| Year |
Citation |
Score |
| 2023 |
Eicher J, Hutcheson BO, Pielak GJ. Properties of a tardigrade desiccation-tolerance protein aerogel. Biophysical Journal. PMID 37149732 DOI: 10.1016/j.bpj.2023.05.002 |
0.366 |
|
| 2023 |
Brom JA, Petrikis RG, Pielak GJ. Correction to "How Sugars Protect Dry Protein Structure". Biochemistry. 62: 1330. PMID 36913527 DOI: 10.1021/acs.biochem.3c00107 |
0.327 |
|
| 2023 |
Chu IT, Hutcheson BO, Malsch HR, Pielak GJ. Macromolecular Crowding by Polyethylene Glycol Reduces Protein Breathing. The Journal of Physical Chemistry Letters. 14: 2599-2605. PMID 36881386 DOI: 10.1021/acs.jpclett.3c00271 |
0.349 |
|
| 2023 |
Brom JA, Petrikis RG, Pielak GJ. How Sugars Protect Dry Protein Structure. Biochemistry. 62: 1044-1052. PMID 36802580 DOI: 10.1021/acs.biochem.2c00692 |
0.35 |
|
| 2023 |
Stewart CJ, Olgenblum GI, Propst A, Harries D, Pielak GJ. Resolving the Enthalpy of Protein Stabilization by Macromolecular Crowding. Protein Science : a Publication of the Protein Society. e4573. PMID 36691735 DOI: 10.1002/pro.4573 |
0.769 |
|
| 2022 |
Eicher JE, Brom JA, Wang S, Sheiko SS, Atkin JM, Pielak GJ. Secondary structure and stability of a gel-forming tardigrade desiccation-tolerance protein. Protein Science : a Publication of the Protein Society. 31: e4495. PMID 36335581 DOI: 10.1002/pro.4495 |
0.396 |
|
| 2022 |
Speer SL, Stewart CJ, Sapir L, Harries D, Pielak GJ. Macromolecular Crowding Is More than Hard-Core Repulsions. Annual Review of Biophysics. 51: 267-300. PMID 35239418 DOI: 10.1146/annurev-biophys-091321-071829 |
0.756 |
|
| 2022 |
Chu IT, Stewart CJ, Speer SL, Pielak GJ. A Difference between and In-Cell Protein Dimer Formation. Biochemistry. PMID 35188746 DOI: 10.1021/acs.biochem.1c00780 |
0.756 |
|
| 2021 |
Crilly CJ, Brom JA, Warmuth O, Esterly HJ, Pielak GJ. Protection by desiccation-tolerance proteins probed at the residue level. Protein Science : a Publication of the Protein Society. PMID 34766407 DOI: 10.1002/pro.4231 |
0.354 |
|
| 2021 |
Crilly CJ, Eicher JE, Warmuth O, Atkin JM, Pielak GJ. Water's Variable Role in Protein Stability Uncovered by Liquid-Observed Vapor Exchange NMR. Biochemistry. 60: 3041-3045. PMID 34596383 DOI: 10.1021/acs.biochem.1c00552 |
0.39 |
|
| 2021 |
Speer SL, Zheng W, Jiang X, Chu IT, Guseman AJ, Liu M, Pielak GJ, Li C. The intracellular environment affects protein-protein interactions. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33836588 DOI: 10.1073/pnas.2019918118 |
0.814 |
|
| 2021 |
Gruebele M, Pielak GJ. Dynamical spectroscopy and microscopy of proteins in cells. Current Opinion in Structural Biology. 70: 1-7. PMID 33662744 DOI: 10.1016/j.sbi.2021.02.001 |
0.372 |
|
| 2021 |
Thole JF, Fadero TC, Bonin JP, Stadmiller SS, Giudice JA, Pielak GJ. Oocytes for Eukaryotic In-Cell NMR. Biochemistry. PMID 33534998 DOI: 10.1021/acs.biochem.0c00922 |
0.384 |
|
| 2021 |
Crilly CJ, Brom JA, Kowalewski ME, Piszkiewicz S, Pielak GJ. Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR. Biochemistry. PMID 33400518 DOI: 10.1021/acs.biochem.0c00863 |
0.39 |
|
| 2020 |
Stadmiller SS, Pielak GJ. Protein-complex stability in cells and in vitro under crowded conditions. Current Opinion in Structural Biology. 66: 183-192. PMID 33285342 DOI: 10.1016/j.sbi.2020.10.024 |
0.427 |
|
| 2020 |
Stadmiller SS, Aguilar JS, Parnham S, Pielak GJ. Protein-Peptide Binding Energetics under Crowded Conditions. The Journal of Physical Chemistry. B. PMID 32936642 DOI: 10.1021/Acs.Jpcb.0C05578 |
0.508 |
|
| 2020 |
Stadmiller SS, Aguilar JS, Waudby CA, Pielak GJ. Rapid Quantification of Protein-Ligand Binding via F NMR Lineshape Analysis. Biophysical Journal. PMID 32348722 DOI: 10.1016/J.Bpj.2020.03.031 |
0.408 |
|
| 2020 |
Chu IT, Speer SL, Pielak GJ. Rheostatic control of protein expression using Tuner™ cells. Biochemistry. PMID 31975578 DOI: 10.1021/Acs.Biochem.9B01101 |
0.434 |
|
| 2020 |
Lauzier FJ, Stewart CJ, Harries D, Pielak GJ, Speer SL. Polyethylene Glycol Size and Protein-Complex Stability Biophysical Journal. 118: 48a. DOI: 10.1016/J.Bpj.2019.11.443 |
0.417 |
|
| 2020 |
Crilly CJ, Noonan Brom JA, Rockcliffe DA, Pielak GJ. Liquid-Observed Vapor Exchange (LOVE) NMR Reveals Residue-Level Effects of Protectants on a Dried Protein Biophysical Journal. 118: 36a. DOI: 10.1016/J.Bpj.2019.11.379 |
0.397 |
|
| 2020 |
Stewart CJ, Speer SL, Lauzier FJ, Harries D, Pielak GJ. Polyethylene Glycol Size and Protein Stability Biophysical Journal. 118: 196a. DOI: 10.1016/J.Bpj.2019.11.1185 |
0.438 |
|
| 2019 |
Piszkiewicz S, Pielak GJ. Protecting enzymes from stress-induced inactivation. Biochemistry. PMID 31436413 DOI: 10.1021/Acs.Biochem.9B00675 |
0.317 |
|
| 2019 |
Speer SL, Guseman AJ, Patteson JB, Ehrmann BM, Pielak GJ. Controlling and quantifying protein concentration in Escherichia coli. Protein Science : a Publication of the Protein Society. PMID 31054180 DOI: 10.1002/Pro.3637 |
0.805 |
|
| 2019 |
Ye Y, Wu Q, Zheng W, Jiang B, Pielak GJ, Liu M, Li C. Positively-Charged Tags Impede Protein Mobility in Cells as Quantified by 19F NMR. The Journal of Physical Chemistry. B. PMID 31042382 DOI: 10.1021/Acs.Jpcb.9B02162 |
0.421 |
|
| 2019 |
