@MSakuma8 Profile picture

m.sk

@MSakuma8

PosDoc in University of British Columbia/Evolution/Enzyme/Single molecule measurement/Microfluidics/Microscope/Running on faith

Joined March 2019
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m.sk Reposted

Our latest manuscript "Understanding epistatic networks in the B1 β-lactamases through coevolutionary statistical modeling and deep mutational scanning" is out @NatureComms It is a great collaboration with Francesco Zamponi and Martin Weigt! nature.com/articles/s4146…


m.sk Reposted

Finally published! Thank you so much @PaolaLaurino and all lab members for your continuous support! @OISTeduでの博士研究がオンラインになりました! #CAZyme #GH19 nature.com/articles/s4146…

Congrats to @d_zome, who published today in @NatureComms part of his PhD work @OISTedu 🥳!!! Pls check it here rdcu.be/dELQk and in the following:



m.sk Reposted

Excited to share our new preprint! We have done a comprehensive bioinformatic analysis of β-lactamases (all major five classes together). The work pretty much repaints our understanding of how β-lactamases are distributed in the environments. biorxiv.org/content/10.110…


m.sk Reposted

Are you interested how #epistasis shapes the AMR evolution? We showed that epistasis can be caused by independently modulating substrate binding and the chemical step ultimately changing the rate-limiting step in the catalytic cycle. @NatureCatalysis nature.com/articles/s4192…


m.sk Reposted

Happy to share that our latest paper led by @chrfrohlich and @AdrianBunzel is out @NatureCatalysis If you like protein evolution and epistasis, this paper will give you interesting insights; Shifting the rate-limiting step can cause strong epistasis. nature.com/articles/s4192…


m.sk Reposted

Happy to share our new manuscript "Measuring differential fitness costs and interactions between genetic cassettes using fluorescent spectrophotometry". We developed a nice and easy way to determine fitness differences using a fluorescent plate reader. journals.asm.org/doi/10.1128/ae…


m.sk Reposted

Our latest paper "Pervasive epistasis exposes intramolecular networks in adaptive enzyme evolution" is now out in @NatureComms A great work from @_karolbuda and @CharlotteMiton, exploring epistasis and idiosyncrasy in enzyme adaptive landscapes. nature.com/articles/s4146…


m.sk Reposted

Origin Of Evolutionary Bifurcation In An Enzyme biorxiv.org/cgi/content/sh… #biorxiv_evobio


m.sk Reposted

We found my father! He seemed to fall down yesterday and hospitalized. He is well now. Thank the person who helped him, VPD and you all!


m.sk Reposted

🚨 Preprint alert! Revealing the mechanisms of EPISTASIS in enzyme evolution (β-lactamase OXA-48). Mutations may be structurally orthogonal, but their combination exhibits powerful epistasis driving AMR. The key? Shifting the rate-limiting step! biorxiv.org/content/10.110…


m.sk Reposted

公募班・加藤グループとD01班・本田教授グループとの共同研究の成果です。安価なキチン粉末を用いた Strep-tag 融合タンパク質の精製手法を開発しました。 onlinelibrary.wiley.com/doi/10.1002/an…


m.sk Reposted

So excited to get to share the preprint of our work (also my very first research article!) at the @tokuriki_lab demonstrating that evolution under static selection pressures can promote functional diversity, and thus population-level evolvability, in proteins.

Thrilled to share our latest preprint collab with the amazing Tokuriki Lab (@tokuriki_lab) and the lead author, Ayse (@erdogananisan)! We explain how the combination of neutral drift & threshold selection maintains phenotypic variation. biorxiv.org/content/10.110…



m.sk Reposted

Happy to share our recent preprint "Neutral Drift and Threshold Selection Promote Phenotypic Variation". This work touches on a profound question of how "phenotypic variation" can arise from evolutionary drift in a simple and static environment. biorxiv.org/content/10.110…


Chem-Stationにて酵素1分子計測(JACS, 2023)の研究成果を掲載していただきました!

酵素の分子個性のダイバーシティは酵素進化のバロメーターとなる | Chem-Station (ケムステ) bit.ly/3m1MXCk

chemstation's tweet image. 酵素の分子個性のダイバーシティは酵素進化のバロメーターとなる | Chem-Station (ケムステ) bit.ly/3m1MXCk


m.sk Reposted

【注目プレスリリース】回転分子モーターの動きをコントロールする「留め金」はモーターの回転方向に依存して外れる ――ATP合成酵素の制御機構の解明―― / 分子科学研究所 research-er.jp/articles/view/…


m.sk Reposted

Our paper is now out from @NatureComms, entitled "Molecular mechanism on forcible ejection of ATPase inhibitory factor 1 from mitochondrial ATP synthase" doi.org/10.1038/s41467…


m.sk Reposted

Happy to share our new preprint conducted by @_karolbuda and @CharlotteMiton, "Higher-Order Epistasis Creates Idiosyncrasy, Confounding Predictions in Protein Evolution". biorxiv.org/content/10.110…

tokuriki_lab's tweet image. Happy to share our new preprint conducted by @_karolbuda and @CharlotteMiton, "Higher-Order Epistasis Creates Idiosyncrasy, Confounding Predictions in Protein Evolution". 
biorxiv.org/content/10.110…

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