.11.1442 |
0.838 |
|
| 2013 |
Dimster-Denk D, Tripp KW, Marini NJ, Marqusee S, Rine J. Mono and dual cofactor dependence of human cystathionine β-synthase enzyme variants in vivo and in vitro. G3 (Bethesda, Md.). 3: 1619-28. PMID 23934999 DOI: 10.1534/G3.113.006916 |
0.761 |
|
| 2013 |
Jagannathan B, Marqusee S. Protein folding and unfolding under force. Biopolymers. 99: 860-9. PMID 23784721 DOI: 10.1002/Bip.22321 |
0.466 |
|
| 2013 |
Hu W, Walters BT, Kan ZY, Mayne L, Rosen LE, Marqusee S, Englander SW. Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 110: 7684-9. PMID 23603271 DOI: 10.1073/Pnas.1305887110 |
0.512 |
|
| 2013 |
Udgaonkar J, Marqusee S. Folding and binding. Current Opinion in Structural Biology. 23: 1-3. PMID 23374590 DOI: 10.1016/J.Sbi.2013.01.002 |
0.652 |
|
| 2013 |
Hamadani KM, Cate JH, Marqusee S. Mechanisms in Co-Translational Protein Folding Elucidated using Single Molecule FRET Biophysical Journal. 104: 515a. DOI: 10.1016/J.Bpj.2012.11.2844 |
0.467 |
|
| 2013 |
Jagannathan B, Marqusee S. A Tale of Two Pulling Geometries: The Complex Mechanical Behavior of a Simple Protein Biophysical Journal. 104: 369a. DOI: 10.1016/J.Bpj.2012.11.2051 |
0.455 |
|
| 2013 |
Marqusee S. Manipulating the Protein Energy Landscape Biophysical Journal. 104: 355a. DOI: 10.1016/J.Bpj.2012.11.1968 |
0.41 |
|
| 2013 |
Leachman SM, Wilson CA, Cervantes B, Ierokomos A, Marqusee S, Bustamante C. A Hybrid Tirf-Magnetic Tweezers Instrument for Studying Force-Induced Conformational Changes in Proteins Biophysical Journal. 104: 211a. DOI: 10.1016/J.Bpj.2012.11.1192 |
0.69 |
|
| 2012 |
Elms PJ, Chodera JD, Bustamante CJ, Marqusee S. Limitations of constant-force-feedback experiments. Biophysical Journal. 103: 1490-9. PMID 23062341 DOI: 10.1016/J.Bpj.2012.06.051 |
0.793 |
|
| 2012 |
Jagannathan B, Elms PJ, Bustamante C, Marqusee S. Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein. Proceedings of the National Academy of Sciences of the United States of America. 109: 17820-5. PMID 22949695 DOI: 10.1073/Pnas.1201800109 |
0.81 |
|
| 2012 |
Elms PJ, Chodera JD, Bustamante C, Marqusee S. The molten globule state is unusually deformable under mechanical force. Proceedings of the National Academy of Sciences of the United States of America. 109: 3796-801. PMID 22355138 DOI: 10.1073/Pnas.1115519109 |
0.806 |
|
| 2012 |
Leachman SM, Wilson CA, Bustamante C, Marqusee S. A Hybrid Tirf-Magnetic Tweezers Instrument for Studying Sub-Nanometer Effects of Force on Proteins Biophysical Journal. 102: 387a. DOI: 10.1016/J.Bpj.2011.11.2118 |
0.689 |
|
| 2011 |
Miller KH, Marqusee S. Propensity for C-terminal domain swapping correlates with increased regional flexibility in the C-terminus of RNase A. Protein Science : a Publication of the Protein Society. 20: 1735-44. PMID 21805524 DOI: 10.1002/Pro.708 |
0.659 |
|
| 2011 |
Cecconi C, Shank EA, Marqusee S, Bustamante C. DNA molecular handles for single-molecule protein-folding studies by optical tweezers. Methods in Molecular Biology (Clifton, N.J.). 749: 255-71. PMID 21674378 DOI: 10.1007/978-1-61779-142-0_18 |
0.802 |
|
| 2011 |
Bernstein R, Schmidt KL, Harbury PB, Marqusee S. Structural and kinetic mapping of side-chain exposure onto the protein energy landscape. Proceedings of the National Academy of Sciences of the United States of America. 108: 10532-7. PMID 21670244 DOI: 10.1073/Pnas.1103629108 |
0.718 |
|
| 2010 |
Hanes MS, Ratcliff K, Marqusee S, Handel TM. Protein-protein binding affinities by pulse proteolysis: application to TEM-1/BLIP protein complexes. Protein Science : a Publication of the Protein Society. 19: 1996-2000. PMID 20669180 DOI: 10.1002/Pro.467 |
