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Artykuły w czasopismach na temat „Β-crystallin”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 24 lipca 2025

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1

Belisle, E. H., S. W. Su, B. W. Lubit та S. C. J. Fu. "Homology among β-crystallins: Monoclonal antibodies to β-heavy crystallin". Current Eye Research 6, № 8 (1987): 951–57. http://dx.doi.org/10.3109/02713688709034866.

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Song, In-Kang, Seungjin Na, Eunok Paek та Kong-Joo Lee. "Cataract-Associated New Mutants S175G/H181Q of βΒ2-Crystallin and P24S/S31G of γD-Crystallin Are Involved in Protein Aggregation by Structural Changes". International Journal of Molecular Sciences 21, № 18 (2020): 6504. http://dx.doi.org/10.3390/ijms21186504.

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β/γ-Crystallins, the main structural protein in human lenses, have highly stable structure for keeping the lens transparent. Their mutations have been linked to cataracts. In this study, we identified 10 new mutations of β/γ-crystallins in lens proteomic dataset of cataract patients using bioinformatics tools. Of these, two double mutants, S175G/H181Q of βΒ2-crystallin and P24S/S31G of γD-crystallin, were found mutations occurred in the largest loop linking the distant β-sheets in the Greek key motif. We selected these double mutants for identifying the properties of these mutations, employing

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3

Saranya, Pandi, Madhu Shekhar, Aravind Haripriya, Veerappan Muthukkaruppan, and Chidambaranathan Gowri Priya. "Towards the Identification and Characterization of Putative Adult Human Lens Epithelial Stem Cells." Cells 12, no. 23 (2023): 2727. http://dx.doi.org/10.3390/cells12232727.

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The anterior lens epithelium has the ability to differentiate into lens fibres throughout its life. The present study aims to identify and functionally characterize the adult stem cells in the human lens epithelium. Whole mounts of lens epithelium from donor eyes (normal/cataract) were immunostained for SOX2, gap junction protein alpha 1 (GJA1), PAX6, α, β and γ-crystallins, followed by a confocal analysis. The functional property of adult stem cells was analysed by their sphere forming ability using cultured lens epithelial cells from different zones. Based on marker expression, the lens epit

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4

Hejtmancik, J. F., P. T. Wingfield та Y. V. Sergeev. "β-Crystallin association". Experimental Eye Research 79, № 3 (2004): 377–83. http://dx.doi.org/10.1016/j.exer.2004.06.011.

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Serebryany, Eugene, Rachel W. Martin та Gemma R. Takahashi. "The Functional Significance of High Cysteine Content in Eye Lens γ-Crystallins". Biomolecules 14, № 5 (2024): 594. http://dx.doi.org/10.3390/biom14050594.

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Cataract disease is strongly associated with progressively accumulating oxidative damage to the extremely long-lived crystallin proteins of the lens. Cysteine oxidation affects crystallin folding, interactions, and light-scattering aggregation especially strongly due to the formation of disulfide bridges. Minimizing crystallin aggregation is crucial for lifelong lens transparency, so one might expect the ubiquitous lens crystallin superfamilies (α and βγ) to contain little cysteine. Yet, the Cys content of γ-crystallins is well above the average for human proteins. We review literature relevan

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6

James, M., та C. Crabbe. "Partial sequence homologies between cytoskeletal proteins, c-myc, Rous sarcoma virus and adenovirus proteins, transducin, and β- and γ-crystallins". Bioscience Reports 5, № 2 (1985): 167–74. http://dx.doi.org/10.1007/bf01117063.

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Computer based sequence comparisons indicate partial sequence homology between human c-myc, Rous sarcoma virus, adenovirus 7, and simian sarcoma virus proteins and the cytoskeletal proteins desmin, keratin and vimentin. In addition, sections of the oncogene proteins showed partial but significant homology to α and β subunits of transducin, γ-II and β-BP crystallins showed partial but significant homology to the cytoskeletal proteins keratin, vimentin, desmin, α and β-tubulin, and to adenovirus 7 and simian sarcoma virus transforming gene proteins. β-BP crystallin showed partial but significant

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7

Joseph, Roy, Michael L. Robinson, Laura Lambert та Om P. Srivastava. "Lens-specific βA3/A1-conditional knockout mice: Phenotypic characteristics and calpain activation causing protein degradation and insolubilization". PLOS ONE 18, № 3 (2023): e0281386. http://dx.doi.org/10.1371/journal.pone.0281386.

