K
Kent E. S. Matlack
Researcher at Massachusetts Institute of Technology
Publications - 17
Citations - 2515
Kent E. S. Matlack is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Endoplasmic reticulum & Sec61. The author has an hindex of 13, co-authored 17 publications receiving 2397 citations. Previous affiliations of Kent E. S. Matlack include University of California, San Francisco & Howard Hughes Medical Institute.
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Journal ArticleDOI
BiP Acts as a Molecular Ratchet during Posttranslational Transport of Prepro-α Factor across the ER Membrane
TL;DR: It is demonstrated that BiP (Kar2p), a member of the Hsp70 family resident in the ER lumen, acts as a molecular ratchet during translocation of the secretory protein prepro-alpha factor through the channel formed by the Sec complex.
Journal ArticleDOI
Functional links between Aβ toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast
Sebastian Treusch,Shusei Hamamichi,Shusei Hamamichi,Jessica L. Goodman,Kent E. S. Matlack,Chee Yeun Chung,Valeriya Baru,Joshua M. Shulman,Joshua M. Shulman,Antonio R. Parrado,Brooke J. Bevis,Julie S. Valastyan,Haesun Han,Malin Lindhagen-Persson,Eric M. Reiman,Eric M. Reiman,Denis A. Evans,David A. Bennett,Anders Olofsson,Philip L. DeJager,Philip L. DeJager,Rudolph E. Tanzi,Kim A. Caldwell,Guy A. Caldwell,Susan Lindquist +24 more
TL;DR: In this article, the authors showed that β-amyloid peptide is an important contributor to Alzheimer's disease (AD) by directing the peptide to the secretory pathway.
Journal ArticleDOI
Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation
Dorit Hanein,Kent E. S. Matlack,Berit Jungnickel,Kathrin Plath,Kathrin Plath,Kai-Uwe Kalies,Kenneth R. Miller,Tom A. Rapoport,Christopher W. Akey +8 more
TL;DR: It is proposed that these cylindrical oligomers represent protein-conducting channels of the ER, formed by ligands specific for co- and posttranslational transport.
Journal ArticleDOI
Protein translocation: tunnel vision.
TL;DR: This manuscript apologizes to colleagues whose important work could only be covered by reference to reviews and discussions in other papers because of a recent review by R. R. Lingappa.
Journal ArticleDOI
Quality Control in the Secretory Pathway: The Role of Calreticulin, Calnexin and BiP in the Retention of Glycoproteins with C-Terminal Truncations
TL;DR: The results showed that the quality control system in the secretory pathway was efficient and sensitive to folding defects, and that it involved multiple interactions with endoplasmic reticulum chaperones.