0.732 |
|
| 2010 |
Shank EA, Cecconi C, Dill JW, Marqusee S, Bustamante C. The folding cooperativity of a protein is controlled by its chain topology. Nature. 465: 637-40. PMID 20495548 DOI: 10.1038/Nature09021 |
0.822 |
|
| 2010 |
Ratcliff K, Marqusee S. Identification of residual structure in the unfolded state of ribonuclease H1 from the moderately thermophilic Chlorobium tepidum: comparison with thermophilic and mesophilic homologues. Biochemistry. 49: 5167-75. PMID 20491485 DOI: 10.1021/Bi1001097 |
0.762 |
|
| 2010 |
Miller KH, Karr JR, Marqusee S. A hinge region cis-proline in ribonuclease A acts as a conformational gatekeeper for C-terminal domain swapping. Journal of Molecular Biology. 400: 567-78. PMID 20471398 DOI: 10.1016/J.Jmb.2010.05.017 |
0.639 |
|
| 2010 |
Miller KH, Karr JR, Marqusee S. Addendum to “A Hinge Region Cis-proline in Ribonuclease A Acts as a Conformational Gatekeeper for C-Terminal Domain Swapping” [J. Mol. Biol. 400/3 (2010) 567–578] Journal of Molecular Biology. 403: 825. DOI: 10.1016/J.Jmb.2010.09.010 |
0.592 |
|
| 2010 |
Miller KH, Marqusee S, Karr J. A Hinge Region Cis-Proline in Bovine Pancreatic RNase a Acts as a Conformational Gatekeeper for C-terminal Domain Swapping Biophysical Journal. 98: 630a. DOI: 10.1016/J.Bpj.2009.12.3448 |
0.631 |
|
| 2010 |
Dill J, Bustamante C, Marqusee S. The Unfolding Behavior of RNase H Under Force Biophysical Journal. 98: 617a. DOI: 10.1016/J.Bpj.2009.12.3369 |
0.838 |
|
| 2010 |
Hamadani KM, Cate JH, Marqusee S. Studying Protein Folding on the Ribosome One Molecule at a Time Biophysical Journal. 98: 446a. DOI: 10.1016/J.Bpj.2009.12.2427 |
0.492 |
|
| 2010 |
Tripp KW, Horner GA, Marqusee S. Reengineering Protein Specificity By Repacking the Hydrophobic Core Biophysical Journal. 98: 25a-26a. DOI: 10.1016/J.Bpj.2009.12.151 |
0.809 |
|
| 2009 |
Connell KB, Horner GA, Marqusee S. A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble. Journal of Molecular Biology. 391: 461-70. PMID 19505477 DOI: 10.1016/J.Jmb.2009.05.084 |
0.82 |
|
| 2009 |
Connell KB, Miller EJ, Marqusee S. The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms. Journal of Molecular Biology. 391: 450-60. PMID 19501596 DOI: 10.1016/J.Jmb.2009.05.085 |
0.847 |
|
| 2009 |
Ratcliff K, Corn J, Marqusee S. Structure, stability, and folding of ribonuclease H1 from the moderately thermophilic Chlorobium tepidum: comparison with thermophilic and mesophilic homologues. Biochemistry. 48: 5890-8. PMID 19408959 DOI: 10.1021/Bi900305P |
0.758 |
|
| 2009 |
Zhang CZ, Seog J, Dill J, Smith SB, Zhang FX, Cecconi C, Marqusee S, Bustamante C, Springer TA. What can we learn from mechanical unfolding of a single protein domain by optical tweezers Aiche Annual Meeting, Conference Proceedings. |
0.79 |
|
| 2008 |
Cecconi C, Shank EA, Dahlquist FW, Marqusee S, Bustamante C. Protein-DNA chimeras for single molecule mechanical folding studies with the optical tweezers. European Biophysics Journal : Ebj. 37: 729-38. PMID 18183383 DOI: 10.1007/S00249-007-0247-Y |
0.804 |
|
| 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 |
0.835 |
|
| 2007 |
Cellitti J, Bernstein R, Marqusee S. Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway. Protein Science : a Publication of the Protein Society. 16: 852-62. PMID 17400925 DOI: 10.1110/Ps.062632807 |
0.833 |
|
| 2007 |
Park C, Zhou S, Gilmore J, Marqusee S. Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis. Journal of Molecular Biology. 368: 1426-37. PMID 17400245 DOI: 10.1016/J.Jmb.2007.02.091 |
0.627 |
|
| 2007 |
