Year |
Citation |
Score |
2024 |
Masse MM, Guzman-Luna V, Varela AE, Mahfuza Shapla U, Hutchinson RB, Srivastava A, Wei W, Fuchs AM, Cavagnero S. Nascent chains derived from a foldable protein sequence interact with specific ribosomal surface sites near the exit tunnel. Scientific Reports. 14: 12324. PMID 38811604 DOI: 10.1038/s41598-024-61274-1 |
0.404 |
|
2024 |
Masse MM, Hutchinson RB, Morgan CE, Allaman HJ, Guan H, Yu EW, Cavagnero S. Mapping Protein-Protein Interactions at Birth: Single-Particle Cryo-EM Analysis of a Ribosome-Nascent Globin Complex. Acs Central Science. 10: 385-401. PMID 38435509 DOI: 10.1021/acscentsci.3c00777 |
0.394 |
|
2023 |
Addabbo RM, Hutchinson RB, Allaman HJ, Dalphin MD, Mecha MF, Liu Y, Staikos A, Cavagnero S. Critical Beginnings: Selective Tuning of Solubility and Structural Accuracy of Newly Synthesized Proteins by the Hsp70 Chaperone System. The Journal of Physical Chemistry. B. 127: 3990-4014. PMID 37130318 DOI: 10.1021/acs.jpcb.2c08485 |
0.376 |
|
2023 |
Eills J, Budker D, Cavagnero S, Chekmenev EY, Elliott SJ, Jannin S, Lesage A, Matysik J, Meersmann T, Prisner T, Reimer JA, Yang H, Koptyug IV. Spin Hyperpolarization in Modern Magnetic Resonance. Chemical Reviews. PMID 36701528 DOI: 10.1021/acs.chemrev.2c00534 |
0.408 |
|
2022 |
Chen X, Hutchinson RB, Cavagnero S. Distribution and solvent exposure of Hsp70 chaperone binding sites across the Escherichia coli proteome. Proteins. PMID 36539330 DOI: 10.1002/prot.26456 |
0.337 |
|
2022 |
Mecha MF, Hutchinson RB, Lee JH, Cavagnero S. Protein folding in vitro and in the cell: From a solitary journey to a team effort. Biophysical Chemistry. 287: 106821. PMID 35667131 DOI: 10.1016/j.bpc.2022.106821 |
0.401 |
|
2021 |
Guzman-Luna V, Fuchs AM, Allen AJ, Staikos A, Cavagnero S. An intrinsically disordered nascent protein interacts with specific regions of the ribosomal surface near the exit tunnel. Communications Biology. 4: 1236. PMID 34716402 DOI: 10.1038/s42003-021-02752-4 |
0.344 |
|
2021 |
Hutchinson RB, Chen X, Zhou N, Cavagnero S. Fluorescence Anisotropy Decays and Microscale-Volume Viscometry Reveal the Compaction of Ribosome-Bound Nascent Proteins. The Journal of Physical Chemistry. B. PMID 34110829 DOI: 10.1021/acs.jpcb.1c04473 |
0.357 |
|
2020 |
Addabbo RM, Dalphin MD, Mecha MF, Liu Y, Staikos A, Guzman-Luna V, Cavagnero S. Complementary Role of Co- and Post-Translational Events in Protein Biogenesis. The Journal of Physical Chemistry. B. PMID 32456434 DOI: 10.1021/Acs.Jpcb.0C03039 |
0.55 |
|
2020 |
Yaeger-Weiss SK, Jennaro TS, Mecha MM, Becker JH, Yang H, Winkler GLW, Cavagnero S. Net Charge and Nonpolar Content Guide the Identification of Folded and Prion Proteins. Biochemistry. PMID 32352283 DOI: 10.1021/Acs.Biochem.9B01114 |
0.487 |
|
2020 |
Dalphin MD, Stangl AJ, Liu Y, Cavagnero S. KLR-70: A Novel Cationic Inhibitor of the Bacterial Hsp70 Chaperone. Biochemistry. PMID 32326704 DOI: 10.1021/Acs.Biochem.0C00320 |
0.424 |
|
2020 |
Lee J, Park SH, Cavagnero S, Lee JH. High-Resolution Diffusion Measurements of Proteins by NMR under Near-Physiological Conditions. Analytical Chemistry. PMID 32163276 DOI: 10.1021/Acs.Analchem.9B05453 |
