A lysine–cysteine redox switch with an NOS bridge regulates enzyme function | Nature https://t.co/C8IU9S3Q9n
the authors observe, and have observed before, evidence for lysine-cysteine NOS linkages in protein crystal structures. they have found certain of these proteins to be redox sensitive https://t.co/CTuBtJcBgM
the authors observe, and have observed before, evidence for lysine-cysteine linkages in protein crystal structures. they have found certain of these proteins to be redox sensitive https://t.co/CTuBtJcBgM
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
教科書を書き換える発見はいつでも。 すべてのタンパク質のモデルが変わっちゃうから予想になっちゃう A lysine–cysteine redox switch with an NOS bridge regulates enzyme function | Nature https://t.co/8QFhDNeW7Q
...nice read on protein switches: A lysine–cysteine redox switch with an NOS bridge regulates enzyme function https://t.co/rvRYAwoWJj
Fundamental regulation mechanism of proteins discovered https://t.co/GFcq4cM2mf https://t.co/qU0GdvscG2 https://t.co/lP0jdvUpUd
RT @rei_nari: 来週からタンパク質についての講義をする予定なので、ジスルフィド結合の話をする時に、NOS結合についても簡単に紹介しようと思っている。 https://t.co/MqGGLNMWIf
RT @rei_nari: 来週からタンパク質についての講義をする予定なので、ジスルフィド結合の話をする時に、NOS結合についても簡単に紹介しようと思っている。 https://t.co/MqGGLNMWIf
来週からタンパク質についての講義をする予定なので、ジスルフィド結合の話をする時に、NOS結合についても簡単に紹介しようと思っている。 https://t.co/MqGGLNMWIf
This was fun to read. It would be lovely to see further evidence of the N-O-S bridge perhaps by XFEL or maybe cryo-EM to fully convince myself that this is really not the radiation effect. In contrast, I am all in with S-nitrosylation (S-N-O) on Cys. https
RT @ricestrada: Tuit 169 con información de: https://t.co/OPKiUwXKN6
Tuit 169 con información de: https://t.co/OPKiUwXKN6
RT @ChemicalBiology: I am still puzzling over the NOS linkage reported in the paper: https://t.co/sQuNn6XaNf The proposed mechanisms involv…
I am still puzzling over the NOS linkage reported in the paper: https://t.co/sQuNn6XaNf The proposed mechanisms involve singlet oxygen + seem unlikely energetically. No clear analogies in the chemical literature. This modification is reversible. Anyone hav
Nature "A lysine–cysteine redox switch with an NOS bridge regulates enzyme function" https://t.co/KpD9L3waM7 https://t.co/444pr8sKgF https://t.co/uPeSNyBR98 Atomic resolution structure, quantum chemical calculation, new chemistry. I want to serve this kin
Nature "A lysine–cysteine redox switch with an NOS bridge regulates enzyme function" https://t.co/KpD9L3waM7 https://t.co/444pr8sKgF https://t.co/uPeSNyBR98 少し前に話題になってた論文。実際、自分の好みだった。真の原子分解能構造・量子化学計算・酵素化学。こういう研究に奉仕したい
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
ほえ〜、機構が気になるな。酸素でブリッジって可逆になるかぁ〜?
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
RT @KintaroOfficial: システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアー…
システインとリシンの間にできる新規の共有結合が発見されてますね。アロステリックな酵素機能スイッチになっていて、ジスルフィド結合とは違って形成と分解に異なる化学で、PDBを調べると類似の結合がけっこう見つかるということで、ネイチャーのアーティクルに載ってます。 https://t.co/3qoXM5WgN3
本日の論文紹介で紹介された文献が面白かったので共有。生体内の共有結合でS-Sではなく、N-O-S結合が初めて発見された。どのくらい堅い結合なのかが気になるところ。今後の進展が楽しみ。 A lysine–cysteine redox switch with an NOS bridge regulates enzyme function https://t.co/0QP20jNe8t
RT @NatMetabolism: #NatMetabPicks | In @nature, a group led by Kai Tittmann (@uniGoettingen; @mpi_bpc) identify a previously unknown cystei…
RT @NatMetabolism: #NatMetabPicks | In @nature, a group led by Kai Tittmann (@uniGoettingen; @mpi_bpc) identify a previously unknown cystei…
RT @NatMetabolism: #NatMetabPicks | In @nature, a group led by Kai Tittmann (@uniGoettingen; @mpi_bpc) identify a previously unknown cystei…
RT @sarakosman: Apart from the remarkable discovery, this paper is beautifully written and a truly enjoyable read !!!