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βA3/A1-crystallin is a lens structural protein that plays an important role in maintaining lens transparency via interactions with other crystallins. While the function of βA3/A1-crystallin in the retina is well studied, its functions in the lens, other than as a structural protein, remain unclear. In the current study, we generated the lens-specific βA3/A1-crystallin conditional knockout mouse (named βA3/A1ckO) and explored phenotypic changes and the function of the crystallin in the lens. The βA3/A1ckO mice showed congenital cataract at birth and exhibited truncation of lens proteins. Severa

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8

Feng, Jinhua, David L. Smith та Jean B. Smith. "Human Lens β-Crystallin Solubility". Journal of Biological Chemistry 275, № 16 (2000): 11585–90. http://dx.doi.org/10.1074/jbc.275.16.11585.

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9

Khadka, Nawal K., Preston Hazen, Dieter Haemmerle та Laxman Mainali. "Interaction of βL- and γ-Crystallin with Phospholipid Membrane Using Atomic Force Microscopy". International Journal of Molecular Sciences 24, № 21 (2023): 15720. http://dx.doi.org/10.3390/ijms242115720.

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Highly concentrated lens proteins, mostly β- and γ-crystallin, are responsible for maintaining the structure and refractivity of the eye lens. However, with aging and cataract formation, β- and γ-crystallin are associated with the lens membrane or other lens proteins forming high-molecular-weight proteins, which further associate with the lens membrane, leading to light scattering and cataract development. The mechanism by which β- and γ-crystallin are associated with the lens membrane is unknown. This work aims to study the interaction of β- and γ-crystallin with the phospholipid membrane wit

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10

Pan, F. M., W. C. Chang, S. F. Lu, A. L. Hsu та S. H. Chiou. "Sequence Analysis of One Major Basic β-Crystallin (β-Bp) of Amphibian Lenses - Evolutionary Comparison and Phylogenetic Relatedness Between β-Crystallin and γ-Crystallin". Biochemical and Biophysical Research Communications 217, № 3 (1995): 940–49. http://dx.doi.org/10.1006/bbrc.1995.2861.

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11

Leng, Xiao-Yao, Hai-Yun Li, Jing Wang, Liang-Bo Qi, Yi-Bo Xi та Yong-Bin Yan. "Congenital microcornea-cataract syndrome-causing mutation X253R increases βB1-crystallin hydrophobicity to promote aggregate formation". Biochemical Journal 473, № 14 (2016): 2087–96. http://dx.doi.org/10.1042/bcj20160247.

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The high solubility and lifelong stability of crystallins are crucial to the maintenance of lens transparency and optical properties. Numerous crystallin mutations have been linked to congenital cataract, which is one of the leading causes of newborn blindness. Besides cataract, several crystallin mutations have also been linked to syndromes such as congenital microcornea-cataract syndrome (CMCC). However, the molecular mechanism of CMCC caused by crystallin mutations remains elusive. In the present study, we investigated the mechanism of CMCC caused by the X253R mutation in βB1-crystallin. Th

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12

Hazen, Preston, Geraline Trossi-Torres, Nawal K. Khadka, Raju Timsina та Laxman Mainali. "Binding of βL-Crystallin with Models of Animal and Human Eye Lens-Lipid Membrane". International Journal of Molecular Sciences 24, № 17 (2023): 13600. http://dx.doi.org/10.3390/ijms241713600.

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Several discoveries show that with age and cataract formation, β-crystallin binds with the lens membrane or associates with other lens proteins, which bind with the fiber cell plasma membrane, accompanied by light scattering and cataract formation. However, how lipids (phospholipids and sphingolipids) and cholesterol (Chol) influence β-crystallin binding to the membrane is unclear. This research aims to elucidate the role of lipids and Chol in the binding of β-crystallin to the membrane and the membrane’s physical properties (mobility, order, and hydrophobicity) with β-crystallin binding. We u

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13

Sun, Jiayue, Toshiya Matsubara, Tamaki Koide, Kirsten J. Lampi, Larry L. David та Takumi Takata. "Characterization of different-sized human αA-crystallin homomers and implications to Asp151 isomerization". PLOS ONE 19, № 7 (2024): e0306856. http://dx.doi.org/10.1371/journal.pone.0306856.