0.313 |
|
2020 |
Masse MM, Varela AE, Srivastava A, Cavagnero S. Effect of Nascent Proteins on the Stability of the Ribosome Biophysical Journal. 118. DOI: 10.1016/J.Bpj.2019.11.1187 |
0.454 |
|
2019 |
Yang H, Hofstetter H, Cavagnero S. Fast-pulsing LED-enhanced NMR: A convenient and inexpensive approach to increase NMR sensitivity. The Journal of Chemical Physics. 151: 245102. PMID 31893873 DOI: 10.1063/1.5131452 |
0.334 |
|
2019 |
Varela AE, England KA, Cavagnero S. Kinetic trapping in protein folding. Protein Engineering, Design & Selection : Peds. PMID 31390019 DOI: 10.1093/Protein/Gzz018 |
0.488 |
|
2019 |
Okuno Y, Mecha MF, Yang H, Zhu L, Fry CG, Cavagnero S. Laser- and cryogenic probe-assisted NMR enables hypersensitive analysis of biomolecules at submicromolar concentration. Proceedings of the National Academy of Sciences of the United States of America. PMID 31142651 DOI: 10.1073/Pnas.1820573116 |
0.397 |
|
2019 |
Dalphin MD, Varela A, Stangl A, Kirchdoerfer R, Addabbo R, Song YJ, Liu Y, Cavagnero S. The Earliest Stages of a Protein's Life Influences its Long-Term Solubility and Structural Accuracy Biophysical Journal. 116. DOI: 10.1016/J.Bpj.2018.11.1062 |
0.345 |
|
2018 |
Varela AE, Lang JF, Wu Y, Dalphin MD, Stangl AJ, Okuno Y, Cavagnero S. Kinetic Trapping of Folded Proteins Relative to Aggregates under Physiologically Relevant Conditions. The Journal of Physical Chemistry. B. PMID 30001623 DOI: 10.1021/Acs.Jpcb.8B05360 |
0.686 |
|
2018 |
Mecha M, Okuno Y, Yang H, Cavagnero S. Laser-assisted NMR in the Presence of a Cryogenic Probe Enables Multidimensional Data Collection on Amino Acids and Proteins at Unprecedented Sensitivity Biophysical Journal. 114: 158a. DOI: 10.1016/J.Bpj.2017.11.886 |
0.361 |
|
2018 |
Dalphin MD, Song YJ, Addabbo R, Liu Y, Varela A, Stangl A, Jennaro T, Cavagnero S. Insights into the Balance between Folding and Aggregation during a Protein's Life Biophysical Journal. 114. DOI: 10.1016/J.Bpj.2017.11.3230 |
0.422 |
|
2018 |
Addabbo RM, Dalphin MD, Liu Y, Mecha MF, Cavagnero S. Teasing Apart the Role of the Ribosome and Molecular Chaperones in Cellular Protein Folding Biophysical Journal. 114: 414a. DOI: 10.1016/J.Bpj.2017.11.2293 |
0.493 |
|
2017 |
Carlson TM, Lam KW, Lam CW, He JZ, Maynard JH, Cavagnero S. Naked-Eye Detection of Reversible Protein Folding and Unfolding in Aqueous Solution Journal of Chemical Education. 94: 350-355. DOI: 10.1021/Acs.Jchemed.6B00507 |
0.474 |
|
2017 |
Addabbo RM, Dalphin MD, Liu Y, Mecha MF, Cavagnero S. Protein Sculpting: Probing the Interplay between the Ribosome and Molecular Chaperones in Protein Folding in the Cell Biophysical Journal. 112: 41a. DOI: 10.1016/J.Bpj.2016.11.260 |
0.525 |
|
2017 |
Cavagnero S, Addabbo RM, Dalphin MD, Liu Y, Mecha MF. Channeling Nascent Proteins Towards the Native State: Role of the Ribosome and Molecular Chaperones Biophysical Journal. 112: 15a. DOI: 10.1016/J.Bpj.2016.11.113 |
0.529 |
|
2016 |
Addabbo RM, Lam HN, Arnold B, Cavagnero S. Kinetic Compensation between Ester-Bond Cleavage, Folding and Release from the Ribosome in Protein Biogenesis Biophysical Journal. 110. DOI: 10.1016/J.Bpj.2015.11.2117 |
