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Kazutoshi Mori
is a Japanese molecular biologist known for research on unfolded protein response. He is a professor of Biophysics at the Graduate School of Science, Kyoto University, and shared the 2014 Albert Lasker Basic Medical Research Award with Peter Walter for discoveries concerning the unfolded protein response — an intracellular quality control system that detects harmful misfolded proteins in the endoplasmic reticulum and signals the nucleus to carry out corrective measures. Early life and education Mori was born in 1958 in Kurashiki, Okayama. In the elementary school era, he was good at mathematics and arithmetic, and learned from the newspaper about the existence of quarks. In the middle school era, he was influenced by the Nobel Prize in Physics of Hideki Yukawa, and he decided to study physics at the Faculty of Science at Kyoto University (at the time, the golden age of elementary particle physics). However, he was finally admitted to the Department of Synthetic Chemistry of t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Kurashiki, Okayama
is a historic city located in western Okayama Prefecture, Japan, sitting on the Takahashi River, on the coast of the Inland Sea. As of March 31, 2017, the city has an estimated population of 483,576 and a population density of 1,400 persons per km². The total area is 355.63 km². History The modern city of Kurashiki was founded on April 1, 1928. Previously, it was the site of clashes between the Taira and Minamoto clans during the Heian period. It gradually developed as a river port. During the Edo period, it became an area directly controlled by the shogunate. Distinctive white-walled, black-tiled warehouses were built to store goods. During the Meiji Restoration (Japan's Industrial Revolution period), factories were built, including the Ohara Spinning Mill, which still stands as the nostalgic tourist attraction Ivy Square. On August 1, 2005, the town of Mabi (from Kibi District), and the town of Funao (from Asakuchi District) were merged with Kurashiki. Geography ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nobel Prize In Physics
) , image = Nobel Prize.png , alt = A golden medallion with an embossed image of a bearded man facing left in profile. To the left of the man is the text "ALFR•" then "NOBEL", and on the right, the text (smaller) "NAT•" then "MDCCCXXXIII" above, followed by (smaller) "OB•" then "MDCCCXCVI" below. , awarded_for = Outstanding contributions for humankind in the field of Physics , presenter = Royal Swedish Academy of Sciences , location = Stockholm, Sweden , date = , reward = 9 million Swedish kronor (2017) , year = 1901 , holder_label = Most recently awarded to , holder = Alain Aspect, John Clauser, and Anton Zeilinger , most_awards = John Bardeen (2) , website nobelprize.org, previous = 2021 , year2=2022, main=2022, next= 2023 The Nobel Prize in Physics is a yearly award given by the Royal Swedish Academy of Sciences for those who have made the most outstanding contributions for humankind in the field of physics. I ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ire1
The serine/threonine-protein kinase/endoribonuclease inositol-requiring enzyme 1 α (IRE1α) is an enzyme that in humans is encoded by the ''ERN1'' gene. Function The protein encoded by this gene is the ER to nucleus signalling 1 protein, a human homologue of the yeast Ire1 gene product. This protein possesses intrinsic kinase activity and an endoribonuclease activity and it is important in altering gene expression as a response to endoplasmic reticulum-based stress signals (mainly the unfolded protein response). Two alternatively spliced transcript variants encoding different isoforms have been found for this gene. Signaling IRE1α possesses two functional enzymatic domains, an endonuclease and a trans-autophosphorylation kinase domain. Upon activation, IRE1α oligomerizes and carries out an unconventional RNA splicing activity, removing an intron from the X-box binding protein 1 ( XBP1) mRNA, and allowing it to become translated into a functional transcription factor, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ATF6
Activating transcription factor 6, also known as ATF6, is a protein that, in humans, is encoded by the ''ATF6'' gene and is involved in the unfolded protein response. Function ATF6 is an endoplasmic reticulum (ER) stress-regulated transmembrane transcription factor that activates the transcription of ER molecules. Accumulation of misfolded proteins in the Endoplasmic Reticulum results in the proteolytic cleavage of ATF6. The cytosolic portion of ATF6 will move to the nucleus and act as a transcription factor to cause the transcription of ER chaperones. See also * Activating transcription factor Interactions ATF6 has been shown to interact with YY1 and Serum response factor Serum response factor, also known as SRF, is a transcription factor protein. Function Serum response factor is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors. This protein binds to the serum .... References Further reading * * * * * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hac1 Xbp1 Intron
The bZIP intron RNA motif is an RNA structure guiding splicing of a non-canonical intron from bZIP-containing genes called HAC1 in yeast, XBP1 in Metazoa, Hxl1 or Cib1 in Basidiomycota and bZIP60 in plants. Splicing is performed independently of the spliceosome by Ire1, a kinase with endoribonuclease activity. Exons are joined by a tRNA ligase. Recognition of the intron splice sites is mediated by a base-paired secondary structure of the mRNA that forms at the exon/intron boundaries. Splicing of the bZIP intron is a key regulatory step in the unfolded protein response (UPR). The Ire-mediated unconventional splicing was first described for HAC1 in ''S. cerevisiae''. Consensus structure The secondary structure of the bZIP intron is very well conserved, and consists of two hairpins (H2 and H3) around the splice sites, and an extended hairpin (H1) that brings the splice sites together (see figure). The sequence of the intron is well conserved only around the splice sites. Non-can ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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