Young TA, Skordalakes E, Marqusee S. Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability. Journal of Molecular Biology. 368: 1438-47. PMID 17397866 DOI: 10.1016/J.Jmb.2007.02.077 |
0.675 |
|
| 2007 |
Cecconi C, Shank EA, Marqusee S, Bustamante CJ. Studying protein folding with laser tweezers Proceedings of the International School of Physics "Enrico Fermi". 165: 145-160. |
0.748 |
|
| 2006 |
Park C, Marqusee S. Quantitative determination of protein stability and ligand binding by pulse proteolysis. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit 20.11. PMID 18429306 DOI: 10.1002/0471140864.Ps2011S46 |
0.579 |
|
| 2006 |
Freedman TS, Sondermann H, Friedland GD, Kortemme T, Bar-Sagi D, Marqusee S, Kuriyan J. A Ras-induced conformational switch in the Ras activator Son of sevenless. Proceedings of the National Academy of Sciences of the United States of America. 103: 16692-7. PMID 17075039 DOI: 10.1073/Pnas.0608127103 |
0.772 |
|
| 2006 |
Wildes D, Anderson LM, Sabogal A, Marqusee S. Native state energetics of the Src SH2 domain: evidence for a partially structured state in the denatured ensemble. Protein Science : a Publication of the Protein Society. 15: 1769-79. PMID 16751610 DOI: 10.1110/Ps.062136006 |
0.811 |
|
| 2006 |
de los Rios MA, Muralidhara BK, Wildes D, Sosnick TR, Marqusee S, Wittung-Stafshede P, Plaxco KW, Ruczinski I. On the precision of experimentally determined protein folding rates and phi-values. Protein Science : a Publication of the Protein Society. 15: 553-63. PMID 16501226 DOI: 10.1110/Ps.051870506 |
0.785 |
|
| 2005 |
Cecconi C, Shank EA, Bustamante C, Marqusee S. Direct observation of the three-state folding of a single protein molecule. Science (New York, N.Y.). 309: 2057-60. PMID 16179479 DOI: 10.1126/Science.1116702 |
0.803 |
|
| 2005 |
Park C, Marqusee S. Pulse proteolysis: a simple method for quantitative determination of protein stability and ligand binding. Nature Methods. 2: 207-12. PMID 15782190 DOI: 10.1038/Nmeth740 |
0.62 |
|
| 2005 |
Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallée-Bélisle A, Main ER, Bemporad F, Qiu L, Teilum K, ... ... Marqusee S, et al. Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Science : a Publication of the Protein Society. 14: 602-16. PMID 15689503 DOI: 10.1110/Ps.041205405 |
0.821 |
|
| 2005 |
Wildes D, Marqusee S. Hydrogen exchange and ligand binding: ligand-dependent and ligand-independent protection in the Src SH3 domain. Protein Science : a Publication of the Protein Society. 14: 81-8. PMID 15576569 DOI: 10.1110/Ps.04990205 |
0.783 |
|
| 2004 |
Park C, Marqusee S. Probing the high energy states in proteins by proteolysis. Journal of Molecular Biology. 343: 1467-76. PMID 15491624 DOI: 10.1016/J.Jmb.2004.08.085 |
0.644 |
|
| 2004 |
Park C, Marqusee S. Analysis of the stability of multimeric proteins by effective DeltaG and effective m-values. Protein Science : a Publication of the Protein Society. 13: 2553-8. PMID 15322294 DOI: 10.1110/Ps.04811004 |
0.578 |
|
| 2004 |
Wildes D, Marqusee S. Hydrogen-exchange strategies applied to energetics of intermediate processes in protein folding. Methods in Enzymology. 380: 328-49. PMID 15051344 DOI: 10.1016/S0076-6879(04)80015-6 |
0.8 |
|
| 2004 |
Spudich GM, Miller EJ, Marqusee S. Destabilization of the Escherichia coli RNase H kinetic intermediate: switching between a two-state and three-state folding mechanism. Journal of Molecular Biology. 335: 609-18. PMID 14672667 DOI: 10.1016/J.Jmb.2003.10.052 |
0.829 |
|
| 2003 |
Robic S, Guzman-Casado M, Sanchez-Ruiz JM, Marqusee S. Role of residual structure in the unfolded state of a thermophilic protein. Proceedings of the National Academy of Sciences of the United States of America. 100: 11345-9. PMID 14504401 DOI: 10.1073/Pnas.1635051100 |