Jiang X, Zhang Z, Cheng K, Wu Q, Jiang L, Pielak GJ, Liu M, Li C. Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. fj201802796R. PMID 30916996 DOI: 10.1096/Fj.201802796R |
0.356 |
|
| 2019 |
Piszkiewicz S, Gunn KH, Warmuth O, Propst A, Mehta A, Nguyen KH, Kuhlman E, Guseman AJ, Stadmiller SS, Boothby TC, Neher SB, Pielak GJ. Protecting activity of desiccated enzymes. Protein Science : a Publication of the Protein Society. PMID 30868674 DOI: 10.1002/Pro.3604 |
0.79 |
|
| 2019 |
Speer SL, Guseman AJ, Pielak GJ. Quantifying a Protein-Protein Interaction in Living Cells Biophysical Journal. 116: 61a. DOI: 10.1016/J.Bpj.2018.11.375 |
0.818 |
|
| 2019 |
Piszkiewicz S, Gunn KH, Speer SL, Warmuth O, Mehta A, Lauzier FJ, Nguyen KH, Kuhlman E, Neher SB, Pielak GJ. Tardigrade Intrinsically Disordered Proteins Protect Enzymes from Desiccation-Induced Inactivation Biophysical Journal. 116: 452a-453a. DOI: 10.1016/J.Bpj.2018.11.2443 |
0.35 |
|
| 2018 |
Cheng K, Wu Q, Zhang Z, Pielak GJ, Liu M, Li C. Crowding and confinement can oppositely affect protein stability. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 30358053 DOI: 10.1002/Cphc.201800857 |
0.522 |
|
| 2018 |
Stadmiller SS, Pielak GJ. The Expanding Zoo of In-Cell Protein NMR. Biophysical Journal. PMID 30314656 DOI: 10.1016/J.Bpj.2018.09.017 |
0.492 |
|
| 2018 |
Guseman AJ, Perez Goncalves GM, Speer SL, Young GB, Pielak GJ. Protein shape modulates crowding effects. Proceedings of the National Academy of Sciences of the United States of America. PMID 30301792 DOI: 10.1073/Pnas.1810054115 |
0.813 |
|
| 2018 |
Stadmiller SS, Pielak GJ. Enthalpic stabilization of an SH3 domain by D O. Protein Science : a Publication of the Protein Society. PMID 30052291 DOI: 10.1002/Pro.3477 |
0.383 |
|
| 2018 |
Rydeen AE, Brustad EM, Pielak GJ. Osmolytes and protein-protein interactions. Journal of the American Chemical Society. PMID 29842777 DOI: 10.1021/Jacs.8B03903 |
0.525 |
|
| 2018 |
Guseman AJ, Speer SL, Perez Goncalves GM, Pielak GJ. Surface-charge modulates protein-protein interactions in physiologically-relevant environments. Biochemistry. PMID 29473738 DOI: 10.1021/Acs.Biochem.8B00061 |
0.81 |
|
| 2017 |
Ye Y, Wu Q, Zheng W, Jiang B, Pielak GJ, Liu M, Li C. Quantification of size effect on protein rotational mobility in cells by 19F NMR spectroscopy. Analytical and Bioanalytical Chemistry. PMID 29184995 DOI: 10.1007/S00216-017-0745-4 |
0.511 |
|
| 2017 |
Acosta LC, Perez Goncalves GM, Pielak GJ, Gorensek-Benitez AH. Large cosolutes, small cosolutes and dihydrofolate reductase activity. Protein Science : a Publication of the Protein Society. PMID 28971539 DOI: 10.1002/Pro.3316 |
0.774 |
|
| 2017 |
Boothby TC, Pielak GJ. Intrinsically Disordered Proteins and Desiccation Tolerance: Elucidating Functional and Mechanistic Underpinnings of Anhydrobiosis. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. PMID 28901557 DOI: 10.1002/Bies.201700119 |
0.436 |
|
| 2017 |
Gorensek-Benitez AH, Smith AE, Stadmiller SS, Perez Goncalves GM, Pielak GJ. Cosolutes, Crowding and Protein Folding Kinetics. The Journal of Physical Chemistry. B. PMID 28605189 DOI: 10.1021/Acs.Jpcb.7B03786 |
0.84 |
|
| 2017 |
Cohen RD, Pielak GJ. Protein quinary interactions with an unfolded state ensemble. Protein Science : a Publication of the Protein Society. PMID 28571108 DOI: 10.1002/Pro.3206 |
0.437 |
|
| 2017 |
Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. Molecular Cell. 65: 975-984.e5. PMID 28306513 DOI: 10.1016/J.Cryobiol.2018.10.077 |
0.319 |
|
| 2017 |
Li C, Zhao J, Cheng K, Ge Y, Wu Q, Ye Y, Xu G, Zhang Z, Zheng W, Zhang X, Zhou X, Pielak G, Liu M. Magnetic Resonance Spectroscopy As a Tool for Assessing Macromolecular Structure and Function in Living Cells. Annual Review of Analytical Chemistry (Palo Alto, Calif.). PMID 28301750 DOI: 10.1146/Annurev-Anchem-061516-045237 |
0.397 |
|
| 2017 |
Stadmiller SS, Gorensek-Benitez AH, Guseman AJ, Pielak GJ. Osmotic-shock induced protein destabilization in living cells and its reversal by glycine betaine. Journal of Molecular Biology. PMID 28263768 DOI: 10.1016/J.Jmb.2017.03.001 |
0.833 |
|
| 2017 |
Guseman AJ, Pielak GJ. Cosolute and Crowding Effects on a Side-By-Side Protein Dimer. Biochemistry. PMID 28102665 DOI: 10.1021/Acs.Biochem.6B01251 |
0.83 |
|
| 2017 |
Stadmiller SS, Pielak GJ. Glycine Betaine Reverses Osmotic Shock Induced Protein Destabilization in Living Cells Biophysical Journal. 112: 57a. DOI: 10.1016/J.Bpj.2016.11.345 |
0.522 |
|
| 2017 |
Piszkiewicz S, Mehta A, Boothby TC, Daniel W, Sheiko S, Goldstein B, Pielak GJ. Tardigrade Intrinsically Disordered Proteins as Potential Excipients for Biologics Biophysical Journal. 112: 512a. DOI: 10.1016/J.Bpj.2016.11.2766 |
0.387 |
|
| 2016 |
Zhai Z, Wu Q, Zheng W, Liu M, Pielak GJ, Li C. Roles of structural plasticity in chaperone HdeA activity are revealed by F NMR. Chemical Science. 7: 2222-2228. PMID 29910910 DOI: 10.1039/C5Sc04297F |
0.37 |
|
| 2016 |
Cohen RD, Pielak GJ. A cell is more than the sum of its (dilute) parts: A brief history of quinary structure. Protein Science : a Publication of the Protein Society. PMID 27977883 DOI: 10.1002/Pro.3092 |
0.46 |
|
| 2016 |