Apart from the remarkable discovery, this paper is beautifully written and a truly enjoyable read !!!
RT @NatMetabolism: #NatMetabPicks | In @nature, a group led by Kai Tittmann (@uniGoettingen; @mpi_bpc) identify a previously unknown cystei…
RT @NatMetabolism: #NatMetabPicks | In @nature, a group led by Kai Tittmann (@uniGoettingen; @mpi_bpc) identify a previously unknown cystei…
RT @NatMetabolism: #NatMetabPicks | In @nature, a group led by Kai Tittmann (@uniGoettingen; @mpi_bpc) identify a previously unknown cystei…
RT @NatMetabolism: #NatMetabPicks | In @nature, a group led by Kai Tittmann (@uniGoettingen; @mpi_bpc) identify a previously unknown cystei…
RT @NatMetabolism: #NatMetabPicks | In @nature, a group led by Kai Tittmann (@uniGoettingen; @mpi_bpc) identify a previously unknown cystei…
RT @NatMetabolism: #NatMetabPicks | In @nature, a group led by Kai Tittmann (@uniGoettingen; @mpi_bpc) identify a previously unknown cystei…
#NatMetabPicks | In @nature, a group led by Kai Tittmann (@uniGoettingen; @mpi_bpc) identify a previously unknown cysteine-lysine protein crosslink that serves as a redox switch. https://t.co/A5wrL23c41
RT @PaulHoskisson: A lysine–cysteine redox switch with an NOS bridge regulates enzyme function #Papers365 https://t.co/ZWQfgujEJZ
A lysine–cysteine redox switch with an NOS bridge regulates enzyme function #Papers365 https://t.co/ZWQfgujEJZ
RT @Carter_Lab: Discovery of a covalent crosslink between a cysteine and a lysine residue with a NOS bridge. Beautiful structural work by t…
RT @Carter_Lab: Discovery of a covalent crosslink between a cysteine and a lysine residue with a NOS bridge. Beautiful structural work by t…
Discovery of a covalent crosslink between a cysteine and a lysine residue with a NOS bridge. Beautiful structural work by the Tittmann lab @uniGoettingen. #journalclub https://t.co/AanllF3QBy https://t.co/xcAmhSu1Mh
RT @souyakuchan: Lys-Cys間架橋の発見、Nature。 淋菌のトランスアルドラーゼで見つかった。酸化還元スイッチとして、Lys-Cys結合がアロステリックに酵素活性を制御。ほか既知のPDB構造内にもありそうとのこと。 A lysine–cysteine r…
"When searching the PDB, we identified a number of proteins from all domains of life that are highly likely to possess one or more NOS bridges." https://t.co/E0eRiFXwwQ
A lysine–cysteine redox switch with an NOS bridge regulates enzyme function | Nature https://t.co/FKcIdhI5bX
RT @JohanaMisas: This is really amazing! 🤯👇 A lysine–cysteine redox switch with an NOS bridge regulates enzyme function…
RT @KirkOvermyer: Cool new protein redox modification found, oxidized Cys crosslinked to Lys acting as an allosteric redox switch. https:/…
RT @KirkOvermyer: Cool new protein redox modification found, oxidized Cys crosslinked to Lys acting as an allosteric redox switch. https:/…
Cool new protein redox modification found, oxidized Cys crosslinked to Lys acting as an allosteric redox switch. https://t.co/UqZDl0czir
Absolutely interesting... https://t.co/1enzPT05bZ
Move over disulphide bonds, there's another natural protein crosslink in town https://t.co/7tiXRpHWYh
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
Lab seminar: A new reversible intermolecular covalent bridge, which determines enzyme activity, was discovered. This linkage appears to exist in various proteins. Can't wait for further research on why such a linker is used for enzymes! By Yutaro https://t