0.492 |
|
2015 |
Lee JH, Zhang D, Hughes C, Okuno Y, Sekhar A, Cavagnero S. Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone. Proceedings of the National Academy of Sciences of the United States of America. 112: E4206-15. PMID 26195753 DOI: 10.1073/Pnas.1505173112 |
0.703 |
|
2015 |
Lee JH, Zhang D, Hughes C, Okuno Y, Sekhar A, Cavagnero S. Backbone chemical shift assignments for the folded/unfolded drkN SH3 protein at pH 7.2 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25501 |
0.645 |
|
2015 |
Lee JH, Zhang D, Hughes C, Okuno Y, Sekhar A, Cavagnero S. Backbone chemical shift assignments for the folded/unfolded drkN SH3 protein in the presence of DnaK chaperone at pH 7.2 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25500 |
0.653 |
|
2015 |
Addabbo RM, Lam HN, Arnold B, Cavagnero S. The Kinetics of Nascent Protein Folding upon Release from the Ribosome Biophysical Journal. 108. DOI: 10.1016/J.Bpj.2014.11.650 |
0.511 |
|
2014 |
Jennaro TS, Beaty MR, Kurt-Yilmaz N, Luskin BL, Cavagnero S. Burial of nonpolar surface area and thermodynamic stabilization of globins as a function of chain elongation. Proteins. 82: 2318-31. PMID 24752983 DOI: 10.1002/Prot.24590 |
0.463 |
|
2014 |
Fedyukina DV, Jennaro TS, Cavagnero S. Charge segregation and low hydrophobicity are key features of ribosomal proteins from different organisms. The Journal of Biological Chemistry. 289: 6740-50. PMID 24398678 DOI: 10.1074/Jbc.M113.507707 |
0.789 |
|
2013 |
Zhu L, Kurt N, Choi J, Lapidus LJ, Cavagnero S. Sub-millisecond chain collapse of the Escherichia coli globin ApoHmpH. The Journal of Physical Chemistry. B. 117: 7868-77. PMID 23750553 DOI: 10.1021/Jp400174E |
0.42 |
|
2013 |
Knight AM, Culviner PH, Kurt-Yilmaz N, Zou T, Ozkan SB, Cavagnero S. Electrostatic effect of the ribosomal surface on nascent polypeptide dynamics. Acs Chemical Biology. 8: 1195-204. PMID 23517476 DOI: 10.1021/Cb400030N |
0.481 |
|
2013 |
Addabbo RM, Arnold B, Cavagnero S. Exploring the Kinetics of Protein Birth Biophysical Journal. 104. DOI: 10.1016/J.Bpj.2012.11.3200 |
0.537 |
|
2013 |
Lee JH, Sekhar A, Zhang D, Santiago M, Lam HN, Cavagnero S. Interaction of RNase HD and Sh3 Proteins with DnaK Molecular Chaperone Biophysical Journal. 104: 570a. DOI: 10.1016/J.Bpj.2012.11.3166 |
0.691 |
|
2012 |
Sekhar A, Lam HN, Cavagnero S. Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system. Protein Science : a Publication of the Protein Society. 21: 1489-502. PMID 22886941 DOI: 10.1002/Pro.2139 |
0.65 |
|
2012 |
Sekhar A, Santiago M, Lam HN, Lee JH, Cavagnero S. Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery. Protein Science : a Publication of the Protein Society. 21: 1042-55. PMID 22549943 DOI: 10.1002/Pro.2087 |
0.643 |
|
2012 |
Rajagopalan S, Cavagnero S, Kurt N, Kwon J. Backbone 1H, 13CA, and 15N Chemical Shifts Assignments and 15N T1 and T2 Relaxation Parameters for the N-terminal (1-119) Fragment of sperm whale apomyoglobin in the presence of DnaK-beta Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16218 |
