250 related articles for article (PubMed ID: 32442520)
1. Asp isomerization increases aggregation of α-crystallin and decreases its chaperone activity in human lens of various ages.
Fujii N; Takata T; Kim I; Morishima K; Inoue R; Magami K; Matsubara T; Sugiyama M; Koide T
Biochim Biophys Acta Proteins Proteom; 2020 Sep; 1868(9):140446. PubMed ID: 32442520
[TBL] [Abstract][Full Text] [Related]
2. Characterization of alphaA-crystallin from high molecular weight aggregates in the normal human lens.
Fujii N; Awakura M; Takemoto L; Inomata M; Takata T; Fujii N; Saito T
Mol Vis; 2003 Jul; 9():315-22. PubMed ID: 12847419
[TBL] [Abstract][Full Text] [Related]
3. Isomerization of Asp residues plays an important role in αA-crystallin dissociation.
Takata T; Fujii N
FEBS J; 2016 Mar; 283(5):850-9. PubMed ID: 26700637
[TBL] [Abstract][Full Text] [Related]
4. Effect of Asp 96 isomerization on the properties of a lens αB-crystallin-derived short peptide.
Takata T; Fujii N
J Pharm Biomed Anal; 2015 Dec; 116():139-44. PubMed ID: 26188790
[TBL] [Abstract][Full Text] [Related]
5. Negative charge at aspartate 151 is important for human lens αA-crystallin stability and chaperone function.
Takata T; Matsubara T; Nakamura-Hirota T; Fujii N
Exp Eye Res; 2019 May; 182():10-18. PubMed ID: 30849387
[TBL] [Abstract][Full Text] [Related]
6. A rapid, comprehensive liquid chromatography-mass spectrometry (LC-MS)-based survey of the Asp isomers in crystallins from human cataract lenses.
Fujii N; Sakaue H; Sasaki H; Fujii N
J Biol Chem; 2012 Nov; 287(47):39992-40002. PubMed ID: 23007399
[TBL] [Abstract][Full Text] [Related]
7. Asp 58 modulates lens αA-crystallin oligomer formation and chaperone function.
Takata T; Nakamura-Hirota T; Inoue R; Morishima K; Sato N; Sugiyama M; Fujii N
FEBS J; 2018 Jun; 285(12):2263-2277. PubMed ID: 29676852
[TBL] [Abstract][Full Text] [Related]
8. Crystallins in water soluble-high molecular weight protein fractions and water insoluble protein fractions in aging and cataractous human lenses.
Harrington V; McCall S; Huynh S; Srivastava K; Srivastava OP
Mol Vis; 2004 Jul; 10():476-89. PubMed ID: 15303090
[TBL] [Abstract][Full Text] [Related]
9. Isomerization of aspartyl residues in crystallins and its influence upon cataract.
Fujii N; Takata T; Fujii N; Aki K
Biochim Biophys Acta; 2016 Jan; 1860(1 Pt B):183-91. PubMed ID: 26275494
[TBL] [Abstract][Full Text] [Related]
10. A single Asp isomer substitution in an αA-crystallin-derived peptide induces a large change in peptide properties.
Magami K; Kim I; Fujii N
Exp Eye Res; 2020 Mar; 192():107930. PubMed ID: 31931001
[TBL] [Abstract][Full Text] [Related]
11. The l-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation.
Warmack RA; Shawa H; Liu K; Lopez K; Loo JA; Horwitz J; Clarke SG
J Biol Chem; 2019 Aug; 294(32):12203-12219. PubMed ID: 31239355
[TBL] [Abstract][Full Text] [Related]
12. Differences in α-Crystallin isomerization reveal the activity of protein isoaspartyl methyltransferase (PIMT) in the nucleus and cortex of human lenses.
Lyon YA; Sabbah GM; Julian RR
Exp Eye Res; 2018 Jun; 171():131-141. PubMed ID: 29571628
[TBL] [Abstract][Full Text] [Related]
13. Influence of Lβ-, Dα- and Dβ-Asp isomers of the Asp-76 residue on the properties of αA-crystallin 70-88 peptide.
Fujii N; Fujii N; Kida M; Kinouchi T
Amino Acids; 2010 Nov; 39(5):1393-9. PubMed ID: 20437187
[TBL] [Abstract][Full Text] [Related]
14. Alpha B- and βA3-crystallins containing d-aspartic acids exist in a monomeric state.
Sakaue H; Takata T; Fujii N; Sasaki H; Fujii N
Biochim Biophys Acta; 2015 Jan; 1854(1):1-9. PubMed ID: 25450505
[TBL] [Abstract][Full Text] [Related]
15. The Aggregation of αB-Crystallin under Crowding Conditions Is Prevented by αA-Crystallin: Implications for α-Crystallin Stability and Lens Transparency.
Grosas AB; Rekas A; Mata JP; Thorn DC; Carver JA
J Mol Biol; 2020 Sep; 432(20):5593-5613. PubMed ID: 32827531
[TBL] [Abstract][Full Text] [Related]
16. Proteomic analysis of water insoluble proteins from normal and cataractous human lenses.
Harrington V; Srivastava OP; Kirk M
Mol Vis; 2007 Sep; 13():1680-94. PubMed ID: 17893670
[TBL] [Abstract][Full Text] [Related]
17. Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation.
Santhoshkumar P; Udupa P; Murugesan R; Sharma KK
J Biol Chem; 2008 Mar; 283(13):8477-85. PubMed ID: 18227073
[TBL] [Abstract][Full Text] [Related]
18. αA-crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of α-crystallin and induces lens protein aggregation.
Santhoshkumar P; Raju M; Sharma KK
PLoS One; 2011 Apr; 6(4):e19291. PubMed ID: 21552534
[TBL] [Abstract][Full Text] [Related]
19. Identification of Isomeric Aspartate residues in βB2-crystallin from Aged Human Lens.
Takata T; Murakami K; Toyama A; Fujii N
Biochim Biophys Acta Proteins Proteom; 2018 Jul; 1866(7):767-774. PubMed ID: 29654977
[TBL] [Abstract][Full Text] [Related]
20. The αA66-80 peptide interacts with soluble α-crystallin and induces its aggregation and precipitation: a contribution to age-related cataract formation.
Kannan R; Santhoshkumar P; Mooney BP; Sharma KK
Biochemistry; 2013 May; 52(21):3638-50. PubMed ID: 23631441
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]