Zobrazeno 1 - 10
of 73
pro vyhledávání: '"Sean S. Molloy"'
Autor:
Sean S. Molloy, Chien Hui Hung, Gary Thomas, Sylvain Feliciangeli, François Jean, Ujwal Shinde, Gregory K. Scott, Laurel Thomas, Ezhilkani Subbian
Publikováno v:
Journal of Biological Chemistry. 281:16108-16116
The folding and activation of furin occur through two pH- and compartment-specific autoproteolytic steps. In the endoplasmic reticulum (ER), profurin folds under the guidance of its prodomain and undergoes an autoproteolytic excision at the consensus
Publikováno v:
Trends in Cell Biology. 9:28-35
Furin is a secretory pathway endoprotease that catalyses the maturation of a strikingly diverse group of proprotein substrates, ranging from growth factors and receptors to pathogen proteins, in multiple compartments within the trans-Golgi network (T
Publikováno v:
The Journal of Cell Biology
The regulated sorting of proteins within the trans-Golgi network (TGN)/endosomal system is a key determinant of their biological activity in vivo. For example, the endoprotease furin activates of a wide range of proproteins in multiple compartments w
Publikováno v:
Journal of Biological Chemistry. 267:16396-16402
Previous work demonstrated that human furin is a predominantly Golgi membrane-localized endoprotease that can efficiently process precursor proteins at paired basic residues (-Lys-Arg- or -Arg-Arg-) in transfected cells. Anion-exchange chromatography
Publikováno v:
Journal of Biological Chemistry. 267:14304-14308
Human furin is a calcium-dependent serine endoprotease that can efficiently cleave many precursor proteins on the carboxyl side of the consensus cleavage sequence, -Arg-X-Lys/Arg-Arg-, both in vivo and in vitro. Analysis of furin proteins in extracts
Autor:
Sean S. Molloy, Mary B. Kennedy
Publikováno v:
Proceedings of the National Academy of Sciences. 88:4756-4760
Autophosphorylation of Thr^(286) on type II Ca^(2+)/calmodulin-dependent protein kinase (CaM kinase) in vitro causes kinase activity to become partially independent of Ca^(2+). Here we report that Thr^(286) is the major CaM kinase autophosphorylation
Publikováno v:
The Journal of biological chemistry. 277(15)
The propeptide of furin has multiple roles in guiding the activation of the endoprotease in vivo. The 83-residue N-terminal propeptide is autoproteolytically excised in the endoplasmic reticulum (ER) at the consensus furin site, -Arg(104)-Thr-Lys-Arg
Autor:
Michael A. Jarvis, Gary Thomas, François Jean, Sean S. Molloy, Gseping Liu, Laurel Thomas, Jay A. Nelson
Current antiviral strategies target viral gene products. Although initially successful, their severe toxicity and susceptibility to circumvention by the generation of drug-resistant variants limit their usefulness. By contrast, the central role of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b61f53124a8693bc07ba0de0f680965e
https://europepmc.org/articles/PMC16021/
https://europepmc.org/articles/PMC16021/
Autor:
Sheree Lynn Rybak, Laurel Thomas, Yang Kevin Xiang, Lei Wan, Sean S. Molloy, Gary Thomas, Gseping Liu
Publikováno v:
Cell. 94(2)
We report the role of one member of a novel gene family, PACS-1, in the localization of trans-Golgi network (TGN) membrane proteins. PACS-1 directs the TGN localization of furin by binding to the protease’s phosphorylated cytosolic domain. Antisens