0.581 |
|
2012 |
Rajagopalan S, Cavagnero S, Kurt N, Kwon J. Backbone 1H, 13CA, and 15N Chemical Shifts Assignments and 15N T1 and T2 Relaxation Parameters for the N-terminal (1-119) Fragment of sperm whale apomyoglobin Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16217 |
0.58 |
|
2011 |
Lee JH, Sekhar A, Cavagnero S. 1H-Detected 13C photo-CIDNP as a sensitivity enhancement tool in solution NMR. Journal of the American Chemical Society. 133: 8062-5. PMID 21548581 DOI: 10.1021/Ja111613C |
0.595 |
|
2011 |
Armstrong BD, Choi J, López C, Wesener DA, Hubbell W, Cavagnero S, Han S. Site-specific hydration dynamics in the nonpolar core of a molten globule by dynamic nuclear polarization of water. Journal of the American Chemical Society. 133: 5987-95. PMID 21443207 DOI: 10.1021/Ja111515S |
0.424 |
|
2011 |
Fedyukina DV, Cavagnero S. Protein folding at the exit tunnel. Annual Review of Biophysics. 40: 337-59. PMID 21370971 DOI: 10.1146/Annurev-Biophys-042910-155338 |
0.809 |
|
2011 |
Rajagopalan S, Kurt N, Cavagnero S. High-resolution conformation and backbone dynamics of a soluble aggregate of apomyoglobin119. Biophysical Journal. 100: 747-55. PMID 21281590 DOI: 10.1016/J.Bpj.2010.12.3722 |
0.673 |
|
2011 |
Cavagnero S. Protein Folding Trends in the Cellular Environment Biophysical Journal. 100: 6a. DOI: 10.1016/J.Bpj.2010.12.241 |
0.544 |
|
2011 |
Zou T, Cavagnero S, Ozkan B. Effect of Ribosomal Surface on Nascent Chain Dynamics Biophysical Journal. 100: 399a. DOI: 10.1016/J.Bpj.2010.12.2369 |
0.434 |
|
2010 |
Fedyukina DV, Rajagopalan S, Sekhar A, Fulmer EC, Eun YJ, Cavagnero S. Contribution of long-range interactions to the secondary structure of an unfolded globin. Biophysical Journal. 99: L37-9. PMID 20816043 DOI: 10.1016/J.Bpj.2010.06.038 |
0.763 |
|
2010 |
Weinreis SA, Ellis JP, Cavagnero S. Dynamic fluorescence depolarization: a powerful tool to explore protein folding on the ribosome. Methods (San Diego, Calif.). 52: 57-73. PMID 20685617 DOI: 10.1016/J.Ymeth.2010.06.001 |
0.719 |
|
2010 |
Ziehr DR, Ellis JP, Culviner PH, Cavagnero S. Production of ribosome-released nascent proteins with optimal physical properties. Analytical Chemistry. 82: 4637-43. PMID 20397641 DOI: 10.1021/Ac902952B |
0.691 |
|
2010 |
Fedyukina D, Cavagnero S. (1-153)Apomyoglobin Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16501 |
0.738 |
|
2010 |
Ellis JP, Culviner PH, Cavagnero S. Confined dynamics of a ribosome-bound nascent globin: Cone angle analysis of fluorescence depolarization decays in the presence of two local motions (Protein Science (2009) 18, (2003-2015)) Protein Science. 19: 1600. DOI: 10.1002/pro.436 |
0.625 |
|
2009 |
Sekhar A, Cavagnero S. EPIC- and CHANCE-HSQC: two 15N-photo-CIDNP-enhanced pulse sequences for the sensitive detection of solvent-exposed tryptophan. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 200: 207-13. PMID 19643649 DOI: 10.1016/J.Jmr.2009.07.001 |
0.577 |
|
2009 |
Ellis JP, Culviner PH, Cavagnero S. Confined dynamics of a ribosome-bound nascent globin: Cone angle analysis of fluorescence depolarization decays in the presence of two local motions. Protein Science : a Publication of the Protein Society. 18: 2003-15. PMID 19569194 DOI: 10.1002/Pro.196 |
