Risa Kashima
University of California, San Francisco
10 Papers
39 Citations
Risa Kashima is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: microRNA & Drosha. The author has an hindex of 8, co-authored 9 publications. Previous affiliations of Risa Kashima include Sapporo Medical University.
Chat about Author
Papers
Dysregulation of microRNA biogenesis machinery in cancer
Akiko Hata,Risa Kashima +1 more
TL;DR: This review focuses on the recent development regarding the dysregulation of the miRNA biogenesis pathway and its contribution to cancer.
The role of TGF-β superfamily signaling in neurological disorders.
Risa Kashima,Akiko Hata +1 more
TL;DR: A gap in knowledge is revealed regarding the association between TGF-β/BMP signaling pathways and neuronal tissue homeostasis and development and facilitate the research with a potential to develop new therapies for neurological ailments by modulating the pathways.
Augmented noncanonical BMP type II receptor signaling mediates the synaptic abnormality of fragile X syndrome
Risa Kashima,Sougata Roy,Manuel Ascano,Verónica Martínez-Cerdeño,Jeanelle Ariza-Torres,Sunghwan Kim,Justin Louie,Yao Lu,Patricio Leyton,Kenneth D. Bloch,Thomas B. Kornberg,Paul J. Hagerman,Randi J Hagerman,Giorgio Lagna,Akiko Hata +14 more
TL;DR: It is found that the messenger RNA encoding bone morphogenetic protein type II receptor (BMPR2) is a target of FMRP, and that the BMPR2-LIMK1 pathway is a putative therapeutic target in patients with FXS and possibly other forms of autism.
Suppression of C9orf72 RNA repeat-induced neurotoxicity by the ALS-associated RNA-binding protein Zfp106.
Barbara Celona,John Von Dollen,Sarat C. Vatsavayai,Risa Kashima,Jeffrey R. Johnson,Amy A. Tang,Akiko Hata,Bruce L. Miller,Eric J. Huang,Nevan J. Krogan,William W. Seeley,Brian L. Black +11 more
TL;DR: The zinc finger protein Zfp106 is identified as a specific GGGGCC RNA repeat-binding protein, and using affinity purification-mass spectrometry, it is shown that ZFP106 interacts with multiple other RNA binding proteins, including the ALS-associated factors TDP-43 and FUS.
Hyperactive locomotion in a Drosophila model is a functional readout for the synaptic abnormalities underlying fragile X syndrome.
Risa Kashima,Patrick L. Redmond,Prajakta Ghatpande,Sougata Roy,Thomas B. Kornberg,Thomas Hanke,Stefan Knapp,Stefan Knapp,Giorgio Lagna,Akiko Hata +9 more
TL;DR: This study demonstrates that the BMPR2-LIMK pathway is a promising therapeutic target for FXS and the locomotion phenotype of FXS larvae is a quantitative functional readout for the neuromorphological phenotype associated withFXS and is amenable to the screening novel FXS therapeutics.