| Year |
Citation |
Score |
| 2023 |
Marszalek J, De Los Rios P, Cyr D, Mayer MP, Adupa V, Andréasson C, Blatch GL, Braun JEA, Brodsky JL, Bukau B, Chapple JP, Conz C, Dementin S, Genevaux P, Genest O, ... ... Hines JK, et al. J-domain proteins: From molecular mechanisms to diseases. Cell Stress & Chaperones. 29: 21-33. PMID 38320449 DOI: 10.1016/j.cstres.2023.12.002 |
0.319 |
|
| 2022 |
Tak Y, Lal SS, Gopan S, Balakrishnan M, Satheesh G, Biswal AK, Verma AK, Cole SJ, Brown RE, Hayward RE, Hines JK, Sahi C. Identification of subfunctionalized aggregate-remodeling J-domain proteins in Arabidopsis thaliana. Journal of Experimental Botany. PMID 36576197 DOI: 10.1093/jxb/erac514 |
0.331 |
|
| 2022 |
Miller SC, Wegrzynowicz AK, Cole SJ, Hayward RE, Ganser SJ, Hines JK. Hsp40/JDP Requirements for the Propagation of Synthetic Yeast Prions. Viruses. 14. PMID 36298715 DOI: 10.3390/v14102160 |
0.433 |
|
| 2019 |
Verma AK, Tamadaddi C, Tak Y, Lal SS, Cole SJ, Hines JK, Sahi C. The expanding world of plant J-domain proteins. Critical Reviews in Plant Sciences. 38: 382-400. PMID 33223602 DOI: 10.1080/07352689.2019.1693716 |
0.368 |
|
| 2019 |
Berger SE, Nolte AM, Kamiya E, Hines JK. Three J-proteins impact Hsp104-mediated variant-specific prion elimination: a new critical role for a low-complexity domain. Current Genetics. PMID 31230108 DOI: 10.1007/S00294-019-01006-5 |
0.513 |
|
| 2019 |
Killian AN, Miller SC, Hines JK. Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast. Viruses. 11. PMID 30995727 DOI: 10.3390/V11040349 |
0.453 |
|
| 2018 |
Bui Q, Sherma J, Hines JK. Using High Performance Thin Layer Chromatography-Densitometry to Study the Influence of the Prion [] and Its Determinant Prion Protein Rnq1 on Yeast Lipid Profiles. Separations. 5. PMID 30003084 DOI: 10.3390/Separations5010006 |
0.314 |
|
| 2018 |
Astor MT, Kamiya E, Sporn ZA, Berger SE, Hines JK. Variant-specific and reciprocal Hsp40 functions in Hsp104-mediated prion elimination. Molecular Microbiology. PMID 29633387 DOI: 10.1111/Mmi.13966 |
0.477 |
|
| 2018 |
Killian AN, Hines JK. Chaperone functional specificity promotes yeast prion diversity. Plos Pathogens. 14: e1006695. PMID 29300791 DOI: 10.1371/Journal.Ppat.1006695 |
0.382 |
|
| 2017 |
Schilke BA, Ciesielski SJ, Ziegelhoffer T, Kamiya E, Tonelli M, Lee W, Cornilescu G, Hines JK, Markley JL, Craig EA. Broadening the functionality of a J-protein/Hsp70 molecular chaperone system. Plos Genetics. 13: e1007084. PMID 29084221 DOI: 10.1371/Journal.Pgen.1007084 |
0.504 |
|
| 2017 |
Oliver EE, Troisi EM, Hines JK. Prion-specific Hsp40 Function: The Role of the Auxilin Homolog Swa2. Prion. 0. PMID 28574745 DOI: 10.1080/19336896.2017.1331810 |
0.519 |
|
| 2017 |
Verma AK, Diwan D, Raut S, Dobriyal N, Brown RE, Gowda V, Hines JK, Sahi C. Evolutionary Conservation and Emerging Functional Diversity of the Cytosolic Hsp70:J Protein Chaperone Network of Arabidopsis thaliana. G3 (Bethesda, Md.). PMID 28450372 DOI: 10.1534/G3.117.042291 |
0.434 |
|
| 2017 |
Butler MW, Bociulis SC, Little AR, Minnick JA, Ritter NJ, Rockman ME, Rossi ML, Hines JK. Quantifying biliverdin in liver and spleen samples from multiple avian species The Auk. 134: 11-21. DOI: 10.1642/Auk-16-73.1 |