0.699 |
|
2009 |
Sekhar A, Cavagnero S. 1H photo-CIDNP enhancements in heteronuclear correlation NMR spectroscopy. The Journal of Physical Chemistry. B. 113: 8310-8. PMID 19462951 DOI: 10.1021/Jp901000Z |
0.584 |
|
2009 |
Mounce BC, Kurt N, Ellison PA, Cavagnero S. Nonrandom distribution of intramolecular contacts in native single-domain proteins. Proteins. 75: 404-12. PMID 18831044 DOI: 10.1002/Prot.22258 |
0.489 |
|
2009 |
Sekhar A, Cavagnero S. 1H photo-CIDNP enhancements in heteronuclear correlation NMR spectroscopy (Journal of Physical Chemistry B (2009) 113B (8310)) Journal of Physical Chemistry B. 113: 10548. DOI: 10.1021/jp905605u |
0.472 |
|
2009 |
Santiago M, Sekhar A, Cavagnero S. Experimental Studies on Protein Folding in the Presence of the Hsp70 Chaperone System Biophysical Journal. 96: 81a. DOI: 10.1016/J.Bpj.2008.12.321 |
0.661 |
|
2008 |
Ellis JP, Bakke CK, Kirchdoerfer RN, Jungbauer LM, Cavagnero S. Chain dynamics of nascent polypeptides emerging from the ribosome. Acs Chemical Biology. 3: 555-66. PMID 18717565 DOI: 10.1021/Cb800059U |
0.795 |
|
2008 |
Kurt N, Mounce BC, Ellison PA, Cavagnero S. Residue-specific contact order and contact breadth in single-domain proteins: implications for folding as a function of chain elongation. Biotechnology Progress. 24: 570-5. PMID 18471028 DOI: 10.1021/Bp070475V |
0.516 |
|
2008 |
Kurt N, Cavagnero S. Nonnative helical motif in a chaperone-bound protein fragment. Biophysical Journal. 94: L48-50. PMID 18192369 DOI: 10.1529/Biophysj.107.127647 |
0.475 |
|
2008 |
Eun YJ, Kurt N, Sekhar A, Cavagnero S. Thermodynamic and kinetic characterization of apoHmpH, a fast-folding bacterial globin. Journal of Molecular Biology. 376: 879-97. PMID 18187151 DOI: 10.1016/J.Jmb.2007.11.038 |
0.649 |
|
2007 |
Kirchdoerfer RN, Huang JJ, Isola MK, Cavagnero S. Fluorescence-based analysis of aminoacyl- and peptidyl-tRNA by low-pH sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Analytical Biochemistry. 364: 92-4. PMID 17368419 DOI: 10.1016/J.Ab.2007.01.019 |
0.363 |
|
2006 |
Vega CA, Kurt N, Chen Z, Rüdiger S, Cavagnero S. Binding specificity of an alpha-helical protein sequence to a full-length Hsp70 chaperone and its minimal substrate-binding domain. Biochemistry. 45: 13835-46. PMID 17105202 DOI: 10.1021/Bi061432A |
0.36 |
|
2006 |
Chen Z, Kurt N, Rajagopalan S, Cavagnero S. Secondary structure mapping of DnaK-bound protein fragments: chain helicity and local helix unwinding at the binding site. Biochemistry. 45: 12325-33. PMID 17014085 DOI: 10.1021/Bi0612263 |
0.672 |
|
2006 |
Jungbauer LM, Cavagnero S. Characterization of protein expression and folding in cell-free systems by maldi-tof mass spectrometry. Analytical Chemistry. 78: 2841-52. PMID 16615801 DOI: 10.1021/Ac052247Q |
0.79 |
|
2006 |
Ellison PA, Cavagnero S. Role of unfolded state heterogeneity and en-route ruggedness in protein folding kinetics. Protein Science : a Publication of the Protein Society. 15: 564-82. PMID 16501227 DOI: 10.1110/Ps.051758206 |
