Ribosomal protein L32 contributes to the growth, antibiotic resistance and virulence of Glaesserella parasuis [PDF]
Frontiers in Veterinary ScienceGlaesserella parasuis is the pathogen that causes Glässer’s disease in pigs, which is characterized by fibrinous polyserositis, arthritis and meningitis.
Qiaodan Chen +8 more
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Ribosomal protein L32 enhances hepatocellular carcinoma progression [PDF]
Cancer Medicine, 2023 Purpose The underlying mechanisms of hepatocellular carcinoma (HCC) have not been fully investigated, and effective biomarkers for HCC are still needed to be explored.
Guoxin Hou +3 more
doaj +5 more sources
Paralogous ribosomal protein l32-1 and l32-2 in fission yeast may function distinctively in cellular proliferation and quiescence by changing the ratio of rpl32 paralogs. [PDF]
PLoS ONE, 2013 Fission yeast cells express Rpl32-2 highly while Rpl32-1 lowly in log phase; in contrast, expression of Rpl32-1 raises and reaches a peak level while Rpl32-2 is downregulated to a low basic level when cells enter into stationary phase.
Lei Sun +11 more
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Sleep-Enhancing Effect of Water Extract from Jujube (Zizyphus jujuba Mill.) Seeds Fermented by Lactobacillus brevis L32 [PDF]
Foods, 2023 Although Ziziphus jujuba Mill (jujube) is used in folk medicine for hypnotic sedative, anxiolytic, and many other purposes, to date, only a few studies have revealed its sleep-promoting effects and related mechanisms.
Gi Yeon Bae +5 more
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Biological effect of ribosomal protein L32 on human breast cancer cell behavior
Molecular Medicine Reports, 2020 Breast cancer (BC) is the most common malignancy among women worldwide. However, identifying effective biomarkers for the diagnosis and treatment of BC is challenging. Based on our previously developed ‘humanized’ mouse model of BC, microarray expression
Lu Xu +6 more
semanticscholar +5 more sources
Erratum: “Photobombing Earth 2.0: Diffraction-limit-related Contamination and Uncertainty in Habitable Planet Spectra” (2022, ApJL, 934, L32) [PDF]
The Astrophysical Journal LettersThe original version of this paper included several incorrect con fi guration fi les, which were used to generate some of the fi gures. The con fi guration fi les titled “ LUVeX1000HrEarthCon fi g.txt ” and “ LUVeX1000HrEarthNIRCon fi g.txt ” both correctly ...
Prabal Saxena
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Chloroplast ribosomal protein L32 is encoded in the chloroplast genome [PDF]
FEBS Letters, 1990 The 50 S subunit of chloroplast ribosomes was prepared from tobacco leaves. The proteins were fractionated and the N‐terminal amino acid sequence of a 14 kDa protein was determined. This sequence matches the N‐terminal sequence deduced from ORF55 located between ndhF and trnL on the small single‐copy region of tobacco chloroplast DNA.
F. Yokoi +5 more
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The synthesis of ribosomal proteins S16 and L32 is not autogenously regulated during mouse myoblast differentiation [PDF]
Molecular and Cellular Biology, 1987 A series of mouse myoblast cell lines was constructed that contain 1 to 34 extra copies of either the S16 or the L32 ribosomal protein (r-protein) gene. The metabolism of the S16 and L32 r-proteins and mRNAs was examined in myoblasts and fibers of these cell lines to determine whether the synthesis of these r-proteins is autogenously regulated.
Lewis H. Bowman
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A processed pseudogene in an intron of the HLA-DP beta 1 chain gene is a member of the ribosomal protein L32 gene family. [PDF]
Nucleic Acids Research, 1985 A sequence in an intron of the human HLA-DP beta 1 gene was identified by its homology to the gene encoding ribosomal protein L32 (rpL32). It lacked introns indicating that it was derived from a processed rpL32 mRNA transcript.
J. Young, J. Trowsdale
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Ribosomal protein L32 of Saccharomyces cerevisiae influences both the splicing of its own transcript and the processing of rRNA [PDF]
Molecular and Cellular Biology, 1997 Ribosomal protein L32 of Saccharomyces cerevisiae binds to and regulates the splicing and the translation of the transcript of its own gene. Selecting for mutants deficient in the regulation of splicing, we have identified a mutant form of L32 that no longer binds to the transcript of RPL32 and therefore does not regulate its splicing.
J. Vilardell, J. R. Warner
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