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Site-specific modifications of aspartate residues spontaneously occur in crystallin, the major protein in the lens. One of the primary modification sites is Asp151 in αA-crystallin. Isomerization and racemization alter the crystallin backbone structure, reducing its stability by inducing abnormal crystallin–crystallin interactions and ultimately leading to the insolubilization of crystallin complexes. These changes are considered significant factors in the formation of senile cataracts. However, the mechanisms driving spontaneous isomerization and racemization have not been experimentally demo

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14

Raman, Bakthisaran, Tadato Ban, Miyo Sakai та ін. "αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid β-peptide and β2-microglobulin". Biochemical Journal 392, № 3 (2005): 573–81. http://dx.doi.org/10.1042/bj20050339.

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αB-crystallin, a small heat-shock protein, exhibits molecular chaperone activity. We have studied the effect of αB-crystallin on the fibril growth of the Aβ (amyloid β)-peptides Aβ-(1–40) and Aβ-(1–42). αB-crystallin, but not BSA or hen egg-white lysozyme, prevented the fibril growth of Aβ-(1–40), as revealed by thioflavin T binding, total internal reflection fluorescence microscopy and CD spectroscopy. Comparison of the activity of some mutants and chimaeric α-crystallins in preventing Aβ-(1–40) fibril growth with their previously reported chaperone ability in preventing dithiothreitol-induce

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15

Leng, Xiao-Yao, Sha Wang, Ni-Qian Cao, Liang-Bo Qi та Yong-Bin Yan. "The N-Terminal Extension of βB1-Crystallin Chaperones β-Crystallin Folding and Cooperates with αA-Crystallin". Biochemistry 53, № 15 (2014): 2464–73. http://dx.doi.org/10.1021/bi500146d.

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16

Wang, Sha, Xiao-Yao Leng та Yong-Bin Yan. "The Benefits of Being β-Crystallin Heteromers: βB1-Crystallin Protects βA3-Crystallin against Aggregation during Co-refolding". Biochemistry 50, № 48 (2011): 10451–61. http://dx.doi.org/10.1021/bi201375p.

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17

Xing, Yan, Shan Liang, Yuanyuan Zhao, Shuo Yang, He Ni, and Haihang Li. "Protection of Aronia melanocarpa Fruit Extract from Sodium-Iodate-Induced Damages in Rat Retina." Nutrients 13, no. 12 (2021): 4411. http://dx.doi.org/10.3390/nu13124411.

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Age-related macular degeneration (AMD) is one of the major causes of blindness in elderly populations. However, the dry form of AMD has lack of effective treatments. The fruits of Aronia melanocarpa are rich in anthocyanins. In this study, the protective effects of aronia fruit extract on rat retina were investigated using a NaIO3-induced dry AMD model. Full-field electroretinograms (ERGs) showed that b-wave amplitudes were significantly decreased and the retina structures were disordered in the model. The extract treatment alleviated the injuries. The b-wave amplitudes increased 61.5% in Scot

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18

Jiang, Y. J., S. H. Chiou та W. C. Chang. "Lens crystallin changes associated with amphibian metamorphosis: Involvement of a β-crystallin polypeptide". Biochemical and Biophysical Research Communications 164, № 3 (1989): 1423–30. http://dx.doi.org/10.1016/0006-291x(89)91829-9.

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19

Lu, Shao-Fan, Fu-Ming Pan та Shyh-Horng Chiou. "Sequence Analysis of Four Acidic β-Crystallin Subunits of Amphibian Lenses: Phylogenetic Comparison between β- and γ-Crystallins". Biochemical and Biophysical Research Communications 221, № 2 (1996): 219–28. http://dx.doi.org/10.1006/bbrc.1996.0577.

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20

Kase, Satoru, Shikun He, Shozo Sonoda та ін. "αB-crystallin regulation of angiogenesis by modulation of VEGF". Blood 115, № 16 (2010): 3398–406. http://dx.doi.org/10.1182/blood-2009-01-197095.