Li C, Bai J, Liu M, Pielak G. Macromolecular and small molecular crowding have similar effects on α-synuclein structure. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 27860069 DOI: 10.1002/Cphc.201601097 |
0.48 |
|
| 2016 |
Cohen R, Pielak GJ. Electrostatic contributions to protein quinary structure. Journal of the American Chemical Society. PMID 27676610 DOI: 10.1021/Jacs.6B07323 |
0.517 |
|
| 2016 |
Senske M, Smith AE, Pielak GJ. Protein Stability in Reverse Micelles. Angewandte Chemie (International Ed. in English). PMID 26854977 DOI: 10.1002/Anie.201508981 |
0.43 |
|
| 2016 |
Smith AE, Zhou LZ, Gorensek AH, Senske M, Pielak GJ. In-cell thermodynamics and a new role for protein surfaces. Proceedings of the National Academy of Sciences of the United States of America. PMID 26755596 DOI: 10.1073/Pnas.1518620113 |
0.539 |
|
| 2016 |
Piszkiewicz S, Mehta A, Boothby T, Goldstein B, Pielak G. Biophysics of Tardigrade Survival Biophysical Journal. 110: 401a. DOI: 10.1016/J.Bpj.2015.11.2166 |
0.376 |
|
| 2016 |
Guseman AJ, Lanier ST, Pielak GJ. Crowding and Protein Dimerization Biophysical Journal. 110: 213a. DOI: 10.1016/J.Bpj.2015.11.1184 |
0.827 |
|
| 2015 |
Tyrrell J, Weeks KM, Pielak GJ. Challenge of Mimicking the Influences of the Cellular Environment on RNA Structure by PEG-Induced Macromolecular Crowding. Biochemistry. 54: 6447-53. PMID 26430778 DOI: 10.1021/Acs.Biochem.5B00767 |
0.611 |
|
| 2015 |
Cohen RD, Guseman AJ, Pielak GJ. Intracellular pH modulates quinary structure. Protein Science : a Publication of the Protein Society. PMID 26257390 DOI: 10.1002/Pro.2765 |
0.797 |
|
| 2015 |
Monteith WB, Cohen RD, Smith AE, Guzman-Cisneros E, Pielak GJ. Quinary structure modulates protein stability in cells. Proceedings of the National Academy of Sciences of the United States of America. 112: 1739-42. PMID 25624496 DOI: 10.1073/Pnas.1417415112 |
0.847 |
|
| 2015 |
Smith AE, Zhou LZ, Pielak GJ. Hydrogen exchange of disordered proteins in Escherichia coli. Protein Science : a Publication of the Protein Society. 24: 706-13. PMID 25611326 DOI: 10.1002/Pro.2643 |
0.41 |
|
| 2015 |
Smith AE, Zhang Z, Pielak GJ, Li C. NMR studies of protein folding and binding in cells and cell-like environments. Current Opinion in Structural Biology. 30: 7-16. PMID 25479354 DOI: 10.1016/J.Sbi.2014.10.004 |
0.515 |
|
| 2014 |
Monteith WB, Pielak GJ. Residue level quantification of protein stability in living cells. Proceedings of the National Academy of Sciences of the United States of America. 111: 11335-40. PMID 25049396 DOI: 10.1073/Pnas.1406845111 |
0.842 |
|
| 2014 |
Sarkar M, Pielak GJ. An osmolyte mitigates the destabilizing effect of protein crowding. Protein Science : a Publication of the Protein Society. 23: 1161-4. PMID 24963990 DOI: 10.1002/Pro.2510 |
0.465 |
|
| 2014 |
Theillet FX, Binolfi A, Frembgen-Kesner T, Hingorani K, Sarkar M, Kyne C, Li C, Crowley PB, Gierasch L, Pielak GJ, Elcock AH, Gershenson A, Selenko P. Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chemical Reviews. 114: 6661-714. PMID 24901537 DOI: 10.1021/Cr400695P |
0.408 |
|
| 2014 |
Xu G, Ye Y, Liu X, Cao S, Wu Q, Cheng K, Liu M, Pielak GJ, Li C. Strategies for protein NMR in Escherichia coli. Biochemistry. 53: 1971-81. PMID 24597855 DOI: 10.1021/Bi500079U |
0.485 |
|
| 2014 |
Sarkar M, Lu J, Pielak GJ. Protein crowder charge and protein stability. Biochemistry. 53: 1601-6. PMID 24552162 DOI: 10.1021/Bi4016346 |
0.477 |
|
| 2014 |
Pielak GJ. 1SDP-01 Intermolecular Quinary Interactions Modulate Protein Stability in Living Cells(1SDP Protein Dynamics and Function in Cells elucidated by in-cell NMR and High Performance Computing,Symposium,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) Seibutsu Butsuri. 54: S123. DOI: 10.2142/biophys.54.S123_2 |
0.358 |
|
| 2014 |
Monteith WB, Pielak GJ. Protein Stability in Living Cells Biophysical Journal. 106: 736a. DOI: 10.1016/J.Bpj.2013.11.4058 |
0.831 |
|
| 2013 |
Sarkar M, Li C, Pielak GJ. Soft interactions and crowding. Biophysical Reviews. 5: 187-194. PMID 28510157 DOI: 10.1007/S12551-013-0104-4 |
0.401 |
|
| 2013 |
Sarkar M, Smith AE, Pielak GJ. Impact of reconstituted cytosol on protein stability. Proceedings of the National Academy of Sciences of the United States of America. 110: 19342-7. PMID 24218610 DOI: 10.1073/Pnas.1312678110 |
0.517 |
|
| 2013 |
Tyrrell J, McGinnis JL, Weeks KM, Pielak GJ. The cellular environment stabilizes adenine riboswitch RNA structure. Biochemistry. 52: 8777-85. PMID 24215455 DOI: 10.1021/Bi401207Q |
0.607 |
|
| 2013 |
Ye Y, Liu X, Zhang Z, Wu Q, Jiang B, Jiang L, Zhang X, Liu M, Pielak GJ, Li C. (19) F NMR spectroscopy as a probe of cytoplasmic viscosity and weak protein interactions in living cells. Chemistry (Weinheim An Der Bergstrasse, Germany). 19: 12705-10. PMID 23922149 DOI: 10.1002/Chem.201301657 |
0.534 |
|
| 2013 |
Smith AE, Sarkar M, Young GB, Pielak GJ. Amide proton exchange of a dynamic loop in cell extracts. Protein Science : a Publication of the Protein Society. 22: 1313-9. PMID 23904228 DOI: 10.1002/Pro.2318 |
0.421 |
|
| 2012 |
Wang Y, Benton LA, Singh V, Pielak GJ. Disordered Protein Diffusion under Crowded Conditions. The Journal of Physical Chemistry Letters. 3: 2703-2706. PMID 23185649 DOI: 10.1021/Jz3010915 |
0.668 |
|