RT @torusengoku: きょう読んだやつ A lysine–cysteine redox switch with an NOS bridge regulates enzyme function https://t.co/nb2xAbVWvj こNOSブリッジと活性中心…
きょう読んだやつ A lysine–cysteine redox switch with an NOS bridge regulates enzyme function https://t.co/nb2xAbVWvj こNOSブリッジと活性中心が遠いし、酸化状態と還元状態のX線構造がほとんど変わってないし、制御機構はまだ分からんと思った
RT @serdar_durdagi: Bazen gerçekler göz önündedir, ancak görmek için iyi bakmak gerekir. Buna çok güzel bir örnek, protein katlanma ve stab…
システイン-酸素-リジンの架橋が見つかったやつ、架橋形成が酵素活性としっかりリンクしてるのね というか一体何がどうなったらこんな結合できるようになったんだ… https://t.co/14sv1x7zjE
RT @serdar_durdagi: Bazen gerçekler göz önündedir, ancak görmek için iyi bakmak gerekir. Buna çok güzel bir örnek, protein katlanma ve stab…
RT @serdar_durdagi: Bazen gerçekler göz önündedir, ancak görmek için iyi bakmak gerekir. Buna çok güzel bir örnek, protein katlanma ve stab…
Bazen gerçekler göz önündedir, ancak görmek için iyi bakmak gerekir. Buna çok güzel bir örnek, protein katlanma ve stabilite çalışmalarına yön verebilecek önemli bir çalışma: https://t.co/sj75w12FId https://t.co/vyUEfEEuQp
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @AlvaroM_ENG: Esta investigación descubre un vínculo proteico entre los residuos de cisteína y lisina en una enzima transaldolasa. Este…
RT @AlvaroM_ENG: Esta investigación descubre un vínculo proteico entre los residuos de cisteína y lisina en una enzima transaldolasa. Este…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @AlvaroM_ENG: Esta investigación descubre un vínculo proteico entre los residuos de cisteína y lisina en una enzima transaldolasa. Este…
Esta investigación descubre un vínculo proteico entre los residuos de cisteína y lisina en una enzima transaldolasa. Este puente NOS sirve para regular la actividad enzimática y bien puede estar escondido a simple vista en otras proteínas.
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
先日の Lys-Cys 架橋
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
RT @NaturePortfolio: Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NO…
Research in Nature discovers a protein linkage between cysteine and lysine residues in a transaldolase enzyme. This NOS bridge serves to regulate enzyme activity and may well be hiding in plain sight in other proteins. https://t.co/jlKmGMwdw1 https://t.co/
RT @notherChemist: Guess what! We found a new type of bond in peptides. Read about it in: A lysine–cysteine redox switch with an NOS bridge…
Reactive species biochemistry keeps surprising us! A covalent N-O-S bridge was discovered in a transaldolase of N. gonorrhoeae, and works as a redox allosteric switch. @nature #FEIRecommends #AcademicTwitter https://t.co/k4dzBP7Oye
5/5 estrellas. Excelente servicio
¡La bioquímica de las especies reactivas no deja de sorprendernos! Descubren un puente covalente N-O-S que sirve como interruptor alosterico redox en una transaldolasa de N. gonorrhoeae. @nature #FEIRecomienda https://t.co/k4dzBP7Oye
RT @notherChemist: Guess what! We found a new type of bond in peptides. Read about it in: A lysine–cysteine redox switch with an NOS bridge…
Cool redox regulation through an NOS bridge formed between Cys and Lys residues, revealed in a recent @nature paper by Kai Tittmann @uniGoettingen. https://t.co/VMlgjRLp9y
A lysine–cysteine redox switch with an NOS bridge is a newly discovered protein cross-link that regulates enzyme function. https://t.co/uIJVMHtKQt https://t.co/EmTZU6MTkA