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プロフィール詳細
Dr. Pratibha K.に依頼
India
Scientific Writer | PhD in Structural Biology | Therapeutic Antibodies | Protein Science | Biologics
プロフィール概要
専門分野
サービス
Writing
Clinical Trial Documentation,
Medical Writing,
Technical Writing,
Creative Writing
職務経験
PostdoctoralResearcher
Uppsala University
12月 2025 - 現在
Associate Manager
Biocon Biologics
9月 2021 - 10月 2024
PostdoctoralResearcher
INSA, Toulouse, France
2月 2020 - 7月 2021
学歴
Doctoral Program
ETHZ - ETH Zurich - Switzerland
3月 2015 - 12月 2019
認定資格
- 認定資格の詳細は未入力です。
出版物
JOURNAL ARTICLE
Pratibha Kumari, Dhiman Ghosh, Agathe Vanas, Yanick Fleischmann, Thomas Wiegand, Gunnar Jeschke, Roland Riek, Cédric Eichmann(2021). Structural insights into α-synuclein monomer–fibril interactions . Proceedings of the National Academy of Sciences. 118. (10). Proceedings of the National Academy of Sciences
Guerrero-Ferreira R, Taylor NM, Arteni AA, Kumari P, Mona D, Ringler P, Britschgi M, Lauer ME, Makky A, Verasdonck J, et al.(2019). Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy . eLife.
Burmann BM, Gerez JA, Matečko-Burmann I, Campioni S, Kumari P, Ghosh D, Mazur A, Aspholm EE, Šulskis D, Wawrzyniuk M, et al.(2019). Regulation of α-synuclein by chaperones in mammalian cells . Nature.
Kumari P, Frey L, Sobol A, Lakomek NA, Riek R(2018). 15N transverse relaxation measurements for the characterization of µs-ms dynamics are deteriorated by the deuterium isotope effect on 15N resulting from solvent exchange . Journal of biomolecular NMR.
Kumar H, Singh J, Kumari P, Udgaonkar JB(2017). Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T . The Journal of biological chemistry.
Eichmann C, Kumari P, Riek R(2017). High-density lipoprotein-like particle formation of Synuclein variants . FEBS letters.
OTHER
Guerrero-Ferreira R, Taylor NM, Arteni A, Kumari P, Mona D, Ringler P, Britschgi M, Lauer ME, Makky A, Verasdock J, et al.(2019). Two new polymorphic structures of alpha-synuclein solved by cryo-electron microscopy .