| 2012 |
Benton LA, Smith AE, Young GB, Pielak GJ. Unexpected effects of macromolecular crowding on protein stability. Biochemistry. 51: 9773-5. PMID 23167542 DOI: 10.1021/Bi300909Q |
0.452 |
|
| 2012 |
Wang Y, Sarkar M, Smith AE, Krois AS, Pielak GJ. Macromolecular crowding and protein stability. Journal of the American Chemical Society. 134: 16614-8. PMID 22954326 DOI: 10.1021/Ja305300M |
0.73 |
|
| 2012 |
Pielak GJ, Tian F. Membrane proteins, magic-angle spinning, and in-cell NMR. Proceedings of the National Academy of Sciences of the United States of America. 109: 4715-6. PMID 22411816 DOI: 10.1073/Pnas.1201502109 |
0.452 |
|
| 2012 |
Zigoneanu IG, Pielak GJ. Interaction of α-synuclein and a cell penetrating fusion peptide with higher eukaryotic cell membranes assessed by ¹⁹F NMR. Molecular Pharmaceutics. 9: 1024-9. PMID 22376087 DOI: 10.1021/Mp200615M |
0.807 |
|
| 2012 |
Zigoneanu IG, Yang YJ, Krois AS, Haque E, Pielak GJ. Interaction of α-synuclein with vesicles that mimic mitochondrial membranes. Biochimica Et Biophysica Acta. 1818: 512-9. PMID 22155643 DOI: 10.1016/J.Bbamem.2011.11.024 |
0.805 |
|
| 2012 |
Sarkar M, Monteith WB, Wang Y, Pielak GJ. Protein Stability and Macromolecular Crowding Biophysical Journal. 102: 55a. DOI: 10.1016/J.Bpj.2011.11.329 |
0.84 |
|
| 2012 |
Tyrrell J, Weeks KM, Pielak GJ. RNA Biophysics in Living Cells using Shape Chemistry Biophysical Journal. 102: 279a. DOI: 10.1016/J.Bpj.2011.11.1543 |
0.594 |
|
| 2012 |
Pielak G. Understanding Protein & RNA Biophysics in Cells Biophysical Journal. 102: 4a. DOI: 10.1016/J.Bpj.2011.11.035 |
0.414 |
|
| 2011 |
Fu R, Wang X, Li C, Santiago-Miranda AN, Pielak GJ, Tian F. In situ structural characterization of a recombinant protein in native Escherichia coli membranes with solid-state magic-angle-spinning NMR. Journal of the American Chemical Society. 133: 12370-3. PMID 21774553 DOI: 10.1021/Ja204062V |
0.395 |
|
| 2011 |
Miklos AC, Li C, Sorrell CD, Lyon LA, Pielak GJ. An upper limit for macromolecular crowding effects. Bmc Biophysics. 4: 13. PMID 21627822 DOI: 10.1186/2046-1682-4-13 |
0.834 |
|
| 2011 |
Schlesinger AP, Wang Y, Tadeo X, Millet O, Pielak GJ. Macromolecular crowding fails to fold a globular protein in cells. Journal of the American Chemical Society. 133: 8082-5. PMID 21534566 DOI: 10.1021/Ja201206T |
0.85 |
|
| 2011 |
Miklos AC, Sarkar M, Wang Y, Pielak GJ. Protein crowding tunes protein stability. Journal of the American Chemical Society. 133: 7116-20. PMID 21506571 DOI: 10.1021/Ja200067P |
0.845 |
|
| 2011 |
Barnes CO, Monteith WB, Pielak GJ. Internal and global protein motion assessed with a fusion construct and in-cell NMR spectroscopy. Chembiochem : a European Journal of Chemical Biology. 12: 390-1. PMID 21290539 DOI: 10.1002/Cbic.201000610 |
0.801 |
|
| 2011 |
Barnes CO, Pielak GJ. In-cell protein NMR and protein leakage. Proteins. 79: 347-51. PMID 21120863 DOI: 10.1002/Prot.22906 |
0.53 |
|
| 2010 |
Pielak GJ, Miklos AC. Crowding and function reunite. Proceedings of the National Academy of Sciences of the United States of America. 107: 17457-8. PMID 20926746 DOI: 10.1073/Pnas.1013095107 |
0.791 |
|
| 2010 |
Wang GF, Li C, Pielak GJ. Probing the micelle-bound aggregation-prone state of α-synuclein with (19)F NMR spectroscopy. Chembiochem : a European Journal of Chemical Biology. 11: 1993-6. PMID 20730847 DOI: 10.1002/Cbic.201000405 |
0.421 |
|
| 2010 |
Miklos AC, Li C, Sharaf NG, Pielak GJ. Volume exclusion and soft interaction effects on protein stability under crowded conditions. Biochemistry. 49: 6984-91. PMID 20672856 DOI: 10.1021/Bi100727Y |
0.843 |
|
| 2010 |
Wang GF, Li C, Pielak GJ. 19F NMR studies of α-synuclein-membrane interactions. Protein Science : a Publication of the Protein Society. 19: 1686-91. PMID 20629174 DOI: 10.1002/Pro.449 |
0.323 |
|
| 2010 |
Wang Y, Li C, Pielak GJ. Effects of proteins on protein diffusion. Journal of the American Chemical Society. 132: 9392-7. PMID 20560582 DOI: 10.1021/Ja102296K |
0.691 |
|
| 2010 |
Li C, Wang GF, Wang Y, Creager-Allen R, Lutz EA, Scronce H, Slade KM, Ruf RA, Mehl RA, Pielak GJ. Protein (19)F NMR in Escherichia coli. Journal of the American Chemical Society. 132: 321-7. PMID 20050707 DOI: 10.1021/Ja907966N |
0.819 |
|
| 2010 |
Sharaf NG, Barnes CO, Charlton LM, Young GB, Pielak GJ. A bioreactor for in-cell protein NMR. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 202: 140-6. PMID 19910228 DOI: 10.1016/J.Jmr.2009.10.008 |
0.81 |
|
| 2010 |
Pielak G, Wang Y, Li C. Protein Diffusion and Macromolecular Crowding Biophysical Journal. 98: 4a. DOI: 10.1016/J.Bpj.2009.12.028 |
0.7 |
|
| 2009 |
Miklos AC, Li C, Pielak GJ. Using NMR-detected backbone amide 1H exchange to assess macromolecular crowding effects on globular-protein stability. Methods in Enzymology. 466: 1-18. PMID 21609855 DOI: 10.1016/S0076-6879(09)66001-8 |
0.839 |
|
| 2009 |
Li C, Wang Y, Pielak GJ. Translational and rotational diffusion of a small globular protein under crowded conditions. The Journal of Physical Chemistry. B. 113: 13390-2. PMID 19791823 DOI: 10.1021/Jp907744M |
0.662 |
|
| 2009 |
Li C, Lutz EA, Slade KM, Ruf RA, Wang GF, Pielak GJ. 19F NMR studies of alpha-synuclein conformation and fibrillation. Biochemistry. 48: 8578-84. PMID 19655784 DOI: 10.1021/Bi900872P |
