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Items: 1 to 20 of 59

1.
Mutations in the regulatory subunit of yeast acetohydroxyacid synthase affect its activation by MgATP
Yu-Ting Lee, Ronald G. Duggleby
Biochem J. 2006 Apr 15; 395(Pt 2): 331–336. Prepublished online 2006 Jan 4. Published online 2006 Mar 28. doi: 10.1042/BJ20051793
PMCID:
PMC1422763
AbstractArticlePDF–384K
2.
Structural insights into the mechanism of inhibition of AHAS by herbicides
Thierry Lonhienne, Mario D. Garcia, Gregory Pierens, Mehdi Mobli, Amanda Nouwens, Luke W. Guddat
Proc Natl Acad Sci U S A. 2018 Feb 27; 115(9): E1945–E1954. Published online 2018 Feb 13. doi: 10.1073/pnas.1714392115
PMCID:
PMC5834681
AbstractArticlePDF–2.1M
3.
The 2.0 Å X-ray structure for yeast acetohydroxyacid synthase provides new insights into its cofactor and quaternary structure requirements
Thierry Lonhienne, Mario D. Garcia, James A. Fraser, Craig M. Williams, Luke W. Guddat
PLoS One. 2017; 12(2): e0171443. Published online 2017 Feb 8. doi: 10.1371/journal.pone.0171443
PMCID:
PMC5298238
AbstractArticlePDF–2.7M
4.
Regulation of yeast acetohydroxyacid synthase by valine and ATP.
S S Pang, R G Duggleby
Biochem J. 2001 Aug 1; 357(Pt 3): 749–757. doi: 10.1042/0264-6021:3570749
PMCID:
PMC1222004
SummaryPDF–204K
5.
The Role of a FAD Cofactor in the Regulation of Acetohydroxyacid Synthase by Redox Signaling Molecules
Thierry Lonhienne, Mario D. Garcia, Luke W. Guddat
J Biol Chem. 2017 Mar 24; 292(12): 5101–5109. Published online 2017 Feb 3. doi: 10.1074/jbc.M116.773242
PMCID:
PMC5377820
AbstractArticlePDF–1.6M
6.
Increased isobutanol production in Saccharomyces cerevisiae by overexpression of genes in valine metabolism
Xiao Chen, Kristian F Nielsen, Irina Borodina, Morten C Kielland-Brandt, Kaisa Karhumaa
Biotechnol Biofuels. 2011; 4: 21. Published online 2011 Jul 28. doi: 10.1186/1754-6834-4-21
PMCID:
PMC3162486
AbstractArticlePDF–614K
7.
Multivalent Repression of Isoleucine-Valine Biosynthesis in Saccharomyces cerevisiae
P. T. Magee, Lynna M. Hereford
J Bacteriol. 1969 Jun; 98(3): 857–862. doi: 10.1128/jb.98.3.857-862.1969
Correction in:
J Bacteriol. 1969 Oct; 100(1): 554.
PMCID:
PMC315264
SummaryPage BrowsePDF–838K
8.
QTL mapping of volatile compound production in Saccharomyces cerevisiae during alcoholic fermentation
Matthias Eder, Isabelle Sanchez, Claire Brice, Carole Camarasa, Jean-Luc Legras, Sylvie Dequin
BMC Genomics. 2018; 19: 166. Published online 2018 Mar 1. doi: 10.1186/s12864-018-4562-8
PMCID:
PMC5831830
AbstractArticlePDF–2.0M
9.
The ribosome quality control factor Asc1 determines the fate of HSP70 mRNA on and off the ribosome
Lokha R Alagar Boopathy, Emma Beadle, Alan RuoChen Xiao, Aitana Garcia-Bueno Rico, Celia Alecki, Irene Garcia de-Andres, Kyla Edelmeier, Luca Lazzari, Mehdi Amiri, Maria Vera
Nucleic Acids Res. 2023 Jul 7; 51(12): 6370–6388. Published online 2023 May 9. doi: 10.1093/nar/gkad338
PMCID:
PMC10325905
AbstractArticlePDF–2.9M
10.
Initiation of the TORC1-Regulated G0 Program Requires Igo1 and Igo2, which License Specific mRNAs to Bypass Degradation via the 5′-3′ mRNA Decay Pathway
Nicolas Talarek, Elisabetta Cameroni, Malika Jaquenoud, Xuan Luo, Séverine Bontron, Soyeon Lippman, Geeta Devgan, Michael Snyder, James R. Broach, Claudio De Virgilio
Mol Cell. Author manuscript; available in PMC 2011 May 14.
Published in final edited form as: Mol Cell. 2010 May 14; 38(3): 345–355. doi: 10.1016/j.molcel.2010.02.039
PMCID:
PMC2919320
AbstractArticlePDF–1.2M
11.
A Genetic Screen To Identify Genes Influencing the Secondary Redox Couple NADPH/NADP+ in the Yeast Saccharomyces cerevisiae
Shambhu Yadav, Tejasvinee Atul Mody, Archi Sharma, Anand Kumar Bachhawat
G3 (Bethesda) 2020 Jan; 10(1): 371–378. Published online 2019 Nov 22. doi: 10.1534/g3.119.400606
PMCID:
PMC6945034
AbstractArticlePDF–1.3M
12.
