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Brooke M. Gardner
Researcher at University of California, San Francisco
Publications - 8
Citations - 1841
Brooke M. Gardner is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Endoplasmic reticulum & Unfolded protein response. The author has an hindex of 4, co-authored 6 publications receiving 1634 citations.
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Journal ArticleDOI
Endoplasmic Reticulum Stress Sensing in the Unfolded Protein Response
TL;DR: The mechanistic principles of ER stress sensing are the focus of this review, and yeast Ire1 directly binds to unfolded proteins, which induces its oligomerization and activation.
Journal ArticleDOI
Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response.
Brooke M. Gardner,Peter Walter +1 more
TL;DR: It is found that the core ER-lumenal domain (cLD) of yeast Ire1 binds to unfolded proteins in yeast cells and to peptides primarily composed of basic and hydrophobic residues in vitro.
Journal ArticleDOI
Direct Membrane Association Drives Mitochondrial Fission by the Parkinson Disease-associated Protein α-Synuclein
Ken Nakamura,Venu M. Nemani,Farnaz Azarbal,Gaia Skibinski,Jon M. Levy,Kiyoshi Egami,Larissa A. Munishkina,Jue Zhang,Brooke M. Gardner,Junko Wakabayashi,Hiromi Sesaki,Yifan Cheng,Steven Finkbeiner,Robert L. Nussbaum,Eliezer Masliah,Robert H. Edwards +15 more
TL;DR: It is shown that the expression of α-synuclein in mammalian cells, including neurons in vitro and in vivo, causes the fragmentation of mitochondria.
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The unfolded protein response element IRE1α senses bacterial proteins invading the ER to activate RIG-I and innate immune signaling
Jin A. Cho,Ann-Hwee Lee,Ann-Hwee Lee,Barbara Platzer,Benedict C. S. Cross,Brooke M. Gardner,Heidi De Luca,Phi Luong,Heather P. Harding,Laurie H. Glimcher,Laurie H. Glimcher,Peter Walter,Peter Walter,Edda Fiebiger,Edda Fiebiger,David Ron,Jonathan C. Kagan,Jonathan C. Kagan,Wayne I. Lencer,Wayne I. Lencer +19 more
TL;DR: Inositol-requiring-1α (IRE1α), an ER protein that signals in the unfolded protein response (UPR), is activated to induce inflammation by binding a portion of cholera toxin as it co-opts the ER to cause disease.
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Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis
TL;DR: In this paper , the authors review the role of Pex1/Pex6 in peroxisome biogenesis and degradation and discuss how the unfolding of potential substrates contributes to peroxysome homeostasis, and also consider how advances in cryo-EM, computational structure prediction, and mechanisms of related ATPases are improving our understanding of how Pex 1 and Pex6 converts ATP hydrolysis into mechanical force.