B
Bogdan Budnik
Researcher at Harvard University
Publications - 68
Citations - 5828
Bogdan Budnik is an academic researcher from Harvard University. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 22, co-authored 53 publications receiving 4206 citations.
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Journal ArticleDOI
The TREM2-APOE Pathway Drives the Transcriptional Phenotype of Dysfunctional Microglia in Neurodegenerative Diseases
Susanne Krasemann,Susanne Krasemann,Charlotte Madore,Ron Cialic,Caroline Baufeld,Narghes Calcagno,Rachid El Fatimy,Lien Beckers,Elaine O’Loughlin,Yang Xu,Zain Fanek,David J. Greco,Scott T. Smith,George Tweet,Zachary Humulock,Tobias Zrzavy,Patricia Conde-Sanroman,Mar Gacias,Zhiping Weng,Hao Chen,Emily C. Tjon,Fargol Mazaheri,Kristin Hartmann,Asaf Madi,Jason D. Ulrich,Markus Glatzel,Anna Worthmann,Joerg Heeren,Bogdan Budnik,Cynthia A. Lemere,Tsuneya Ikezu,Frank L. Heppner,Vladimir Litvak,David M. Holtzman,Hans Lassmann,Howard L. Weiner,Jordi Ochando,Christian Haass,Oleg Butovsky +38 more
TL;DR: The TREM2-APOE pathway is identified as a major regulator of microglial functional phenotype in neurodegenerative diseases and serves as a novel target that could aid in the restoration of homeostatic microglia.
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Peptidomic discovery of short open reading frame–encoded peptides in human cells
Sarah A. Slavoff,Andrew J. Mitchell,Adam G. Schwaid,Moran N. Cabili,Moran N. Cabili,Jiao Ma,Joshua Z. Levin,Amir Karger,Bogdan Budnik,John L. Rinn,John L. Rinn,Alan Saghatelian +11 more
TL;DR: A peptidomic strategy to detect short ORF (sORF)-encoded polypeptides (SEPs) in human cells is developed, and 90 SEPs are identified, 86 of which are novel, the largest number of human SEPs ever reported.
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SCoPE-MS: mass spectrometry of single mammalian cells quantifies proteome heterogeneity during cell differentiation.
TL;DR: This work develops Single Cell ProtEomics by Mass Spectrometry (SCoPE-MS) and validate its ability to identify distinct human cancer cell types based on their proteomes and uses it to quantify over a thousand proteins in differentiating mouse embryonic stem cells.
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Reversible, Specific, Active Aggregates of Endogenous Proteins Assemble upon Heat Stress.
Edward W. J. Wallace,Jamie L. Kear-Scott,Evgeny V. Pilipenko,Michael H. Schwartz,Pawel R. Laskowski,Alexandra E Rojek,Alexandra E Rojek,Christopher D. Katanski,Joshua A. Riback,Michael F. Dion,Alexander Franks,Edoardo M. Airoldi,Tao Pan,Bogdan Budnik,D. Allan Drummond +14 more
TL;DR: It is proposed that most heat-induced aggregation of mature proteins reflects the operation of an adaptive, autoregulatory process of functionally significant aggregate assembly and disassembly that aids cellular adaptation to thermal stress.
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Misfolded proteins impose a dosage-dependent fitness cost and trigger a cytosolic unfolded protein response in yeast
Kerry Geiler-Samerotte,Michael F. Dion,Bogdan Budnik,Stephanie M. Wang,Daniel L. Hartl,D. Allan Drummond +5 more
TL;DR: Assuming that most misfolded proteins impose similar costs, yeast cells express almost all proteins at steady-state levels sufficient to expose their encoding genes to selection against misfolding, lending credibility to the recent suggestion that such selection imposes a global constraint on molecular evolution.