0.802 |
|
| 2009 |
Slade KM, Baker R, Chua M, Thompson NL, Pielak GJ. Effects of recombinant protein expression on green fluorescent protein diffusion in Escherichia coli. Biochemistry. 48: 5083-9. PMID 19413350 DOI: 10.1021/Bi9004107 |
0.81 |
|
| 2009 |
Slade KM, Steele BL, Pielak GJ, Thompson NL. Quantifying green fluorescent protein diffusion in Escherichia coli by using continuous photobleaching with evanescent illumination. The Journal of Physical Chemistry. B. 113: 4837-45. PMID 19296673 DOI: 10.1021/Jp810642D |
0.754 |
|
| 2009 |
Li C, Pielak GJ. Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions. Journal of the American Chemical Society. 131: 1368-9. PMID 19140727 DOI: 10.1021/Ja808428D |
0.413 |
|
| 2009 |
Pielak GJ, Li C, Miklos AC, Schlesinger AP, Slade KM, Wang GF, Zigoneanu IG. Protein nuclear magnetic resonance under physiological conditions. Biochemistry. 48: 226-34. PMID 19113834 DOI: 10.1021/Bi8018948 |
0.812 |
|
| 2009 |
Li C, Wang Y, Pielak GJ. Erratum: Translational and rotational diffusion of a small globular protein under crowded conditions (Journal of Physical Chemistry B (2009) 113 (13390)) Journal of Physical Chemistry B. 113. DOI: 10.1021/Jp909360E |
0.639 |
|
| 2009 |
Pielak GJ, Li C, Miklos AC, Schlesinger AP, Slade KM, Wang GF, Zigoneanu IG. Protein nuclear magnetic resonance under physiological conditions (Biochemistry (2009) 48, (226) DOI: 10.1021/bi8018948)) Biochemistry. 48: 9170. DOI: 10.1021/Bi9014715 |
0.773 |
|
| 2008 |
Ruf RA, Lutz EA, Zigoneanu IG, Pielak GJ. Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation. Biochemistry. 47: 13604-9. PMID 19049426 DOI: 10.1016/J.Bpj.2008.12.2991 |
0.783 |
|
| 2008 |
Charlton LM, Barnes CO, Li C, Orans J, Young GB, Pielak GJ. Residue-level interrogation of macromolecular crowding effects on protein stability. Journal of the American Chemical Society. 130: 6826-30. PMID 18459780 DOI: 10.1021/Ja8005995 |
0.845 |
|
| 2008 |
Li C, Charlton LM, Lakkavaram A, Seagle C, Wang G, Young GB, Macdonald JM, Pielak GJ. Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: implications for in-cell NMR spectroscopy. Journal of the American Chemical Society. 130: 6310-1. PMID 18419123 DOI: 10.1021/Ja801020Z |
0.824 |
|
| 2007 |
Winzor DJ, Patel CN, Pielak GJ. Reconsideration of sedimentation equilibrium distributions reflecting the effects of small inert cosolutes on the dimerization of alpha-chymotrypsin. Biophysical Chemistry. 130: 89-92. PMID 17716806 DOI: 10.1016/J.Bpc.2007.07.006 |
0.569 |
|
| 2006 |
Bryant JE, Lecomte JT, Lee AL, Young GB, Pielak GJ. Cytosol has a small effect on protein backbone dynamics. Biochemistry. 45: 10085-91. PMID 16906766 DOI: 10.1021/Bi060547B |
0.659 |
|
| 2006 |
Charlton LM, Pielak GJ. Peeking into living eukaryotic cells with high-resolution NMR. Proceedings of the National Academy of Sciences of the United States of America. 103: 11817-8. PMID 16880379 DOI: 10.1073/Pnas.0605297103 |
0.787 |
|
| 2006 |
Pielak GJ. Woes of proline: a cautionary kinetic tale. Protein Science : a Publication of the Protein Society. 15: 393-4. PMID 16501220 DOI: 10.1110/Ps.052051106 |
0.395 |
|
| 2006 |
McNulty BC, Tripathy A, Young GB, Charlton LM, Orans J, Pielak GJ. Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein. Protein Science : a Publication of the Protein Society. 15: 602-8. PMID 16452621 DOI: 10.1110/Ps.051867106 |
0.817 |
|
| 2006 |
McNulty BC, Young GB, Pielak GJ. Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder. Journal of Molecular Biology. 355: 893-7. PMID 16343531 DOI: 10.1016/J.Jmb.2005.11.033 |
0.807 |
|
| 2005 |
Bryant JE, Lecomte JT, Lee AL, Young GB, Pielak GJ. Protein dynamics in living cells. Biochemistry. 44: 9275-9. PMID 15981993 DOI: 10.1021/Bi050786J |
0.685 |
|
| 2005 |
Pielak GJ. A model of intracellular organization. Proceedings of the National Academy of Sciences of the United States of America. 102: 5901-2. PMID 15840719 DOI: 10.1073/Pnas.0501812102 |
0.441 |
|
| 2005 |
Yi F, Sims DA, Pielak GJ, Edgell MH. High-Throughput, precise protein stability measurements facilitated by robotics Jala - Journal of the Association For Laboratory Automation. 10: 98-101. DOI: 10.1016/J.Jala.2005.02.003 |
0.637 |
|
| 2004 |
Olteanu A, Pielak GJ. Peroxidative aggregation of alpha-synuclein requires tyrosines. Protein Science : a Publication of the Protein Society. 13: 2852-6. PMID 15459341 DOI: 10.1110/Ps.04947204 |
0.595 |
|
| 2004 |
Batchelor JD, Olteanu A, Tripathy A, Pielak GJ. Impact of protein denaturants and stabilizers on water structure. Journal of the American Chemical Society. 126: 1958-61. PMID 14971928 DOI: 10.1021/Ja039335H |
0.665 |
|
| 2003 |
Olteanu A, Patel CN, Dedmon MM, Kennedy S, Linhoff MW, Minder CM, Potts PR, Deshmukh M, Pielak GJ. Stability and apoptotic activity of recombinant human cytochrome c. Biochemical and Biophysical Research Communications. 312: 733-40. PMID 14680826 DOI: 10.1016/J.Bbrc.2003.10.182 |
0.752 |
|
| 2003 |
Yi F, Sims DA, Pielak GJ, Edgell MH. Testing hypotheses about determinants of protein structure with high-precision, high-throughput stability measurements and statistical modeling. Biochemistry. 42: 7594-603. PMID 12809516 DOI: 10.1021/Bi0340649 |
