 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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| 1996 | 4 | 0 | 4 | | 1997 | 5 | 1 | 6 | | 1998 | 5 | 0 | 5 | | 1999 | 8 | 1 | 9 | | 2000 | 8 | 0 | 8 | | 2001 | 5 | 3 | 8 | | 2002 | 7 | 6 | 13 | | 2003 | 7 | 6 | 13 | | 2004 | 8 | 5 | 13 | | 2005 | 7 | 4 | 11 | | 2006 | 11 | 6 | 17 | | 2007 | 4 | 1 | 5 | | 2008 | 12 | 2 | 14 | | 2009 | 6 | 4 | 10 | | 2010 | 7 | 3 | 10 | | 2011 | 9 | 4 | 13 | | 2012 | 7 | 6 | 13 | | 2013 | 13 | 1 | 14 | | 2014 | 9 | 4 | 13 | | 2015 | 10 | 2 | 12 | | 2016 | 6 | 5 | 11 | | 2017 | 16 | 5 | 21 | | 2018 | 10 | 5 | 15 | | 2019 | 4 | 6 | 10 | | 2020 | 5 | 2 | 7 | | 2021 | 8 | 3 | 11 | | 2022 | 8 | 2 | 10 | | 2023 | 10 | 1 | 11 | | 2024 | 5 | 2 | 7 | | 2025 | 7 | 1 | 8 | | 2026 | 3 | 0 | 3 |
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Below are the most recent publications written about "Saccharomyces cerevisiae Proteins" by people in Profiles.
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Wettstein R, King GA, Henggeler A, Walsh ME, Ruediger CT, Ünal E, Matos J. Synaptonemal complex SUMOylation is maintained by Nup60-dependent docking of Ulp1 at the nuclear periphery. Cell Rep. 2026 Jun 23; 45(6):117539.
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Li X, Li J, Shi S, Kuang Z, Srivastava P, Issaian A, Bevers S, Wagley ME, D'Alessandro A, Zhao R. U1 snRNP and RNA polymerase II interaction is predominantly mediated by Prp40 rather than U1-70K in yeast. Nucleic Acids Res. 2026 Jun 08; 54(11).
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Walsh KE, Goodrich JA, Kugel JF. CPSF73 activation and 3' RNA polymerase II pausing are lost during readthrough transcription after heat shock. Cell Rep. 2026 Mar 24; 45(3):117039.
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Dam M, Moreno DF, Brownlow N, Furst A, Spiegelhalter C, Mendoza M. Roles of Srs2/PARI-family DNA helicases in NoCut checkpoint signaling and abscission regulation. J Cell Biol. 2025 12 01; 224(12).
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Walsh ME, Chetlapalli K, Styler BS, Upadhyayula S, King GA, Ünal E. A conserved disruption of nucleocytoplasmic compartmentalization in meiosis is controlled by a kinase-phosphatase pair in Saccharomyces cerevisiae. Mol Biol Cell. 2025 Dec 01; 36(12):ar147.
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Alemany K, Johnson S, Moore JK. Kinesin-8/Kip3 requires beta tubulin tail for depolymerase activity. J Cell Biol. 2025 10 06; 224(10).
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Becht DC, Song J, Selvam K, Yin K, Bai W, Zhao Y, Wu R, Zheng YG, Kutateladze TG. The YEATS domain is a selective reader of histone methacrylation. Structure. 2025 Jul 03; 33(7):1233-1239.e5.
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Tonsager AJ, Zukowski A, Radebaugh CA, Weirich A, Stargell LA, Ramachandran S. The histone chaperone Spn1 preserves chromatin protections at promoters and nucleosome positioning in open reading frames. G3 (Bethesda). 2025 04 17; 15(4).
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Das E, Le L, Sokolova V, Orth JD, Park S. Spatial mechanisms of quality control during chaperone-mediated assembly of the proteasome. Nat Commun. 2025 Apr 09; 16(1):3358.
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Moeller-McCoy CA, Wieser TA, Lubin JW, Gillespie AE, Ramirez JA, Paschini M, Wuttke DS, Lundblad V. The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity. Proc Natl Acad Sci U S A. 2025 Feb 18; 122(7):e2419309122.
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