Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageing
about
Identification of the in vivo truncation sites at the C-terminal region of alpha-A crystallin from aged bovine and human lens.Extensive deamidation at asparagine residue 279 accounts for weak immunoreactivity of tau with RD4 antibody in Alzheimer's disease brain.Biochemistry of human alpha amylase isoenzymes.The ability of lens alpha crystallin to protect against heat-induced aggregation is age-dependent.Synthesis of alpha-crystallin by a cell line derived from the lens of a transgenic animal.Multiple sclerosis: an important role for post-translational modifications of myelin basic protein in pathogenesis.'Fast isoamylases' in parotid saliva of heterozygous carriers of cystic fibrosis.Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure.Site-specific racemization in aging alpha A-crystallin.Post-synthetic modifications of aldolase isozymes in rabbit lens during aging.Immunolocalization of the C-terminal and N-terminal regions of alpha-A and alpha-B crystallins.Immunological comparison of heat-shock proteins and alpha-crystallin.Domain structure and evolution in alpha-crystallins and small heat-shock proteins.Non-enzymatic glycation of α-crystallin as an in vitro model for aging, diabetes and degenerative diseases.
P2860
Q36787220-7DBBD0F7-5F59-43F3-B9DF-85E06E8ED295Q37485553-A135CE3E-37F5-4777-BC96-A40DE8B2D648Q38382049-EC86014C-866D-4701-944C-85AA922D195CQ41099392-5445B3BB-F2D5-46E1-996A-C3ACB4AC2391Q41752354-08FF101F-94C9-456D-824C-72BC48ED4FFFQ44495415-45D07316-6695-47CB-8E36-4CEB5B405356Q44670647-0C363582-367A-4F1E-862B-3A3FB513C15EQ44875494-EFFBD625-5ACD-4D2B-8361-E85922CAB4CBQ44924059-D61D3C91-6CC6-4095-88BF-59D2CED5DCAEQ48382699-6641E470-001D-42BA-9FD9-B11228E3D236Q52215990-6F649FBD-4422-4B0B-A854-5FAC06A559D9Q52458642-321E3702-C9D3-4528-8E12-FF155FE52FF8Q52466890-4A7625CE-972F-4435-AC32-D27B10908CDEQ53405754-5A68B6D8-0931-4014-8451-A748543E950C
P2860
Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageing
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature в листопаді 1975
@uk
name
Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageing
@en
Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageing
@nl
type
label
Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageing
@en
Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageing
@nl
prefLabel
Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageing
@en
Stepwise degradations and deamidation of the eye lens protein α-crystallin in ageing
@nl
P2093
P356
P1433
P1476
Stepwise degradations and deamidation of the eye lens protein alpha-crystallin in ageing
@en
P2093
F S Van Kleef
H J Hoenders
W W De Jong
P2888
P304
P356
10.1038/258264A0
P407
P577
1975-11-01T00:00:00Z
P6179
1018524077