 Saccharomyces cerevisiae Proteins
"Saccharomyces cerevisiae Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
| Descriptor ID |
D029701
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| MeSH Number(s) |
D12.776.354.750
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Saccharomyces cerevisiae Proteins".
Below are MeSH descriptors whose meaning is more specific than "Saccharomyces cerevisiae Proteins".
This graph shows the total number of publications written about "Saccharomyces cerevisiae Proteins" by people in this website by year, and whether "Saccharomyces cerevisiae Proteins" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
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| 1990 | 1 | 1 | 2 | | 1992 | 1 | 1 | 2 | | 1993 | 8 | 2 | 10 | | 1994 | 16 | 2 | 18 | | 1995 | 12 | 0 | 12 | | 1996 | 16 | 1 | 17 | | 1997 | 22 | 5 | 27 | | 1998 | 22 | 3 | 25 | | 1999 | 23 | 1 | 24 | | 2000 | 19 | 2 | 21 | | 2001 | 20 | 8 | 28 | | 2002 | 21 | 6 | 27 | | 2003 | 22 | 12 | 34 | | 2004 | 19 | 11 | 30 | | 2005 | 11 | 9 | 20 | | 2006 | 9 | 3 | 12 | | 2007 | 10 | 7 | 17 | | 2008 | 12 | 4 | 16 | | 2009 | 13 | 4 | 17 | | 2010 | 5 | 5 | 10 | | 2011 | 11 | 6 | 17 | | 2012 | 10 | 2 | 12 | | 2013 | 9 | 4 | 13 | | 2014 | 9 | 3 | 12 | | 2015 | 11 | 1 | 12 | | 2016 | 8 | 3 | 11 | | 2017 | 8 | 0 | 8 | | 2018 | 3 | 2 | 5 |
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Below are the most recent publications written about "Saccharomyces cerevisiae Proteins" by people in Profiles.
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Li J, Kolberg K, Schlecht U, St Onge RP, Aparicio AM, Horecka J, Davis RW, Hillenmeyer ME, Harvey CJB. A biosensor-based approach reveals links between efflux pump expression and cell cycle regulation in pleiotropic drug resistance of yeast. J Biol Chem. 2019 01 25; 294(4):1257-1266.
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Vijayraghavan S, Kozmin SG, Strope PK, Skelly DA, Lin Z, Kennell J, Magwene PM, Dietrich FS, McCusker JH. Mitochondrial Genome Variation Affects Multiple Respiration and Nonrespiration Phenotypes in Saccharomyces cerevisiae. Genetics. 2019 02; 211(2):773-786.
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Brahma S, Ngubo M, Paul S, Udugama M, Bartholomew B. The Arp8 and Arp4 module acts as a DNA sensor controlling INO80 chromatin remodeling. Nat Commun. 2018 08 17; 9(1):3309.
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Roh SH, Stam NJ, Hryc CF, Couoh-Cardel S, Pintilie G, Chiu W, Wilkens S. The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase Vo Proton Channel. Mol Cell. 2018 03 15; 69(6):993-1004.e3.
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Emerson CH, Lopez CR, Ribes-Zamora A, Polleys EJ, Williams CL, Yeo L, Zaneveld JE, Chen R, Bertuch AA. Ku DNA End-Binding Activity Promotes Repair Fidelity and Influences End-Processing During Nonhomologous End-Joining in Saccharomyces cerevisiae. Genetics. 2018 05; 209(1):115-128.
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Chen H, Xue J, Churikov D, Hass EP, Shi S, Lemon LD, Luciano P, Bertuch AA, Zappulla DC, Géli V, Wu J, Lei M. Structural Insights into Yeast Telomerase Recruitment to Telomeres. Cell. 2018 01 11; 172(1-2):331-343.e13.
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Lee J, Sung N, Yeo L, Chang C, Lee S, Tsai FTF. Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase. Biosci Rep. 2017 12 22; 37(6).
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Elango R, Sheng Z, Jackson J, DeCata J, Ibrahim Y, Pham NT, Liang DH, Sakofsky CJ, Vindigni A, Lobachev KS, Ira G, Malkova A. Break-induced replication promotes formation of lethal joint molecules dissolved by Srs2. Nat Commun. 2017 11 27; 8(1):1790.
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Buzovetsky O, Kwon Y, Pham NT, Kim C, Ira G, Sung P, Xiong Y. Role of the Pif1-PCNA Complex in Pol d-Dependent Strand Displacement DNA Synthesis and Break-Induced Replication. Cell Rep. 2017 Nov 14; 21(7):1707-1714.
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Lee J, Sung N, Mercado JM, Hryc CF, Chang C, Lee S, Tsai FTF. Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation. Sci Rep. 2017 09 11; 7(1):11184.
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