As part of the trans-National Institutes of Health (NIH) Mouse Brain Molecular Anatomy Project (BMAP), and in close coordination with the NIH Mammalian Gene Collection Program (MGC), we initiated a large-scale project to clone, identify, and sequence the complete open reading frame (ORF) of transcripts expressed in the developing mouse nervous system. Here we report the analysis of the ORF sequence of 1274 cDNAs, obtained from 47 full-length-enriched cDNA libraries, constructed by using a novel approach, herein described. cDNA libraries were derived from size-fractionated cytoplasmic mRNA isolated from brain and eye tissues obtained at several embryonic stages and postnatal days. Altogether, including the full-ORF MGC sequences derived from these libraries by the MGC sequencing team, NIH_BMAP full-ORF sequences correspond to approximately 20% of all transcripts currently represented in mouse MGC. We show that NIH_BMAP clones comprise 68% of mouse MGC cDNAs > or =5 kb, and 54% of those > or =4 kb, as of March 15, 2004. Importantly, we identified transcripts, among the 1274 full-ORF sequences, that are exclusively or predominantly expressed in brain and eye tissues, many of which encode yet uncharacterized proteins.
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http://dx.doi.org/10.1101/gr.2601304 | DOI Listing |
J Adv Res
January 2025
Key Laboratory of Basic Pharmacology of Ministry of Education and Joint International Research Laboratory of Ethnomedicine of Ministry of Education and Key Laboratory of Basic Pharmacology of Guizhou Province and Laboratory Animal Centre, Zunyi Medical University, Zunyi, Guizhou, China. Electronic address:
Background: Neurodegenerative diseases (NDs) constitute a significant public health challenge, as they are increasingly contributing to global mortality and morbidity, particularly among the elderly population. Pathogenesis of NDs is intricate and multifactorial. Recently, post-transcriptional modifications (PTMs) of RNA, with a particular focus on mRNA methylation, have been gaining increasing attention.
View Article and Find Full Text PDFPlant Physiol Biochem
December 2024
College of Horticulture, South China Agricultural University, Guangzhou 510642, China. Electronic address:
Chinese cabbage is an important vegetable in southern China. Excessive nitrogen fertilizer application can lead to the accumulation of nitrate in edible organs, which affects food value. Hence, the cultivation of varieties with high nitrogen utilization efficiency (NUE) and low nitrate accumulation is essential for molecular breeding.
View Article and Find Full Text PDFPlant Physiol Biochem
January 2025
College of Life Sciences, Engineering Research Center of the Chinese Ministry of Education for Bioreactor and Pharmaceutical Development, Jilin Agricultural University, Changchun, 130118, China; Institute for Safflower Industry Research / Pharmacy School of Shihezi University, Shihezi, 832003, China. Electronic address:
Moderate UV-B promotes plant growth, but excessive UV-B inhibits plant development. The induction mechanism of how CtWD40-6 responds to UV-B is still unclear in safflower. Our results showed that CtWD40-6 is expressed at the top of safflower leaves and is strongly induced by UV-B.
View Article and Find Full Text PDFPhytomedicine
December 2024
Department of Neurology, Fujian Medical University Union Hospital, Fuzhou, China; Fujian Key Laboratory of Molecular Neurology, Fujian Medical University, Fuzhou, China; Institute of Clinical Neurology, Fujian Medical University, Fuzhou, China. Electronic address:
Background: Perilladehyde, an extract of perillae in the Labiatae family, can produce significant anti-inflammatory and antioxidant effects. Although literature evidences the favorable effect of perillaldehyde on ischemic stroke, the exact mechanism remains blurred.
Purpose: This study attempted to explore the impact of perillaldehyde on cerebral ischemia-reperfusion injury and the related action mechanism.
Int Immunopharmacol
January 2025
AT-31 BIO Inc., 403 Business Incubation Center, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Republic of Korea; Laboratory of Immunobiology, School of Life Science and Biotechnology, College of Natural Sciences, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Republic of Korea. Electronic address:
Recombinant GH16B β-agarase-catalyzed liquefaction of 5-7 %(w/v) melted agarose at 50 °C completely hydrolyzed agarose into neoagarohexaose (NA6) and neoagarotetraose (NA4). Subsequent saccharification by recombinant GH50A β-agarase or recombinant GH50A β-agarase/recombinant GH117A α-neoagarobiose hydrolase at 35 °C converted NA6/NA4 into neoagarobiose (NA2) or 3,6-anhydro-L-galactose (L-AHG)/D-galactose, respectively. Purification of NA6/NA4 and NA2 was achieved by Sephadex G-15 column chromatography, while L-AHG was purified by Sephadex G-10, achieving ≥ 98 % purity.
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