Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Kevin Maciuba"'
Autor:
Felicity R. Sterling, Jon D'Amico, Alexandria M. Brumfield, Kara L. Huegel, Patricia S. Vaughan, Kathryn Morris, Shelby Schwarz, Michelle V. Joyce, Bill Boggess, Matthew M. Champion, Kevin Maciuba, Philip Allen, Eric Marasco, Grant Koch, Peter Gonzalez, Shannon Hodges, Shannon Leahy, Erica Gerstbauer, Edward H. Hinchcliffe, Kevin T. Vaughan
Publikováno v:
Journal of Cell Science. 136
The pathological accumulation of cholesterol is a signature feature of Niemann–Pick type C (NPC) disease, in which excessive lipid levels induce Purkinje cell death in the cerebellum. NPC1 encodes a lysosomal cholesterol-binding protein, and mutati
Publikováno v:
Annu Rev Biochem
Manipulation of individual molecules with optical tweezers provides a powerful means of interrogating the structure and folding of proteins. Mechanical force is not only a relevant quantity in cellular protein folding and function, but also a conveni
Autor:
Kevin Maciuba, Christian M. Kaiser
Publikováno v:
Methods Mol Biol
Optical Tweezers ISBN: 9781071622285
Optical Tweezers ISBN: 9781071622285
Tethering proteins to force probes, typically micrometer-sized beads, is a prerequisite for dissecting their properties with optical tweezers. DNA handles serve as spacers between the tethered protein of interest and the bead surface. Attachment site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55c555231e410ba9b753a8f5e1e8a7df
https://europepmc.org/articles/PMC9924098/
https://europepmc.org/articles/PMC9924098/
Publikováno v:
Biophys J
Single-molecule force spectroscopy with optical tweezers has emerged as a powerful tool for dissecting protein folding. The requirement to stably attach "molecular handles" to specific points in the protein of interest by preparative biochemical tech
Publikováno v:
BioEssays. 43:2100042
The coupling of protein synthesis and folding is a crucial yet poorly understood aspect of cellular protein folding. Over the past few years, it has become possible to experimentally follow and define protein folding on the ribosome, revealing princi
Publikováno v:
Molecular Cell. 74:310-319.e7
Multi-domain proteins, containing several structural units within a single polypeptide, constitute a large fraction of all proteomes. Co-translational folding is assumed to simplify the conformational search problem for large proteins, but the events
Publikováno v:
Biophysical Journal. 116:38a
Publikováno v:
Biophysical Journal. 114:552a