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Abstract αB-crystallin is a chaperone belonging to the small heat shock protein family. Herein we show attenuation of intraocular angiogenesis in αB-crystallin knockout (αB-crystallin−/−) mice in 2 models of intraocular disease: oxygen-induced retinopathy and laser-induced choroidal neovascularization. Vascular endothelial growth factor A (VEGF-A) mRNA and hypoxia inducible factor-1α protein expression were induced during retinal angiogenesis, but VEGF-A protein expression remained low in αB-crystallin−/− retina versus wild-type mice, whereas VEGF-R2 expression was not affected. Both αB-crysta

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21

Liang, Jack J. N. "Interaction between β-amyloid and lens αB-crystallin". FEBS Letters 484, № 2 (2000): 98–101. http://dx.doi.org/10.1016/s0014-5793(00)02136-0.

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22

Wu, Fang, Liangkai Cheng, Qi Yu, Lin Zhang, Hong Li та Caiyan Wang. "Purification and Functional Characterization of the C-Terminal Domain of the β-Actin-Binding Protein AIM1 In Vitro". Molecules 23, № 12 (2018): 3281. http://dx.doi.org/10.3390/molecules23123281.

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The protein absent in melanoma 1 (AIM1) is a member of the βγ-crystal lens superfamily that is associated with the development of multiple cancers. The binding of AIM1 to β-actin affects the migration and invasion of prostate cancer epithelial cells. The C-terminus of AIM1 is required for the β-actin interaction. However, the characteristics of AIM1 in vitro and the interaction mode between AIM1 and β-actin remain unknown. We describe novel methods to prepare pure recombinant AIM1 and identify possible binding modes between AIM1 and β-actin; we also obtain the crystal of the first two βγ-cryst

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23

YAN, Hong, Antony C. WILLIS та John J. HARDING. "γIII-Crystallin is the primary target of glycation in the bovine lens incubated under physiological conditions". Biochemical Journal 374, № 3 (2003): 677–85. http://dx.doi.org/10.1042/bj20030542.

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Several mechanisms have been proposed for the way in which glucose and its metabolites cause cataract, retinopathy and other complications of diabetes, the most convincing being glycation. Glycation, the reaction of sugars with free amino groups of proteins, is one of a variety of non-enzymic post-translational modifications. The aim of the present study was to identify some of the most reactive proteins in the lens when incubated under physiological conditions. Fresh intact bovine lenses were incubated with [14C]glucose in a conventional tissue-culture medium with added antibiotics. After 3 a

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24

Feil, Ingeborg K., Marc Malfois, Jörg Hendle, Hans van der Zandt та Dmitri I. Svergun. "A Novel Quaternary Structure of the Dimeric α-Crystallin Domain with Chaperone-like Activity". Journal of Biological Chemistry 276, № 15 (2001): 12024–29. http://dx.doi.org/10.1074/jbc.m010856200.

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αB-crystallin, a member of the small heat-shock protein family and a major eye lens protein, is a high molecular mass assembly and can act as a molecular chaperone. We report a synchrotron radiation x-ray solution scattering study of a truncation mutant from the human αB-crystallin (αB57–157), a dimeric protein that comprises the α-crystallin domain of the αB-crystallin and retains a significant chaperone-like activity. According to the sequence analysis (more than 23% identity), the monomeric fold of the α-crystallin domain should be close to that of the small heat-shock protein fromMethanoco

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25

Flokis, Mary, та Frank J. Lovicu. "FGF-2 Differentially Regulates Lens Epithelial Cell Behaviour during TGF-β-Induced EMT". Cells 12, № 6 (2023): 827. http://dx.doi.org/10.3390/cells12060827.

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Fibroblast growth factor (FGF) and transforming growth factor-beta (TGF-β) can regulate and/or dysregulate lens epithelial cell (LEC) behaviour, including proliferation, fibre differentiation, and epithelial–mesenchymal transition (EMT). Earlier studies have investigated the crosstalk between FGF and TGF-β in dictating lens cell fate, that appears to be dose dependent. Here, we tested the hypothesis that a fibre-differentiating dose of FGF differentially regulates the behaviour of lens epithelial cells undergoing TGF-β-induced EMT. Postnatal 21-day-old rat lens epithelial explants were treated

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26

Sudipa, Saha, та P. Das K. "Hydrophobicity of α-crystallin and its relationship with chaperone activitybis-ANS binding study". Journal of Indian Chemical Society Vol. 94, Sep 2017 (2017): 959–70. https://doi.org/10.5281/zenodo.5636995.