0.599 |
|
| 2003 |
Edgell MH, Sims DA, Pielak GJ, Yi F. High-precision, high-throughput stability determinations facilitated by robotics and a semiautomated titrating fluorometer. Biochemistry. 42: 7587-93. PMID 12809515 DOI: 10.1021/Bi034063G |
0.611 |
|
| 2003 |
Engstrom G, Rajagukguk R, Saunders AJ, Patel CN, Rajagukguk S, Merbitz-Zahradnik T, Xiao K, Pielak GJ, Trumpower B, Yu CA, Yu L, Durham B, Millett F. Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex. Biochemistry. 42: 2816-24. PMID 12627947 DOI: 10.1021/Bi027213G |
0.593 |
|
| 2002 |
Beasley JR, Doyle DF, Chen L, Cohen DS, Fine BR, Pielak GJ. Searching for quantitative entropy-enthalpy compensation among protein variants. Proteins. 49: 398-402. PMID 12360529 DOI: 10.1002/Prot.10189 |
0.704 |
|
| 2002 |
Dedmon MM, Patel CN, Young GB, Pielak GJ. FlgM gains structure in living cells. Proceedings of the National Academy of Sciences of the United States of America. 99: 12681-4. PMID 12271132 DOI: 10.1073/Pnas.202331299 |
0.663 |
|
| 2002 |
Patel CN, Noble SM, Weatherly GT, Tripathy A, Winzor DJ, Pielak GJ. Effects of molecular crowding by saccharides on alpha-chymotrypsin dimerization. Protein Science : a Publication of the Protein Society. 11: 997-1003. PMID 11967357 DOI: 10.1110/Ps.4450102 |
0.802 |
|
| 2002 |
Morar AS, Pielak GJ. Crowding by trisaccharides and the 2:1 cytochrome c-cytochrome c peroxidase complex. Biochemistry. 41: 547-51. PMID 11781093 DOI: 10.1021/Bi0111810 |
0.806 |
|
| 2001 |
Morar AS, Olteanu A, Young GB, Pielak GJ. Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c. Protein Science : a Publication of the Protein Society. 10: 2195-9. PMID 11604526 DOI: 10.1110/Ps.24301 |
0.8 |
|
| 2001 |
Patel CN, Lind MC, Pielak GJ. Characterization of horse cytochrome c expressed in Escherichia coli. Protein Expression and Purification. 22: 220-4. PMID 11437597 DOI: 10.1006/Prep.2001.1438 |
0.657 |
|
| 2001 |
Davis-Searles PR, Saunders AJ, Erie DA, Winzor DJ, Pielak GJ. Interpreting the effects of small uncharged solutes on protein-folding equilibria. Annual Review of Biophysics and Biomolecular Structure. 30: 271-306. PMID 11340061 DOI: 10.1146/Annurev.Biophys.30.1.271 |
0.527 |
|
| 2001 |
Weatherly GT, Pielak GJ. Second virial coefficients as a measure of protein--osmolyte interactions. Protein Science : a Publication of the Protein Society. 10: 12-6. PMID 11266589 DOI: 10.1110/Ps.29301 |
0.837 |
|
| 2001 |
Pielak GJ, Wang X. Interactions between yeast iso-1-cytochrome c and its peroxidase. Biochemistry. 40: 422-8. PMID 11148036 DOI: 10.1021/Bi002124U |
0.403 |
|
| 2001 |
Morar AS, Wang X, Pielak GJ. Effects of crowding by mono-, di-, and tetrasaccharides on cytochrome c-cytochrome c peroxidase binding: comparing experiment to theory. Biochemistry. 40: 281-5. PMID 11141081 DOI: 10.1021/Bi002296R |
0.827 |
|
| 2000 |
Saunders AJ, Davis-Searles PR, Allen DL, Pielak GJ, Erie DA. Osmolyte-induced changes in protein conformational equilibria. Biopolymers. 53: 293-307. PMID 10685050 DOI: 10.1002/(Sici)1097-0282(20000405)53:4<293::Aid-Bip2>3.0.Co;2-T |
0.496 |
|
| 1999 |
Lahr SJ, Broadwater A, Carter CW, Collier ML, Hensley L, Waldner JC, Pielak GJ, Edgell MH. Patterned library analysis: a method for the quantitative assessment of hypotheses concerning the determinants of protein structure. Proceedings of the National Academy of Sciences of the United States of America. 96: 14860-5. PMID 10611303 DOI: 10.1073/Pnas.96.26.14860 |
0.41 |
|
| 1999 |
Wang X, Pielak GJ. Equilibrium thermodynamics of a physiologically-relevant heme-protein complex. Biochemistry. 38: 16876-81. PMID 10606521 DOI: 10.1021/Bi992005I |
0.378 |
|
| 1999 |
Morar AS, Kakouras D, Young GB, Boyd J, Pielak GJ. Expression of 15N-labeled eukaryotic cytochrome c in Escherichia coli. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 4: 220-2. PMID 10499094 DOI: 10.1007/S007750050307 |
0.796 |
|
| 1999 |
Hostetter DR, Weatherly GT, Beasley JR, Bortone K, Cohen DS, Finger SA, Hardwidge P, Kakouras DS, Saunders AJ, Trojak SK, Waldner JC, Pielak GJ. Partially formed native tertiary interactions in the A-state of cytochrome c. Journal of Molecular Biology. 289: 639-44. PMID 10356334 DOI: 10.1006/Jmbi.1999.2764 |
0.815 |
|
| 1999 |
Mei H, Wang K, Peffer N, Weatherly G, Cohen DS, Miller M, Pielak G, Durham B, Millett F. Role of configurational gating in intracomplex electron transfer from cytochrome c to the radical cation in cytochrome c peroxidase Biochemistry. 38: 6846-6854. PMID 10346906 DOI: 10.1021/Bi983002T |
0.767 |
|
| 1999 |
Waldner JC, Lahr SJ, Edgell MH, Pielak GJ. Nonideality and protein thermal denaturation. Biopolymers. 49: 471-9. PMID 10193194 DOI: 10.1002/(Sici)1097-0282(199905)49:6<471::Aid-Bip5>3.0.Co;2-Z |
0.451 |
|
| 1999 |
Boyd J, Dobson CM, Morar AS, Williams RJP, Pielak GJ. 1H and 15N hyperfine shifts of cytochrome c [15] Journal of the American Chemical Society. 121: 9247-9248. DOI: 10.1021/Ja9920361 |
0.766 |
|
| 1998 |
Davis-Searles PR, Morar AS, Saunders AJ, Erie DA, Pielak GJ. Sugar-induced molten-globule model. Biochemistry. 37: 17048-53. PMID 9836600 DOI: 10.1021/Bi981364V |
0.827 |
|
| 1998 |
