ATF6 activation reduces the secretion and extracellular aggregation of destabilized variants of an amyloidogenic protein.
about
Endoplasmic reticulum quality control and systemic amyloid disease: Impacting protein stability from the inside outRecent Insights into the Role of Unfolded Protein Response in ER Stress in Health and Disease.A Bystander Mechanism Explains the Specific Phenotype of a Broadly Expressed Misfolded Protein.Small molecule proteostasis regulators that reprogram the ER to reduce extracellular protein aggregation.The endoplasmic reticulum HSP40 co-chaperone ERdj3/DNAJB11 assembles and functions as a tetramer.Regulating Secretory Proteostasis through the Unfolded Protein Response: From Function to Therapy.Conditional, Genetically Encoded, Small Molecule-Regulated Inhibition of NFκB Signaling in RPE Cells.Regulating extracellular proteostasis capacity through the unfolded protein response.Endoplasmic Reticulum Proteostasis Influences the Oligomeric State of an Amyloidogenic Protein Secreted from Mammalian CellsEmerging therapeutic targets currently under investigation for the treatment of systemic amyloidosis.Adapting Secretory Proteostasis and Function Through the Unfolded Protein Response.Paradoxical roles of ATF6α and ATF6β in modulating disease severity caused by mutations in collagen X.Pharmacologic ATF6 activating compounds are metabolically activated to selectively modify endoplasmic reticulum proteinsA Destabilizing Domain Allows for Fast, Noninvasive, Conditional Control of Protein Abundance in the Mouse Eye - Implications for Ocular Gene Therapy
P2860
Q28084013-F51F8CE2-3C19-4136-8165-FD81352EAF09Q33653691-69C1A8BF-599F-4830-A40A-0B4111B94D99Q36215027-89E9D232-1D34-4F16-8DCA-C8A499C88618Q38437041-D6149EA7-363D-44C3-B59B-C0B7FF8D3362Q38698836-6DC4408F-11E7-4088-975C-B1D27919E5A3Q39396098-55470E55-8664-4D89-9765-A9199C657C16Q41483603-590F587F-3DDF-4C06-B54D-9E5938767BA8Q41887040-6B12DC50-B427-4CC3-89C3-EA2F50A5529BQ42369036-81A5482E-5606-4074-82C3-CECF7D1415F4Q47404960-5751F02A-6DB7-4F83-A2ED-5A60FA17515EQ47774233-978E9D04-C8C6-4551-ACFB-7C81C3D2E120Q52664254-52A92CC0-E9A0-4C8D-8C0E-0CFD132815F0Q56530196-56167D30-D424-4475-8F20-72B59A539F81Q57819244-0C2DC0C5-D611-4556-8908-B180BE8FE8C9
P2860
ATF6 activation reduces the secretion and extracellular aggregation of destabilized variants of an amyloidogenic protein.
description
2014 nî lūn-bûn
@nan
2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
ATF6 activation reduces the se ...... s of an amyloidogenic protein.
@ast
ATF6 activation reduces the se ...... s of an amyloidogenic protein.
@en
ATF6 activation reduces the se ...... s of an amyloidogenic protein.
@nl
type
label
ATF6 activation reduces the se ...... s of an amyloidogenic protein.
@ast
ATF6 activation reduces the se ...... s of an amyloidogenic protein.
@en
ATF6 activation reduces the se ...... s of an amyloidogenic protein.
@nl
prefLabel
ATF6 activation reduces the se ...... s of an amyloidogenic protein.
@ast
ATF6 activation reduces the se ...... s of an amyloidogenic protein.
@en
ATF6 activation reduces the se ...... s of an amyloidogenic protein.
@nl
P2093
P2860
P1476
ATF6 activation reduces the se ...... s of an amyloidogenic protein.
@en
P2093
John D Hulleman
John J Chen
Joseph C Genereux
Matthew D Shoulders
P2860
P304
P356
10.1016/J.CHEMBIOL.2014.09.009
P577
2014-10-23T00:00:00Z