0.468 |
|
2006 |
Jungbauer LM, Bakke CK, Cavagnero S. Experimental and computational analysis of translation products in apomyoglobin expression. Journal of Molecular Biology. 357: 1121-43. PMID 16483602 DOI: 10.1016/J.Jmb.2006.01.012 |
0.787 |
|
2006 |
Kurt N, Rajagopalan S, Cavagnero S. Effect of hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chain. Journal of Molecular Biology. 355: 809-20. PMID 16309705 DOI: 10.1016/J.Jmb.2005.10.029 |
0.705 |
|
2006 |
Chow C, Kurt N, Murphy RM, Cavagnero S. Structural characterization of apomyoglobin self-associated species in aqueous buffer and urea solution. Biophysical Journal. 90: 298-309. PMID 16214860 DOI: 10.1529/Biophysj.105.070227 |
0.448 |
|
2006 |
Bakke CK, Jungbauer LM, Cavagnero S. In vitro expression and characterization of native apomyoglobin under low molecular crowding conditions. Protein Expression and Purification. 45: 381-92. PMID 16169747 DOI: 10.1016/J.Pep.2005.08.001 |
0.799 |
|
2005 |
Kurt N, Cavagnero S. The burial of solvent-accessible surface area is a predictor of polypeptide folding and misfolding as a function of chain elongation. Journal of the American Chemical Society. 127: 15690-1. PMID 16277496 DOI: 10.1021/Ja0560682 |
0.426 |
|
2005 |
Cavagnero S, Jungbauer LM. Painting protein misfolding in the cell in real time with an atomic-scale brush. Trends in Biotechnology. 23: 157-62. PMID 15734559 DOI: 10.1016/J.Tibtech.2005.01.008 |
0.788 |
|
2004 |
Rajagopalan S, Chow C, Raghunathan V, Fry CG, Cavagnero S. NMR spectroscopic filtration of polypeptides and proteins in complex mixtures. Journal of Biomolecular Nmr. 29: 505-16. PMID 15243181 DOI: 10.1023/B:Jnmr.0000034354.30702.De |
0.66 |
|
2003 |
Chow CC, Chow C, Raghunathan V, Huppert TJ, Kimball EB, Cavagnero S. Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices. Biochemistry. 42: 7090-9. PMID 12795605 DOI: 10.1021/Bi0273056 |
0.467 |
|
2003 |
Cavagnero S. Using NMR to determine protein structure in solution Journal of Chemical Education. 80: 125-127. DOI: 10.1021/Ed080P125 |
0.358 |
|
2001 |
Cavagnero S, Nishimura C, Schwarzinger S, Dyson HJ, Wright PE. Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway. Biochemistry. 40: 14459-67. PMID 11724558 DOI: 10.1021/Bi011500N |
0.332 |
|
1999 |
Cavagnero S, Dyson HJ, Wright PE. Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin. Journal of Molecular Biology. 285: 269-82. PMID 9878405 DOI: 10.1006/Jmbi.1998.2273 |
0.359 |
|
1998 |
Cavagnero S, Zhou ZH, Adams MW, Chan SI. Unfolding mechanism of rubredoxin from Pyrococcus furiosus. Biochemistry. 37: 3377-85. PMID 9521658 DOI: 10.1021/Bi9721804 |
0.576 |
|
1998 |
Cavagnero S, Debe DA, Zhou ZH, Adams MW, Chan SI. Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins. Biochemistry. 37: 3369-76. PMID 9521657 DOI: 10.1021/Bi9721795 |
0.773 |
|
1995 |
Cavagnero S, Zhou ZH, Adams MW, Chan SI. Response of rubredoxin from Pyrococcus furiosus to environmental changes: implications for the origin of hyperthermostability. Biochemistry. 34: 9865-73. PMID 7632687 DOI: 10.1021/Bi00031A007 |
0.511 |
|
Show low-probability matches. |