Waldner JC, Lahr SJ, Edgell MH, Pielak GJ. Effect of a polyhistidine terminal extension on eglin c stability. Analytical Biochemistry. 263: 116-8. PMID 9750153 DOI: 10.1006/Abio.1998.2808 |
0.325 |
|
| 1998 |
Allen DL, Pielak GJ. Baseline length and automated fitting of denaturation data. Protein Science : a Publication of the Protein Society. 7: 1262-3. PMID 9605334 DOI: 10.1002/Pro.5560070524 |
0.385 |
|
| 1998 |
Marmorino JL, Lehti M, Pielak GJ. Native tertiary structure in an A-state. Journal of Molecular Biology. 275: 379-88. PMID 9466916 DOI: 10.1006/Jmbi.1997.1450 |
0.406 |
|
| 1998 |
Wrobel JA, Chao SF, Conrad MJ, Merker JD, Swanstrom R, Pielak GJ, Hutchison CA. A genetic approach for identifying critical residues in the fingers and palm subdomains of HIV-1 reverse transcriptase. Proceedings of the National Academy of Sciences of the United States of America. 95: 638-45. PMID 9435245 DOI: 10.1073/Pnas.95.2.638 |
0.393 |
|
| 1996 |
Mei H, Wang K, McKee S, Wang X, Waldner JL, Pielak GJ, Durham B, Millett F. Control of formation and dissociation of the high-affinity complex between cytochrome c and cytochrome c peroxidase by ionic strength and the low-affinity binding site. Biochemistry. 35: 15800-6. PMID 8961943 DOI: 10.1021/Bi961487K |
0.316 |
|
| 1996 |
Wang K, Mei H, Geren L, Miller MA, Saunders A, Wang X, Waldner JL, Pielak GJ, Durham B, Millett F. Design of a ruthenium-cytochrome c derivative to measure electron transfer to the radical cation and oxyferryl heme in cytochrome c peroxidase. Biochemistry. 35: 15107-19. PMID 8942678 DOI: 10.1021/Bi9611117 |
0.304 |
|
| 1996 |
Pappa HS, Tajbaksh S, Saunders AJ, Pielak GJ, Poulos TL. Probing the cytochrome c peroxidase-cytochrome c electron transfer reaction using site specific cross-linking. Biochemistry. 35: 4837-45. PMID 8664274 DOI: 10.1021/Bi952935B |
0.321 |
|
| 1996 |
Betz SF, Marmorino JL, Saunders AJ, Doyle DF, Young GB, Pielak GJ. Unusual effects of an engineered disulfide on global and local protein stability. Biochemistry. 35: 7422-8. PMID 8652519 DOI: 10.1021/Bi9528558 |
0.785 |
|
| 1996 |
Doyle DF, Waldner JC, Parikh S, Alcazar-Roman L, Pielak GJ. Changing the transition state for protein (Un) folding. Biochemistry. 35: 7403-11. PMID 8652517 DOI: 10.1021/Bi960409U |
0.677 |
|
| 1996 |
Miller MA, Geren L, Han GW, Saunders A, Beasley J, Pielak GJ, Durham B, Millett F, Kraut J. Identifying the physiological electron transfer site of cytochrome c peroxidase by structure-based engineering. Biochemistry. 35: 667-73. PMID 8547245 DOI: 10.1021/Bi952557A |
0.306 |
|
| 1995 |
Pielak GJ, Auld DS, Beasley JR, Betz SF, Cohen DS, Doyle DF, Finger SA, Fredericks ZL, Hilgen-Willis S, Saunders AJ. Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface. Biochemistry. 34: 3268-76. PMID 7880822 DOI: 10.1021/bi00010a017 |
0.786 |
|
| 1995 |
Marmorino JL, Pielak GJ. A native tertiary interaction stabilizes the A state of cytochrome c. Biochemistry. 34: 3140-3. PMID 7880808 DOI: 10.1021/Bi00010A002 |
0.454 |
|
| 1995 |
Cohen DS, Pielak GJ. Entropic stabilization of cytochrome c upon reduction Journal of the American Chemical Society. 117: 1675-1677. DOI: 10.1021/Ja00111A001 |
0.313 |
|
| 1994 |
Cohen DS, Pielak GJ. Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature. Protein Science : a Publication of the Protein Society. 3: 1253-60. PMID 7987220 DOI: 10.1002/Pro.5560030811 |
0.314 |
|
| 1993 |
Greene RM, Betz SF, Hilgen-Willis S, Auld DS, Fencl JB, Pielak GJ. Changes in global stability and local structure of cytochrome c upon substituting phenylalanine-82 with tyrosine. Journal of Inorganic Biochemistry. 51: 663-76. PMID 8409983 DOI: 10.1016/0162-0134(93)85038-A |
0.703 |
|
| 1993 |
Hilgen-Willis S, Bowden EF, Pielak GJ. Dramatic stabilization of ferricytochrome c upon reduction. Journal of Inorganic Biochemistry. 51: 649-53. PMID 8409982 DOI: 10.1016/0162-0134(93)85036-8 |
0.428 |
|
| 1993 |
Fredericks ZL, Pielak GJ. Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix. Biochemistry. 32: 929-36. PMID 8380714 DOI: 10.1021/Bi00054A026 |
0.391 |
|
| 1993 |
Auld DS, Young GB, Saunders AJ, Doyle DF, Betz SF, Pielak GJ. Probing weakly polar interactions in cytochrome c. Protein Science : a Publication of the Protein Society. 2: 2187-97. PMID 8298464 DOI: 10.1002/Pro.5560021218 |
0.791 |
|
| 1993 |
Marmorino JL, Auld DS, Betz SF, Doyle DF, Young GB, Pielak GJ. Amide proton exchange rates of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochrome c. Protein Science : a Publication of the Protein Society. 2: 1966-74. PMID 8268806 DOI: 10.1002/Pro.5560021118 |
0.796 |
|
| 1993 |
Willis SH, Doyle DF, Auld DS, Betz SF, Fredericks ZL, Pielak GJ, Fencl JB, Bowden EF. An electrochemical probe of the denatured state Protein Engineering, Design and Selection. 6: 25a. DOI: 10.1093/Protein/6.Supplement.25A |
0.749 |
|
| 1992 |
Gao Y, McLendon G, Pielak GJ, Williams RJ. Electron-proton coupling in cytochrome c studied using protein variants. European Journal of Biochemistry / Febs. 204: 337-52. PMID 1371254 DOI: 10.1111/J.1432-1033.1992.Tb16642.X |
0.507 |
|
| 1992 |
Betz SF, Pielak GJ. Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state. Biochemistry. 31: 12337-44. PMID 1334426 DOI: 10.1021/Bi00164A007 |