0.814 |
|
| 2003 |
Kim R, Lai L, Lee HH, Cheong GW, Kim KK, Wu Z, Yokota H, Marqusee S, Kim SH. On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii. Proceedings of the National Academy of Sciences of the United States of America. 100: 8151-5. PMID 12817080 DOI: 10.1073/Pnas.1032940100 |
0.433 |
|
| 2003 |
Guzman-Casado M, Parody-Morreale A, Robic S, Marqusee S, Sanchez-Ruiz JM. Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of Thermus thermophilus ribonuclease H. Journal of Molecular Biology. 329: 731-43. PMID 12787674 DOI: 10.1016/S0022-2836(03)00513-8 |
0.764 |
|
| 2002 |
Miller EJ, Fischer KF, Marqusee S. Experimental evaluation of topological parameters determining protein-folding rates. Proceedings of the National Academy of Sciences of the United States of America. 99: 10359-63. PMID 12149462 DOI: 10.1073/Pnas.162219099 |
0.788 |
|
| 2002 |
Kern G, Pelton J, Marqusee S, Kern D. Structural properties of the histidine-containing loop in HIV-1 RNase H. Biophysical Chemistry. 96: 285-91. PMID 12034447 DOI: 10.1016/S0301-4622(02)00019-4 |
0.438 |
|
| 2002 |
Nicholson EM, Mo H, Prusiner SB, Cohen FE, Marqusee S. Differences between the prion protein and its homolog Doppel: a partially structured state with implications for scrapie formation. Journal of Molecular Biology. 316: 807-15. PMID 11866533 DOI: 10.1006/Jmbi.2001.5347 |
0.569 |
|
| 2002 |
Hollien J, Marqusee S. Comparison of the folding processes of T. thermophilus and E. coli ribonucleases H. Journal of Molecular Biology. 316: 327-40. PMID 11851342 DOI: 10.1006/Jmbi.2001.5346 |
0.802 |
|
| 2002 |
Spudich G, Lorenz S, Marqusee S. Propagation of a single destabilizing mutation throughout the Escherichia coli ribonuclease HI native state. Protein Science : a Publication of the Protein Society. 11: 522-8. PMID 11847275 DOI: 10.1110/Ps.37202 |
0.799 |
|
| 2002 |
Robic S, Berger JM, Marqusee S. Contributions of folding cores to the thermostabilities of two ribonucleases H. Protein Science : a Publication of the Protein Society. 11: 381-9. PMID 11790848 DOI: 10.1110/Ps.38602 |
0.815 |
|
| 2001 |
Goedken ER, Marqusee S. Native-state energetics of a thermostabilized variant of ribonuclease HI. Journal of Molecular Biology. 314: 863-71. PMID 11734003 DOI: 10.1006/Jmbi.2001.5184 |
0.801 |
|
| 2001 |
Parker MJ, Marqusee S. A kinetic folding intermediate probed by native state hydrogen exchange. Journal of Molecular Biology. 305: 593-602. PMID 11152615 DOI: 10.1006/Jmbi.2000.4314 |
0.362 |
|
| 2001 |
Goedken ER, Marqusee S. Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two divalent metals bound in the active site. The Journal of Biological Chemistry. 276: 7266-71. PMID 11083878 DOI: 10.1074/Jbc.M009626200 |
0.716 |
|
| 2000 |
Goedken ER, Keck JL, Berger JM, Marqusee S. Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI. Protein Science : a Publication of the Protein Society. 9: 1914-21. PMID 11106164 DOI: 10.1110/Ps.9.10.1914 |
0.811 |
|
| 2000 |
Spudich G, Marqusee S. A change in the apparent m value reveals a populated intermediate under equilibrium conditions in Escherichia coli ribonuclease HI. Biochemistry. 39: 11677-83. PMID 10995235 DOI: 10.1021/Bi000466U |
0.766 |
|
| 2000 |
Fischer KF, Marqusee S. A rapid test for identification of autonomous folding units in proteins. Journal of Molecular Biology. 302: 701-12. PMID 10986128 DOI: 10.1006/Jmbi.2000.4049 |
0.749 |
|
| 2000 |
Toth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO. The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. Journal of Molecular Biology. 301: 433-50. PMID 10926519 DOI: 10.1006/Jmbi.2000.3970 |
