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今回総説を執筆するにあたって、とりあえず忘れないようにメモをしておきたいTargeting tau: Clinical trials and novel therapeutic approacheshttps://www.sciencedirect.com/science/article/pii/S0304394020301890Nature (Published: 31 August 2016) The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease aducanumabの衝撃的デビューhttps://www.nature.com/articles/nature19323Why not bapineuzumab? https://www.evaluate.com/vantage/articles/analysis/why-not-bapineuzumabAlzheimer's disease Attack on amyloid-β protein 2016年当時のアミロイド仮説 Nature https://www.nature.com/articles/537036aThe Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade https://content.iospress.com/articles/journal-of-alzheimers-disease/jad179941Chemical Communications ・ Control of the toxic conformation of amyloid β42 by intramolecular disulfide bond formation† https://pubs.rsc.org/en/content/articlelanding/2020/cc/d0cc01053g#!divAbstractStructural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-β (23 April 2018)https://t.co/Kro6TuNvJOシヌクレインに関して何か最近の話題があったようなきがしたが~~~~~~~~~~~~~~~~~~~~~~~~~~~~以下はまあどうでもよい備忘録メモ LLPS関係3件Phase separation of the LINE-1 ORF1 protein is mediated by the N-terminus and coiled-coil domain https://www.sciencedirect.com/science/article/pii/S0006349521002587Phase separation of p53 precedes aggregation and is affected by oncogenic mutations and ligands† https://pubs.rsc.org/en/content/articlehtml/2021/sc/d1sc01739jSynthetic Protein Condensates That Inducibly Recruit and Release Protein Activity in Living Cells https://pubs.acs.org/doi/10.1021/jacs.0c12375AMPKについて TJ強化メカニズム論文の本命ではないか?Mechanisms involved in AMPK-mediated deposition of tight junction components to the plasma membrane https://journals.physiology.org/doi/full/10.1152/ajpcell.00422.2019あとAXINがLLPSする話どうしたっけか
2021.06.11
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Domain swapping fibril 実験法の主要論文リストアップ全部じゃないけれどもとりあえず備忘録代わりに例のごとく玉石混交です、きにしないきにしないGB1http://www.jbc.org/content/286/33/28988.fullhttp://www.sciencedirect.com/science/article/pii/S0022283605002767http://pubs.acs.org/doi/abs/10.1021/bi048197lSUMOhttp://pubs.acs.org/doi/abs/10.1021/bm3004385 Venturahttp://pubs.acs.org/doi/abs/10.1021/bm401776z Entropic bristle, MUST READhttp://journal.frontiersin.org/article/10.3389/fmicb.2015.01516/abstract Rho terminatorhttp://www.mdpi.com/1422-0067/14/9/17830/htm URN-FF domainHELhttp://onlinelibrary.wiley.com/doi/10.1110/ps.9.2.369/pdfhttp://onlinelibrary.wiley.com/doi/10.1110/ps.03183404/fullhttp://www.sciencedirect.com/science/article/pii/S0022283600938622http://pubs.acs.org/doi/pdf/10.1021/bm0498979AL amyloidosishttp://pubs.acs.org/doi/abs/10.1021/bi5007892濱田大三先生http://onlinelibrary.wiley.com/doi/10.1002/pro.2228/full 阿部義人先生http://link.springer.com/article/10.1007/s00726-015-1918-0#/page-1阿部義人先生http://elifesciences.org/content/4/e10935v2small mol wt inhibitor AL amyloidosishttp://onlinelibrary.wiley.com/doi/10.1002/pro.2790/fullp53Detection of p53 Protein Aggregation in Cancer Cell Lines and Tumor Sampleshttp://link.springer.com/protocol/10.1007/978-1-4939-1661-0_7#page-1Amyloidogenicity of p53: a hidden link between protein misfolding and cancerhttp://www.ingentaconnect.com/content/ben/cpps/2015/00000016/00000002/art00006Reversible amyloid formation by the p53 tetramerization domain and a cancer-associated mutanthttp://www.sciencedirect.com/science/article/pii/S002228360300175XUnfolding, aggregation, and amyloid formation by the tetramerization domain from mutant p53 associated with lung cancer(坂口先生)http://pubs.acs.org/doi/abs/10.1021/bi051192jDisruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrilshttp://onlinelibrary.wiley.com/doi/10.1110/ps.051622005/fullFibrillar aggregates of the tumor suppressor p53 core domainhttp://pubs.acs.org/doi/abs/10.1021/bi034218k74 被引用数 これが大本か?The (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assembliesfull textp53 Aggregates Penetrate Cells and Induce the Co-Aggregation of Intracellular p53http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0069242ブログ村で生命科学系論文紹介のブログを探してみる
2016.03.25
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最悪だ。読まねばならない論文があとからあとから湧いてでるではないか!というわけで第二弾。どうしたもんですかね。でもまあ気づいてよかった。Lu JX, Qiang W, Yau WM, Schwieters CD, Meredith SC, Tycko R. Molecular structure of β-amyloid fibrils in Alzheimer’s disease brain tissue. Cell. 2013 Sep 12;154(6):1257-68. Abstract [PDF]どうやらヒト患者からとってきたアミロイドの構造論文らしいが、ほんとうなのだろうか?関連付けられているPDBは2lmp。どんなのか手っ取り早く知りたければPDBSUMで。勝手に画像だけは貼ってしまおう。でもこれは2008年にTyckoらが決めた固体NMRの構造だし、Abeta1-40(毒性の低い、取り扱いの楽な試料のほう)だし、Cell論文と一緒に出されても、なんだか違和感が・・・。中身をしっかり読まないとまずいらしい。時間ないけど。Aguzzi A, Gitler AD. A template for new drugs against Alzheimer’s disease. Cell. 2013 Sep 12;154(6):1182-4. Abstract [PDF]で、こっちは創薬だ。大変だ。備忘録ついでに。講義やアカデミック利用の研究会での資料用に、なんと素敵なパワポが公開されているではないか。http://www.ipa-online.org/neurosite/presentations.asp International Psychogeriatric Association国際老年精神医学会のサポートページのようです。美麗、秀逸。ブログ村で蛋白質立体構造関連のブログを探してみる
2013.09.18
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