立命館大学 研究者学術情報データベース
English>>
TOPページ
ウエハラ リョウ
上原 了
UEHARA RYO
所属
生命科学部 生物工学科
職名
助教
論文
1.
2022/04
Asteltoxin inhibits extracellular vesicle production through AMPK/mTOR-mediated activation of lysosome function. │ Scientific reports │ 12 (1),6674
2.
2022/04
MEK/ERK-mediated oncogenic signals promote secretion of extracellular vesicles by controlling lysosome function. │ Cancer science │ 113 (4),1264-1276
3.
2021/02
Insertion loop-mediated folding propagation governs efficient maturation of hyperthermophilic Tk-subtilisin at high temperatures. │ FEBS letters │ 595 (4),452-461
4.
2020/09
Crystal structure of a GH1 β-glucosidase from Hamamotoa singularis. │ Protein science : a publication of the Protein Society │ 29 (9),2000-2008
5.
2020/02
Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli. │ Acta crystallographica. Section F, Structural biology communications │ 76 (Pt 2),86-93
6.
2020
Val143 of human ribonuclease H2 is not critical for, but plays a role in determining catalytic activity and substrate specificity. │ PloS one │ 15 (2),e0228774
7.
2019/08
Unlike the Escherichia coli counterpart, archaeal RNase HII cannot process ribose monophosphate abasic sites and oxidized ribonucleotides embedded in DNA. │ The Journal of biological chemistry │ 294 (35),13061-13072
8.
2019/05
Aicardi-Goutières syndrome gene Rnaseh2c is a metastasis susceptibility gene in breast cancer. │ PLOS Genetics │ 15 (5),e1008020
9.
2018/10
Two RNase H2 Mutants with Differential rNMP Processing Activity Reveal a Threshold of Ribonucleotide Tolerance for Embryonic Development. │ Cell Reports │ 25 (5),1135-1145
10.
2013/12
Formation of the high-affinity calcium binding site in pro-subtilisin E with the insertion sequence IS1 of pro-Tk-subtilisin. │ Biochemistry │ 52 (50),9080-9088
11.
2013/10
Increase in activation rate of Pro-Tk-subtilisin by a single nonpolar-to-polar amino acid substitution at the hydrophobic core of the propeptide domain. │ Protein Science │ 22 (12),1711-1721
12.
2013/02
Accelerated maturation of Tk-subtilisin by a Leu→Pro mutation at the C-terminus of the propeptide, which reduces the binding of the propeptide to Tk-subtilisin. │ FEBS Journal │ 280 (4),994-1006
13.
2012/11
Requirement of insertion sequence IS1 for thermal adaptation of Pro-Tk-subtilisin from hyperthermophilic archaeon. │ Extremophiles │ 16 (6),841-851
14.
2012/06
Requirement of Ca2+ Ions for the Hyperthermostability of Tk-subtilisin from Thermococcus kodakarensis. │ Biochemistry │ 51 (26),5369-5278