0.769 |
|
| 2000 |
Parker MJ, Marqusee S. A statistical appraisal of native state hydrogen exchange data: evidence for a burst phase continuum? Journal of Molecular Biology. 300: 1361-75. PMID 10903874 DOI: 10.1006/Jmbi.2000.3922 |
0.449 |
|
| 2000 |
Chamberlain AK, Marqusee S. Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms. Advances in Protein Chemistry. 53: 283-328. PMID 10751947 DOI: 10.1016/S0065-3233(00)53006-X |
0.526 |
|
| 1999 |
Goedken ER, Marqusee S. Metal binding and activation of the ribonuclease H domain from moloney murine leukemia virus. Protein Engineering. 12: 975-80. PMID 10585503 DOI: 10.1093/Protein/12.11.975 |
0.732 |
|
| 1999 |
Hollien J, Marqusee S. Structural distribution of stability in a thermophilic enzyme. Proceedings of the National Academy of Sciences of the United States of America. 96: 13674-8. PMID 10570131 DOI: 10.1073/Pnas.96.24.13674 |
0.781 |
|
| 1999 |
Parker MJ, Marqusee S. The cooperativity of burst phase reactions explored. Journal of Molecular Biology. 293: 1195-210. PMID 10547295 DOI: 10.1006/Jmbi.1999.3204 |
0.431 |
|
| 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 |
0.657 |
|
| 1999 |
Raschke TM, Kho J, Marqusee S. Confirmation of the hierarchical folding of RNase H: a protein engineering study. Nature Structural Biology. 6: 825-31. PMID 10467093 DOI: 10.1038/12277 |
0.53 |
|
| 1999 |
Liu H, Farr-Jones S, Ulyanov NB, Llinas M, Marqusee S, Groth D, Cohen FE, Prusiner SB, James TL. Solution structure of Syrian hamster prion protein rPrP(90-231). Biochemistry. 38: 5362-77. PMID 10220323 DOI: 10.1021/Bi982878X |
0.698 |
|
| 1999 |
Hollien J, Marqusee S. A thermodynamic comparison of mesophilic and thermophilic ribonucleases H. Biochemistry. 38: 3831-6. PMID 10090773 DOI: 10.1021/Bi982684H |
0.776 |
|
| 1998 |
Keck JL, Goedken ER, Marqusee S. Activation/attenuation model for RNase H. A one-metal mechanism with second-metal inhibition. The Journal of Biological Chemistry. 273: 34128-33. PMID 9852071 DOI: 10.1074/Jbc.273.51.34128 |
0.77 |
|
| 1998 |
Kern G, Handel T, Marqusee S. Characterization of a folding intermediate from HIV-1 ribonuclease H. Protein Science : a Publication of the Protein Society. 7: 2164-74. PMID 9792104 DOI: 10.1002/Pro.5560071014 |
0.357 |
|
| 1998 |
Goedken ER, Marqusee S. Folding the ribonuclease H domain of Moloney murine leukemia virus reverse transcriptase requires metal binding or a short N-terminal extension. Proteins. 33: 135-43. PMID 9741851 DOI: 10.1002/(Sici)1097-0134(19981001)33:1<135::Aid-Prot12>3.0.Co;2-M |
0.755 |
|
| 1998 |
Llinás M, Marqusee S. Subdomain interactions as a determinant in the folding and stability of T4 lysozyme. Protein Science : a Publication of the Protein Society. 7: 96-104. PMID 9514264 DOI: 10.1002/Pro.5560070110 |
0.698 |
|
| 1998 |
Raschke TM, Marqusee S. Hydrogen exchange studies of protein structure. Current Opinion in Biotechnology. 9: 80-6. PMID 9503592 DOI: 10.1016/S0958-1669(98)80088-8 |
0.498 |
|
| 1998 |
Chamberlain AK, Marqusee S. Molten globule unfolding monitored by hydrogen exchange in urea. Biochemistry. 37: 1736-42. PMID 9492739 DOI: 10.1021/Bi972692I |
0.402 |
|
| 1997 |
Chamberlain AK, Marqusee S. Touring the landscapes: partially folded proteins examined by hydrogen exchange. Structure (London, England : 1993). 5: 859-63. PMID 9261079 DOI: 10.1016/S0969-2126(97)00240-2 |
0.538 |
|
| 1997 |
Goedken ER, Raschke TM, Marqusee S. Importance of the C-terminal helix to the stability and enzymatic activity of Escherichia coli ribonuclease H. Biochemistry. 36: 7256-63. PMID 9188727 DOI: 10.1021/Bi970060Q |