0.714 |
|
| 1991 |
Gao YA, Boyd J, Pielak GJ, Williams RJ. Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts. Biochemistry. 30: 1928-34. PMID 1847077 DOI: 10.1021/Bi00221A028 |
0.484 |
|
| 1991 |
Wang XH, Pielak GJ. Temperature-sensitive variants of Saccharomyces cerevisiae iso-1-cytochrome c produced by random mutagenesis of codons 43 to 54. Journal of Molecular Biology. 221: 97-105. PMID 1656051 DOI: 10.1016/0022-2836(91)80207-B |
0.319 |
|
| 1991 |
Hildebrandt P, Pielak GJ, Williams RJ. Structural studies of yeast iso-1 cytochrome c mutants by resonance Raman spectroscopy. European Journal of Biochemistry / Febs. 201: 211-6. PMID 1655427 DOI: 10.1111/J.1432-1033.1991.Tb16276.X |
0.5 |
|
| 1991 |
Hilgen SE, Pielak GJ. The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector. Protein Engineering. 4: 575-8. PMID 1653957 DOI: 10.1093/Protein/4.5.575 |
0.337 |
|
| 1991 |
Whitford D, Gao Y, Pielak GJ, Williams RJ, McLendon GL, Sherman F. The role of the internal hydrogen bond network in first-order protein electron transfer between Saccharomyces cerevisiae iso-1-cytochrome c and bovine microsomal cytochrome b5. European Journal of Biochemistry / Febs. 200: 359-67. PMID 1653702 DOI: 10.1111/J.1432-1033.1991.Tb16193.X |
0.519 |
|
| 1991 |
Auld DS, Pielak GJ. Constraints on amino acid substitutions in the N-terminal helix of cytochrome c explored by random mutagenesis. Biochemistry. 30: 8684-90. PMID 1653604 DOI: 10.1021/Bi00099A028 |
0.355 |
|
| 1991 |
Gao Y, Boyd J, Pielak GJ, Williams RJ. Proton nuclear magnetic resonance as a probe of differences in structure between the C102T and F82S,C102T variants of iso-1-cytochrome c from the yeast Saccharomyces cerevisiae. Biochemistry. 30: 7033-40. PMID 1648968 DOI: 10.1021/Bi00242A032 |
0.521 |
|
| 1991 |
Thurgood AG, Pielak GJ, Cutler RL, Davies AM, Greenwood C, Mauk AG, Smith M, Williamson DJ, Moore GR. Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c. Febs Letters. 284: 173-7. PMID 1647980 DOI: 10.1016/0014-5793(91)80678-V |
0.627 |
|
| 1991 |
Betz SF, Garcia L, Hilgen SE, Sorrell TN, Pielak GJ. Variants of saccharomyces cerevisiae iso-1 -cytochromec c at positions 18,20, 52, 82 AND 102. Journal of Inorganic Biochemistry. 43: 317. DOI: 10.1016/0162-0134(91)84304-R |
0.642 |
|
| 1990 |
Gao Y, Boyd J, Williams RJ, Pielak GJ. Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso-1-cytochrome c and horse cytochrome c. Biochemistry. 29: 6994-7003. PMID 2171638 DOI: 10.1021/Bi00482A007 |
0.56 |
|
| 1988 |
Louie GV, Pielak GJ, Smith M, Brayer GD. Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position. Biochemistry. 27: 7870-6. PMID 2849996 DOI: 10.1021/Bi00420A043 |
0.488 |
|
| 1988 |
Pielak GJ, Atkinson RA, Boyd J, Williams RJ. Two-dimensional NMR as a probe of structural similarity applied to mutants of cytochrome c. European Journal of Biochemistry / Febs. 177: 179-85. PMID 2846295 DOI: 10.1111/J.1432-1033.1988.Tb14360.X-I2 |
0.551 |
|
| 1988 |
Pielak GJ, Boyd J, Moore GR, Williams RJ. Proton-NMR studies show that the Thr-102 mutant of yeast iso-1-cytochrome c is a typical member of the eukaryotic cytochrome c family. European Journal of Biochemistry / Febs. 177: 167-77. PMID 2846294 DOI: 10.1111/J.1432-1033.1988.Tb14359.X-I2 |
0.645 |
|
| 1988 |
Liang N, Mauk AG, Pielak GJ, Johnson JA, Smith M, Hoffman BM. Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c. Science (New York, N.Y.). 240: 311-3. PMID 2832950 DOI: 10.1126/Science.2832950 |
0.399 |
|
| 1987 |
Cutler RL, Pielak GJ, Mauk AG, Smith M. Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein. Protein Engineering. 1: 95-9. PMID 2853358 DOI: 10.1093/Protein/1.2.95 |
0.524 |
|
| 1987 |
Pielak GJ, Concar DW, Moore GR, Williams RJ. The structure of cytochrome c and its relation to recent studies of long-range electron transfer. Protein Engineering. 1: 83-8. PMID 2853357 DOI: 10.1093/Protein/1.2.83 |
0.579 |
|
| 1986 |
Pielak GJ, Gurusiddaiah S, Legg JI. Quantification of azo-coupled lysine in azo proteins by amino acid analysis. Analytical Biochemistry. 156: 403-5. PMID 3094399 DOI: 10.1016/0003-2697(86)90272-1 |
0.57 |
|
| 1986 |
Pielak GJ, Oikawa K, Mauk AG, Smith M, Kay CM. Elimination of the negative soret Cotton effect of cytochrome c by replacement of the invariant phenylalanine using site-directed mutagenesis Journal of the American Chemical Society. 108: 2724-2727. DOI: 10.1021/Ja00270A035 |
0.374 |
|
| 1985 |
Pielak GJ, Mauk AG, Smith M. Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function. Nature. 313: 152-4. PMID 2981414 DOI: 10.1038/313152A0 |
0.491 |
|
| 1984 |
Pielak GJ, Urdea MS, Legg JI. Preparation and characterization of sulfanilazo and arsanilazo proteins Biochemistry. 23: 596-603. DOI: 10.1021/Bi00299A003 |
0.664 |
|
| 1984 |
Pielak GJ, Urdea MS, Igi K, Legg JI. Azo protein analogs: synthesis and characterization of arsanilazo and sulfanilazo derivatives of tyrosine and histidine Biochemistry. 23: 589-596. DOI: 10.1021/Bi00299A002 |
0.574 |
|
| 1984 |
Pielak GJ, Urdea MS, Legg JI. Preparation and characterization of sulfanilazo and arsanilazo proteins Biochemistry. 23: 596-603. |
0.375 |
|
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