The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils.
about
Structural Insights into High Density Lipoprotein: Old Models and New FactsAmyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosisHuman apolipoprotein A-I natural variants: molecular mechanisms underlying amyloidogenic propensityStructural and Functional Analysis of the ApolipoproteinA-I A164S VariantElucidation of the Aggregation Pathways of Helix-Turn-Helix Peptides: Stabilization at the Turn Region Is Critical for Fibril Formation.Amyloid triangles, squares, and loops of apolipoprotein C-III.Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I.EPR assessment of protein sites for incorporation of Gd(III) MRI contrast labelsSecondary structure changes in ApoA-I Milano (R173C) are not accompanied by a decrease in protein stability or solubility.Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I.Dual role of an N-terminal amyloidogenic mutation in apolipoprotein A-I: destabilization of helix bundle and enhancement of fibril formation.Discoidal HDL and apoA-I-derived peptides improve glucose uptake in skeletal muscle.Apolipoprotein A-I: the dual face of a protein.Molecular crowding impacts the structure of apolipoprotein A-I with potential implications on in vivo metabolism and function.The secondary structure of apolipoprotein A-I on 9.6-nm reconstituted high-density lipoprotein determined by EPR spectroscopy.Single injections of apoA-I acutely improve in vivo glucose tolerance in insulin-resistant mice.ApoA-I Milano stimulates lipolysis in adipose cells independently of cAMP/PKA activation.Plasma stem cell factor levels are associated with risk of cardiovascular disease and death.
P2860
Q26770434-2A96E539-691D-4CC1-BC91-3739FA913E56Q28116206-B95FA234-08DE-4AC3-BAAE-82EE1BDC6F7BQ28482893-492300C9-8A86-4811-A959-12CA0BA02F81Q28551157-EB9236CB-57CE-401C-876E-FDEB1D4425ADQ30660049-693218FA-CBB9-4D01-950D-C882456F6FCBQ33684952-B46C053B-B118-445E-89A3-175E057BD44FQ34559652-8E415CE1-4399-4668-9E4D-2A7922E8B43DQ34680348-D2E02578-F799-426E-AF52-257CCE911793Q35154892-3AFF8E29-9C1D-4372-A07D-D101018C8229Q35536293-E51445CF-1877-4051-A19A-267923015CC4Q36562153-2131C22B-70B7-4F62-91CD-6EB4230C9C51Q36842237-D588DEFF-C6B2-4E33-9AEC-948828795B94Q38993412-BADCDCBB-63D6-4338-AFCC-6B1FF8864773Q39815577-F0894E10-637F-495D-97AB-F553CFA824CDQ41900133-5ED2D7C3-3FF7-4574-AD77-A16809B5BC14Q41993762-362BD7C4-29BA-4AC7-8655-7F9F7192B5F6Q43160205-46F239BB-2013-4DA4-915E-8A434F333C73Q47902774-0D86DC19-7008-40BB-B1B1-B3FB632B22B8
P2860
The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils.
@en
type
label
The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils.
@en
prefLabel
The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils.
@en
P2093
P2860
P356
P1476
The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils.
@en
P2093
Annika Axelsson
Jens O Lagerstedt
Jitka Petrlova
Linda M Roberts
Matthias Mörgelin
Megan C Cochran
Trang Duong
P2860
P304
P356
10.1194/JLR.M020883
P577
2011-12-19T00:00:00Z