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Department of Biotechnology, St. Xavier’s College, Kolkata-700 016, India <em>E-mail</em> : sahasudipa74@yahoo.co.in Department of Chemistry, Bose Institute, Kolkata-700 009, India E-mail : kalipada@jcboseinst.ac.in, daskp25@gmail.com <em>Manuscript received 04 May 2017, accepted 15 June 2017</em> <em>α</em>-Crystallin is the major structural protein of eye lens of vertebrates. The temperature driven exposure of hydrophobic surfaces in <em>α</em>-crystallin was accompanied by enhancement in chaperone activity. We have used bis-ANS and ANS binding to understand some structural

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27

Stege, G. J. J., K. Renkawek, P. S. G. Overkamp та ін. "The Molecular Chaperone αB-crystallin Enhances Amyloid β Neurotoxicity". Biochemical and Biophysical Research Communications 262, № 1 (1999): 152–56. http://dx.doi.org/10.1006/bbrc.1999.1167.

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CRAGHILL, Jane, Andrew D. CRONSHAW, and John J. HARDING. "The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens." Biochemical Journal 379, no. 3 (2004): 595–600. http://dx.doi.org/10.1042/bj20031367.

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The glutathionylation of human lens proteins was examined by Western-blot analysis with an anti-GSH antibody and scanning. Several different glutathionylated proteins were observed, and a 47 kDa band was of particular interest. This band did not appear after SDS/PAGE under reducing conditions, suggesting that it was a glutathionylated fraction. The 47 kDa band was found principally in the outer part of the lens, the cortex, but not in the lens nucleus where older proteins are present. The 47 kDa component was composed of βB1-, βB2- and γS-crystallin, with the γS-crystallin having glutathione b

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Kretschmar, M., E. M. Mayr, and R. Jaenicke. "Homo-Dimeric Spherulin 3a: A Single-Domain Member of the bg-Crystallin Superfamily." Biological Chemistry 380, no. 1 (1999): 89–94. http://dx.doi.org/10.1515/bc.1999.012.

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Abstract The βγ-crystallin superfamily of eye lens proteins comprises a class of structurally related members with a wide variety of different functions. Common features of these proteins are 1. the Greek-key motif of antiparallel β-sheets, called the crystallin fold, and 2. the high intrinsic long-term stability. Spherulin 3a (S3a), a dormant protein from the spherules of Physarum polycephalum, is the only known single-domain protein within the βγ-crystallin family. Based on sequence homology and ‘domain swapping’, it has been proposed to represent an evolutionary ancestor of present-day eye

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Shinkai, Yasuhiro, Yunjie Ding, Takashi Miura та Yoshito Kumagai. "Aggregation of β-crystallin through covalent binding to 1,2-naphthoquinone is rescued by α-crystallin chaperone". Journal of Toxicological Sciences 45, № 1 (2020): 37–43. http://dx.doi.org/10.2131/jts.45.37.

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Reddy, G. Bhanuprakash, P. Yadagiri Reddy, and Avadhesha Surolia. "Alzheimer’s and Danish dementia peptides induce cataract and perturb retinal architecture in rats." Biomolecular Concepts 8, no. 1 (2017): 45–84. http://dx.doi.org/10.1515/bmc-2016-0025.

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AbstractFamilial Danish dementias (FDDs) are autosomal dominant neurodegenerative disorders that are associated with visual defects. In some aspects, FDD is similar to Alzheimer’s disease (AD)– the amyloid deposits in FDD and AD are made of short peptides: amyloid β (Aβ) in AD and ADan in FDD. Previously, we demonstrated an interaction between the dementia peptides and α-crystallin leading to lens opacification in organ culture due to impaired chaperone activity of α-crystallin. Herein, we report the in vivo effects of ADan and Aβ on the eye. ADan [reduced (ADan-red) and oxidized (ADan-oxi)] a

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Duncan, Melinda K., John I. Haynes, Ales Cvekl та Joram Piatigorsky. "Dual Roles for Pax-6: a Transcriptional Repressor of Lens Fiber Cell-Specific β-Crystallin Genes". Molecular and Cellular Biology 18, № 9 (1998): 5579–86. http://dx.doi.org/10.1128/mcb.18.9.5579.

