[1] SRINIVAS P, NARAHARI A, PETRASH JM, et al. Importance of eye lens α-crystallin heteropolymer with 3:1 αA to αB ratio:stability, aggregation, and modifications[J]. IUBMB Life.2010, 62(9):693-702.
[2] PÉREZ S, DE SANCTIS D.Glycoscience@Synchrotron:synchrotron radiation applied to structural glycoscience[J]. Beilstein J Org Chem, 2017, 13:1145-1167.
[3] BORSHCHEVSKIY V, ROUND E, EROFEEV I, et al. Low-dose X-ray radiation induces structural alterations in proteins[J]. Acta Crystallogr D Biol Crystallogr, 2014, 70(Pt 10):2675-2685.
[4] BARENDS T R, FOUCAR L, BOTHA S, et al. De novo protein crystal structure determination from X-ray free-electron laser data[J]. Nature, 2014, 505(7482):244-247.
[5] YOUSAF T, DERVENOULAS G, POLITIS M.Advances in MRI methodology[J]. Int Rev Neurobiol, 2018, 141:31-76.
[6] MARKLEY J L.View from nuclear magnetic resonance spectroscopy[J]. Adv Exp Med Biol, 2018, 1105:19-22.
[7] CARVER J A, LINDNER R A.NMR spectroscopy of alpha-crystallin.Insights into the structure, interactions and chaperone action of small heat-shock proteins[J]. Int J Biol Macromol, 1998, 22(3-4):197-209.
[8] WU Z, DELAGLIO F, WYATT K, et al. Solution structure of (gamma) S-crystallin by molecular fragment replacement NMR[J]. Protein Sci, 2005, 14(12):3101-3114.
[9] FRANK J.Cryo-electron microscopy as an investigative tool:the ribosome as an example[J]. Bioessays, 2001, 23(8):725-732.
[10] BECK M, BAUMEISTER W.Cryo-electron tomography:can it reveal the molecular sociology of cells in atomic detail?[J] Trends Cell Biol, 2016, 26(11):825-837.
[11] ROH S H, HRYC C F, JEONG H H, et al. Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM[J]. Proc Natl Acad Sci U S A, 2017, 114(31):8259-8264.
[12] RENAUD J P, CHARI A, CIFERRI C, et al. Cryo-EM in drug discovery:achievements, limitations and prospects[J]. Nat Rev Drug Discov, 2018, 17(7):471-492.
[13] VÉNIEN-BRYAN C, LI Z, VUILLARD L, et al. Cryo-electron microscopy and X-ray crystallography:complementary approaches to structural biology and drug discovery[J]. Acta Crystallogr F Struct Biol Commun, 2017, 73(Pt 4):174-183.
[14] CRAMER P.Structural molecular biology-a personal reflection on the occasion of John Kendrew's 100th birthday[J]. J Mol Bio, 2017, 429(17):2603-2610.
[15] HASLBECK M, PESCHEK J, BUCHNER J, et al. Structure and function of α-crystallins:traversing from in vitro to in vivo[J]. Biochim Biophys Acta, 2016, 1860(1 Pt B):149-166.
[16] KUNDU M, SEN P C, DAS K P.Structure, stability, and chaperone function of alphaA-crystallin:role of N-terminal region[J]. Biopolymers, 2007, 86(3):177-192.
[17] LAGANOWSKY A, BENESCH J L, LANDAU M, et al. Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function[J]. Protein Sci, 2010, 19(5):1031-1043.
[18] SELIVANOVA O M, GALZITSKAYA O V.Structural and functional peculiarities of α-crystallin[J]. Biology (Basel), 2020, 9(4):85.
[19] KAISER C J O, PETERS C, SCHMID P W N, et al. The structure and oxidation of the eye lens chaperone αA-crystallin[J]. Nat Struct Mol Biol, 2019, 26(12):1141-1150.
[20] BRAUN N, ZACHARIAS M, PESCHEK J, et al. Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach[J]. Proc Natl Acad Sci U S A, 2011, 108(51):20491-20496.
[21] HALEY D A, HORWITZ J, STEWART P L.The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure[J]. J Mol Biol, 1998, 277(1):27-35.
[22] KHOSHAMAN K, YOUSEFI R, TAMADDON A M, et al. The impact of different mutations at Arg54 on structure, chaperone-like activity and oligomerization state of human αA-crystallin:The pathomechanism underlying congenital cataract-causing mutations R54L, R54P and R54C[J]. Biochim Biophys Acta Proteins Proteom, 2017, 1865(5):604-618.
[23] GHAHRAMANI M, YOUSEFI R, KRIVANDIN A, et al. Structural and functional characterization of D109H and R69C mutant versions of human αB-crystallin:the biochemical pathomechanism underlying cataract and myopathy development[J]. Int J Biol Macromol, 2020, 146:1142-1160.
[24] ANDLEY U P.Crystallins in the eye:function and pathology[J]. Prog Retin Eye Res, 2007, 26(1):78-98.
[25] VAN RENS G L, HOL F A, DE JONG W W, et al. Presence of hybridizing DNA sequences homologous to bovine acidic and basic beta-crystallins in all classes of vertebrates[J]. J Mol Evol, 1991, 33(5):457-463.
[26] BAX B, LAPATTO R, NALINI V, et al. X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins[J]. Nature, 1990, 347(6295):776-780.
[27] SMITH M A, BATEMAN O A, JAENICKE R, et al. Mutation of interfaces in domain-swapped human betaB2-crystallin[J]. Protein Sci, 2007, 16(4):615-625.
[28] XI Z, WHITLEY M J, GRONENBORN A M.Human βB2-crystallin forms a face-en-face dimer in solution:an integrated NMR and SAXS Study[J]. Structure, 2017, 25(3):496-505.
[29] BLUNDELL T, LINDLEY P, MILLER L, et al. The molecular structure and stability of the eye lens:x-ray analysis of gamma-crystallin Ⅱ[J]. Nature, 1981, 289(5800):771-717.
[30] SLINGSBY C, CLOUT N J.Structure of the crystallins[J]. Eye (Lond), 1999, 13(Pt 3b):395-402.
[31] PURKISS A G, BATEMAN O A, GOODFELLOW J M, et al. The X-ray crystal structure of human gamma S-crystallin C-terminal domain[J]. J Biol Chem, 2002, 277(6):4199-4205.
[32] VANITA V, SINGH J R, SINGH D, et al. Novel mutation in the gamma-S crystallin gene causing autosomal dominant cataract[J]. Mol Vis, 2009, 15:476-481.
[33] SPRAGUE-PIERCY M A, WONG E, ROSKAMP K W, et al. Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein[J]. Biochim Biophys Acta Gen Subj, 2020, 1864(3):129502.
[34] ZHU S, XI X B, DUAN T L, et al. The cataract-causing mutation G75V promotes γS-crystallin aggregation by modifying and destabilizing the native structure[J]. Int J Biol Macromol, 2018, 117:807-814.
[35] ZHAO L, CHEN X J, ZHU J, et al. Lanosterol reverses protein aggregation in cataracts[J]. Nature, 2015, 523(7562):607-611.
[36] LIN H, OUYANG H, ZHU J, et al. Lens regeneration using endogenous stem cells with gain of visual function[J]. Nature, 2016, 531(7594):323-328. |