0.751 |
|
| 1997 |
Raschke TM, Marqusee S. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nature Structural Biology. 4: 298-304. PMID 9095198 DOI: 10.1038/Nsb0497-298 |
0.489 |
|
| 1997 |
Chamberlain AK, Handel TM, Marqusee S. Detection of protein unfolding and fluctuations by native state hydrogen exchange Techniques in Protein Chemistry. 8: 727-734. DOI: 10.1016/S1080-8914(97)80071-3 |
0.482 |
|
| 1997 |
Keck JL, Marqusee S. Metal activation and regulation of E. coli RNase H Techniques in Protein Chemistry. 8: 409-416. DOI: 10.1016/S1080-8914(97)80041-5 |
0.619 |
|
| 1996 |
Dabora JM, Pelton JG, Marqusee S. Structure of the acid state of Escherichia coli ribonuclease HI. Biochemistry. 35: 11951-8. PMID 8810899 DOI: 10.1021/Bi9611671 |
0.454 |
|
| 1996 |
Chamberlain AK, Handel TM, Marqusee S. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nature Structural Biology. 3: 782-7. PMID 8784352 DOI: 10.1038/Nsb0996-782 |
0.55 |
|
| 1996 |
Keck JL, Marqusee S. The putative substrate recognition loop of Escherichia coli ribonuclease H is not essential for activity. The Journal of Biological Chemistry. 271: 19883-7. PMID 8702700 DOI: 10.1074/Jbc.271.33.19883 |
0.631 |
|
| 1995 |
Keck JL, Marqusee S. Substitution of a highly basic helix/loop sequence into the RNase H domain of human immunodeficiency virus reverse transcriptase restores its Mn(2+)-dependent RNase H activity. Proceedings of the National Academy of Sciences of the United States of America. 92: 2740-4. PMID 7535929 DOI: 10.1073/Pnas.92.7.2740 |
0.591 |
|
| 1994 |
Dabora JM, Marqusee S. Equilibrium unfolding of Escherichia coli ribonuclease H: characterization of a partially folded state. Protein Science : a Publication of the Protein Society. 3: 1401-8. PMID 7833802 DOI: 10.1002/Pro.5560030906 |
0.449 |
|
| 1994 |
Marqusee S, Sauer RT. Contributions of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structure in lambda repressor. Protein Science : a Publication of the Protein Society. 3: 2217-25. PMID 7756981 DOI: 10.1002/Pro.5560031207 |
0.544 |
|
| 1991 |
Marqusee S, Regan L. Deconstructing protein structure. Current Biology : Cb. 1: 207-8. PMID 15336120 DOI: 10.1016/0960-9822(91)90057-4 |
0.373 |
|
| 1991 |
Scholtz JM, Marqusee S, Baldwin RL, York EJ, Stewart JM, Santoro M, Bolen DW. Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water. Proceedings of the National Academy of Sciences of the United States of America. 88: 2854-8. PMID 2011594 DOI: 10.1073/Pnas.88.7.2854 |
0.67 |
|
| 1990 |
Padmanabhan S, Marqusee S, Ridgeway T, Laue TM, Baldwin RL. Relative helix-forming tendencies of nonpolar amino acids. Nature. 344: 268-70. PMID 2314462 DOI: 10.1038/344268A0 |
0.454 |
|
| 1989 |
Marqusee S, Robbins VH, Baldwin RL. Unusually stable helix formation in short alanine-based peptides. Proceedings of the National Academy of Sciences of the United States of America. 86: 5286-90. PMID 2748584 DOI: 10.1073/Pnas.86.14.5286 |
0.471 |
|
| 1987 |
Marqusee S, Baldwin RL. Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design. Proceedings of the National Academy of Sciences of the United States of America. 84: 8898-902. PMID 3122208 DOI: 10.1073/Pnas.84.24.8898 |
0.436 |
|
| 1985 |
Shoemaker KR, Kim PS, Brems DN, Marqusee S, York EJ, Chaiken IM, Stewart JM, Baldwin RL. Nature of the charged-group effect on the stability of the C-peptide helix. Proceedings of the National Academy of Sciences of the United States of America. 82: 2349-53. PMID 3857585 DOI: 10.1073/Pnas.82.8.2349 |
0.634 |
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