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ABSTRACT It has been demonstrated previously that Pax-6, a paired domain (PD)/homeodomain (HD) transcription factor critical for eye development, contributes to the activation of the αB-, αA-, δ1-, and ζ-crystallin genes in the lens. Here we have examined the possibility that the inverse relationship between the expression of Pax-6 and β-crystallin genes within the developing chicken lens reflects a negative regulatory role of Pax-6. Cotransfection of a plasmid containing the βB1-crystallin promoter fused to the chloramphenicol acetyltransferase reporter gene and a plasmid containing the full-

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Chen, Jyh-Yih, Bei-En Chang, Yi-Hsuan Chen, Cliff Ji-Fan Lin, Jen-Leih Wu та Ching-Ming Kuo. "Molecular Cloning, Developmental Expression, and Hormonal Regulation of Zebrafish (Danio rerio) β Crystallin B1, a Member of the Superfamily of β Crystallin Proteins". Biochemical and Biophysical Research Communications 285, № 1 (2001): 105–10. http://dx.doi.org/10.1006/bbrc.2001.5099.

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Kroone, R. C., G. S. Elliott, A. Ferszt, C. Slingsby, N. H. Lubsen та J. G. G. Schoenmakers. "The role of the sequence extensions in β-crystallin assembly". "Protein Engineering, Design and Selection" 7, № 11 (1994): 1395–99. http://dx.doi.org/10.1093/protein/7.11.1395.

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Hejtmancik, J. F., P. T. Wingfield та Y. V. Sergeev. "β-Crystallin association [Experimental Eye Research 79 (2004) 377–383]". Experimental Eye Research 79, № 6 (2004): 785. http://dx.doi.org/10.1016/s0014-4835(04)00303-3.

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Siezen, Roland J., Robert D. Anello та John A. Thomson. "Interactions of lens proteins. Concentration dependence of β-crystallin aggregation". Experimental Eye Research 43, № 3 (1986): 293–303. http://dx.doi.org/10.1016/s0014-4835(86)80067-7.

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Lapatto, R., V. Nalini, B. Bax та ін. "High resolution structure of an oligomeric eye lens β-crystallin". Journal of Molecular Biology 222, № 4 (1991): 1067–83. http://dx.doi.org/10.1016/0022-2836(91)90594-v.

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Srinivas, P. N. B. S., P. Yadagiri Reddy та G. Bhanuprakash Reddy. "Significance of α-crystallin heteropolymer with a 3:1 αA/αB ratio: chaperone-like activity, structure and hydrophobicity". Biochemical Journal 414, № 3 (2008): 453–60. http://dx.doi.org/10.1042/bj20080544.

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The small heat-shock protein α-crystallin isolated from the eye lens exists as a large (700 kDa) heteropolymer composed of two subunits, αA and αB, of 20 kDa each. Although trace amounts of αA-crystallin are found in other tissues, non-lenticular distribution of α-crystallin is dominated by the αB homopolymer. In most vertebrate lens, the molar ratio of αA to αB is generally 3:1. However, the importance of this ratio in the eye lens is not known. In the present study, we have investigated the physiological significance of the 3:1 ratio by determining the secondary/tertiary structure, hydrophob

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Herzog, Rebecca, Juan Manuel Sacnun, Guadalupe González-Mateo та ін. "Lithium preserves peritoneal membrane integrity by suppressing mesothelial cell αB-crystallin". Science Translational Medicine 13, № 608 (2021): eaaz9705. http://dx.doi.org/10.1126/scitranslmed.aaz9705.

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Life-saving renal replacement therapy by peritoneal dialysis (PD) is limited in use and duration by progressive impairment of peritoneal membrane integrity and homeostasis. Preservation of peritoneal membrane integrity during chronic PD remains an urgent but long unmet medical need. PD therapy failure results from peritoneal fibrosis and angiogenesis caused by hypertonic PD fluid (PDF)–induced mesothelial cytotoxicity. However, the pathophysiological mechanisms involved are incompletely understood, limiting identification of therapeutic targets. We report that addition of lithium chloride (LiC

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Macdonald, James T., Andrew G. Purkiss, Myron A. Smith, Paul Evans, Julia M. Goodfellow та Christine Slingsby. "Unfolding crystallins: The destabilizing role of a β-hairpin cysteine in βB2-crystallin by simulation and experiment". Protein Science 14, № 5 (2005): 1282–92. http://dx.doi.org/10.1110/ps.041227805.