Proteasomal Proteomics: Identification of Nucleotide-sensitive Proteasome-interacting Proteins by Mass Spectrometric Analysis of Affinity-purified Proteasomes
Rati Verma, Stephen Chen, Renny Feldman, David Schieltz, John Yates, Juergen Dohmen, Raymond J. Deshaies
Mol Biol Cell. 2000 Oct; 11(10): 3425–3439. doi: 10.1091/mbc.11.10.3425
PMCID:
PMC15004
AbstractArticlePDF–469K
13.
MitoStores: chaperone‐controlled protein granules store mitochondrial precursors in the cytosol
Lena Krämer, Niko Dalheimer, Markus Räschle, Zuzana Storchová, Jan Pielage, Felix Boos, Johannes M Herrmann
EMBO J. 2023 Apr; 42(7): e112309. Published online 2023 Jan 27. doi: 10.15252/embj.2022112309
PMCID:
PMC10068336
AbstractArticlePDF–3.9M
14.
Ubiquitination drives COPI priming and Golgi SNARE localization
Swapneeta S Date, Peng Xu, Nathaniel L Hepowit, Nicholas S Diab, Jordan Best, Boyang Xie, Jiale Du, Eric R Strieter, Lauren P Jackson, Jason A MacGurn, Todd R Graham
eLife. 2022; 11: e80911. Published online 2022 Jul 29. doi: 10.7554/eLife.80911
PMCID:
PMC9374436
AbstractArticlePDF–4.3M
15.
Improving Identification of In-organello Protein-Protein Interactions Using an Affinity-enrichable, Isotopically Coded, and Mass Spectrometry-cleavable Chemical Crosslinker
Karl A. T. Makepeace, Yassene Mohammed, Elena L. Rudashevskaya, Evgeniy V. Petrotchenko, F.-Nora Vögtle, Chris Meisinger, Albert Sickmann, Christoph H. Borchers
Mol Cell Proteomics. 2020 Apr; 19(4): 624–639. Published online 2020 Feb 12. doi: 10.1074/mcp.RA119.001839
PMCID:
PMC7124466
AbstractArticlePDF–7.8M
16.
Elucidation of the interaction proteome of mitochondrial chaperone Hsp78 highlights its role in protein aggregation during heat stress
Witold Jaworek, Marc Sylvester, Giovanna Cenini, Wolfgang Voos
J Biol Chem. 2022 Oct; 298(10): 102494. Published online 2022 Sep 15. doi: 10.1016/j.jbc.2022.102494
PMCID:
PMC9574514
AbstractArticlePDF–1.9M
17.
The S. cerevisiae m6A-reader Pho92 promotes timely meiotic recombination by controlling key methylated transcripts
Jérémy Scutenaire, Damien Plassard, Mélody Matelot, Tommaso Villa, Julie Zumsteg, Domenico Libri, Bertrand Séraphin
Nucleic Acids Res. 2023 Jan 25; 51(2): 517–535. Published online 2022 Aug 8. doi: 10.1093/nar/gkac640
PMCID:
PMC9881176
AbstractArticlePDF–7.3M
18.
Ribosome-Associated Mba1 Escorts Cox2 from Insertion Machinery to Maturing Assembly Intermediates
Isotta Lorenzi, Silke Oeljeklaus, Christin Ronsör, Bettina Bareth, Bettina Warscheid, Peter Rehling, Sven Dennerlein
Mol Cell Biol. 2016 Nov 15; 36(22): 2782–2793. Prepublished online 2016 Aug 22. Published online 2016 Oct 28. doi: 10.1128/MCB.00361-16
PMCID:
PMC5086520
AbstractArticlePDF–2.4M
19.
The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage
Andrew W. Truman, Kolbrun Kristjansdottir, Donald Wolfgeher, Natalia Ricco, Anoop Mayampurath, Samuel L. Volchenboum, Josep Clotet, Stephen J. Kron
Data Brief. 2015 Mar; 2: 12–15. Published online 2014 Nov 7. doi: 10.1016/j.dib.2014.10.006
PMCID:
PMC4459869
AbstractArticlePDF–178K
20.
Quantitative proteomics of the yeast Hsp70/Hsp90 interactomes during DNA damage reveals chaperone-dependent regulation of ribonucleotide reductase
Andrew W. Truman, Kolbrun Kristjansdottir, Donald Wolfgeher, Natalia Ricco, Anoop Mayampurath, Samuel L. Volchenboum, Josep Clotet, Stephen J. Kron
J Proteomics. Author manuscript; available in PMC 2015 Jun 30.
Published in final edited form as: J Proteomics. 2015 Jan 1; 112: 285–300. Published online 2014 Oct 18. doi: 10.1016/j.jprot.2014.09.028
PMCID:
PMC4485990
AbstractArticlePDF–2.0M

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