0.636 |
|
| 2016 |
Bui Q, Sherma J, Fried B, Hines JK. Determination of Growth-Phase Dependent Influences Exerted by Prions on Yeast Lipid Content Using HPTLC-Densitometry. Acta Chromatographica. 28: 373-385. PMID 27974871 DOI: 10.1556/1326.2016.28.3.7 |
0.328 |
|
| 2015 |
Troisi EM, Rockman ME, Nguyen PP, Oliver EE, Hines JK. Swa2, the yeast homolog of mammalian auxilin, is specifically required for the propagation of the prion variant [URE3-1]. Molecular Microbiology. PMID 26031938 DOI: 10.1111/Mmi.13076 |
0.691 |
|
| 2015 |
Sporn ZA, Hines JK. Hsp40 function in yeast prion propagation: Amyloid diversity necessitates chaperone functional complexity. Prion. 9: 80-9. PMID 25738774 DOI: 10.1080/19336896.2015.1020268 |
0.469 |
|
| 2014 |
Harris JM, Nguyen PP, Patel MJ, Sporn ZA, Hines JK. Functional diversification of hsp40: distinct j-protein functional requirements for two prions allow for chaperone-dependent prion selection. Plos Genetics. 10: e1004510. PMID 25058638 DOI: 10.1371/Journal.Pgen.1004510 |
0.496 |
|
| 2014 |
Hines J, Harris J, Nguyen P, Sporn Z, Patel M. Chaperone-dependent prion selection: prion-specific bifunctionality in the J-protein Sis1 (567.3) The Faseb Journal. 28. DOI: 10.1096/Fasebj.28.1_Supplement.567.3 |
0.448 |
|
| 2014 |
Rockman M, Troisi E, Hines J. Ectopic expression studies of the J‐protein Swa2 and its potential role in yeast prion propagation (567.2) The Faseb Journal. 28. DOI: 10.1096/Fasebj.28.1_Supplement.567.2 |
0.684 |
|
| 2011 |
Hines JK, Higurashi T, Srinivasan M, Craig EA. Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion. 5: 238-44. PMID 22156732 DOI: 10.4161/Pri.17818 |
0.361 |
|
| 2011 |
Hines JK, Craig EA. The sensitive [SWI (+)] prion: new perspectives on yeast prion diversity. Prion. 5: 164-8. PMID 21811098 DOI: 10.4161/Pri.5.3.16895 |
0.449 |
|
| 2011 |
Hines JK, Li X, Du Z, Higurashi T, Li L, Craig EA. [SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity. Plos Genetics. 7: e1001309. PMID 21379326 DOI: 10.1371/Journal.Pgen.1001309 |
0.525 |
|
| 2008 |
Higurashi T, Hines JK, Sahi C, Aron R, Craig EA. Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proceedings of the National Academy of Sciences of the United States of America. 105: 16596-601. PMID 18955697 DOI: 10.1073/Pnas.0808934105 |
0.514 |
|
| 2007 |
Hines JK, Chen X, Nix JC, Fromm HJ, Honzatko RB. Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition. The Journal of Biological Chemistry. 282: 36121-31. PMID 17933867 DOI: 10.1074/Jbc.M707302200 |
0.569 |
|
| 2007 |
Hines JK, Kruesel CE, Fromm HJ, Honzatko RB. Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch. The Journal of Biological Chemistry. 282: 24697-706. PMID 17567577 DOI: 10.1074/Jbc.M703580200 |
0.589 |
|
| 2007 |
Hines JK, Fromm HJ, Honzatko RB. Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state. The Journal of Biological Chemistry. 282: 11696-704. PMID 17314096 DOI: 10.1074/Jbc.M611104200 |
0.595 |
|
| 2006 |
Hines JK, Fromm HJ, Honzatko RB. Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase. The Journal of Biological Chemistry. 281: 18386-93. PMID 16670087 DOI: 10.1074/Jbc.M602553200 |
0.59 |
|
| Show low-probability matches. |