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Maiti, Motilal, Masahiro Kono та Bireswar Chakrabarti. "Heat-induced changes in the conformation of α- and β-crystalline: Unique thermal stability of α-crystallin". FEBS Letters 236, № 1 (1988): 109–14. http://dx.doi.org/10.1016/0014-5793(88)80295-3.

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Chiou, Shyh-Horng, Fu-Ming Pan, Hsuan-Wan Peng, Yen-Kai Chao та Wen-Chang Chang. "Characterization of γS-Crystallin Isoforms from a Catfish: Evolutionary Comparison of Various γ-, γS-, and β-Crystallins". Biochemical and Biophysical Research Communications 252, № 2 (1998): 412–19. http://dx.doi.org/10.1006/bbrc.1998.9657.

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Liedtke, Thomas, Jens Christian Schwamborn, Uwe Schröer та Solon Thanos. "Elongation of Axons during Regeneration Involves Retinal Crystallin β b2 (crybb2)". Molecular & Cellular Proteomics 6, № 5 (2007): 895–907. http://dx.doi.org/10.1074/mcp.m600245-mcp200.

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Coop, Audrey, Kirsten E. H. Wiesmann та M. James C. Crabbe. "Translocation of β crystallin in neural cells in response to stress". FEBS Letters 431, № 3 (1998): 319–21. http://dx.doi.org/10.1016/s0014-5793(98)00783-2.

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Bateman, O. A., R. Sarra, S. T. van Genesen, G. Kappé, N. H. Lubsen та C. Slingsby. "The stability of human acidic β-crystallin oligomers and hetero-oligomers". Experimental Eye Research 77, № 4 (2003): 409–22. http://dx.doi.org/10.1016/s0014-4835(03)00173-8.

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Wang, Kai Jie. "Novel β-Crystallin Gene Mutations in Chinese Families With Nuclear Cataracts". Archives of Ophthalmology 129, № 3 (2011): 337. http://dx.doi.org/10.1001/archophthalmol.2011.11.

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Pan, Fu-Ming, Ming-Hong Chuang та Shyh-Horng Chiou. "Characterization of γS-Crystallin Isoforms from Lip Shark (Chiloscyllium colax): Evolutionary Comparison between γS and β/γ Crystallins". Biochemical and Biophysical Research Communications 240, № 1 (1997): 51–56. http://dx.doi.org/10.1006/bbrc.1997.7600.

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Kenworthy, Anne K., Alan D. Magid, Timothy N. Oliver та Thomas J. McIntosh. "Colloid Osmotic Pressure of Steer and β-Crystallins: Possible Functional Roles for Lens Crystallin Distribution and Structural Diversity". Experimental Eye Research 59, № 1 (1994): 11–30. http://dx.doi.org/10.1006/exer.1994.1077.

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Koh, Timothy J., and Joel Escobedo. "Cytoskeletal disruption and small heat shock protein translocation immediately after lengthening contractions." American Journal of Physiology-Cell Physiology 286, no. 3 (2004): C713—C722. http://dx.doi.org/10.1152/ajpcell.00341.2003.

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The purposes of this study were to determine whether, immediately after lengthening contractions, 1) levels of specific force-transmitting cytoskeletal elements are reduced in skeletal muscle cells and 2) cytosolic small heat shock proteins (HSPs) translocate to structures prone to disruption. Western blot analysis demonstrated decreased concentrations of z-disk proteins α-actinin and plectin and membrane scaffolding proteins dystrophin and β-spectrin in muscle exposed to lengthening contractions compared with contralateral control muscle. Lengthening contractions also resulted in immediate tr

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Ryan, Philip, Andy Hsien Wei Koh, Anna Elizabeth Lohning, and Santosh Rudrawar. "Solid-Phase O-Glycosylation with a Glucosamine Derivative for the Synthesis of a Glycopeptide." Australian Journal of Chemistry 70, no. 10 (2017): 1151. http://dx.doi.org/10.1071/ch17201.

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An efficient synthesis of the O-linked glycosylamino acid Fmoc–l-Ser((Ac)3–β-d-GlcNAc)-OH building block is described. The utility of the method was demonstrated with direct solid-phase O-glycosylation of the hydroxyl group on the amino acid (Ser) side chain of a human α-A crystallin-derived peptide (AIPVSREEK) in nearly quantitative glycosylation yield.

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