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References from Biophysical Insights into Implications of PEG-400 on the α-Crystallin Structure: Multispectroscopic and Microscopic Approach. Local targets link to admitted publications; unresolved targets remain external evidence.
Surgical interventions for age-related cataract
10.1016/j.ajo.2007.02.015 · 2007 · External reference
Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation
10.1074/jbc.m308203200 · 2004 · External reference
Cataract, Alzheimer’s disease, and other conformational diseases
10.1097/00055735-199802000-00003 · 1998 · External reference
Lens aging: effects of crystallins
10.1016/j.bbagen.2009.05.008 · 2009 · External reference
Alpha-crystallin can function as a molecular chaperone
10.1073/pnas.89.21.10449 · 1992 · External reference
Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin
10.1073/pnas.79.7.2360 · 1982 · External reference
Alpha B-crystallin is a small heat shock protein
10.1073/pnas.88.9.3652 · 1991 · External reference
Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
10.1093/emboj/16.2.221 · 1997 · External reference
Small heat shock proteins are molecular chaperones
10.1016/s0021-9258(18)53882-5 · 1993 · External reference
A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
10.1093/emboj/16.3.659 · 1997 · External reference
alpha A-crystallin is expressed in non-ocular tissues
10.1016/s0021-9258(18)50096-x · 1992 · External reference
Therapeutic potential of α-crystallin
10.1016/j.bbagen.2015.03.012 · 2016 · External reference
Structural and functional properties, chaperone activity and posttranslational modifications of alpha-crystallin and its related subunits in the crystalline lens: N-acetylcarnosine, carnosine and carcinine act as alpha-crystallin/small heat shock protein enhancers in prevention and dissolution of cataract in ocular drug delivery formulations of novel therapeutic agents
10.2174/187221112800672976 · 2012 · External reference
Direct Interaction between the β-Amyloid Core and Tau Facilitates Cross-Seeding: A Novel Target for Therapeutic Intervention
10.1021/acs.biochem.9b01087 · 2020 · External reference
Retinal toxicity of intravitreal polyethylene glycol 400
10.1089/jop.2015.0069 · 2016 · External reference
The ultraviolet fluorescence of proteins in neutral solution
10.1042/bj0760381 · 1960 · External reference
Lifetime distributions and anisotropy decays of indole fluorescence in cyclohexane/ethanol mixtures by frequency-domain fluorometry
10.1016/0301-4622(88)87005-4 · 1988 · External reference
Fluorescent protein FRET: the good, the bad and the ugly
10.1016/j.tibs.2007.08.003 · 2007 · External reference
Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates
10.1002/pro.5560040813 · 1995 · External reference
First evidence of formation of pre-molten globule state in myoglobin: A macromolecular crowding approach towards protein folding in vivo
10.1016/j.ijbiomac.2018.12.170 · 2019 · External reference
Glyoxal induced structural transition of buffalo kidney cystatin to molten globule and aggregates: Anti-fibrillation potency of quinic acid
10.1002/iub.1471 · 2016 · External reference
An insight into the biophysical characterization of insoluble collagen aggregates: implication for arthritis
10.1007/s10895-014-1424-x · 2014 · External reference
Aggregation as a consequence of glycation: insight into the pathogenesis of arthritis
10.1007/s00249-016-1119-0 · 2016 · External reference
Structural, functional and unfolding characteristics of glutathione S-transferase of Plasmodium vivax
10.1016/j.abb.2009.05.011 · 2009 · External reference
Thioflavin T as a molecular rotor: fluorescent properties of thioflavin T in solvents with different viscosity
10.1021/jp805822c · 2008 · External reference
The molecular chaperone, α-crystallin, inhibits amyloid formation by apolipoprotein C-II
10.1074/jbc.m105285200 · 2001 · External reference
Probing the interaction of human serum albumin with iprodione, a fungicide: spectroscopic and molecular docking insight
10.1080/07391102.2018.1442252 · 2019 · External reference
Extrinsic fluorescent dyes as tools for protein characterization
10.1007/s11095-007-9516-9 · 2008 · External reference
Correction: Deciphering Structural Intermediates and Genotoxic Fibrillar Aggregates of Albumins: A Molecular Mechanism Underlying for Degenerative Diseases
10.1371/annotation/04fa421f-3dfe-466a-8c21-17a7bab1494c · 2013 · External reference
Understanding the binding between Rosmarinic acid and serum albumin: In vitro and in silico insight
10.1016/j.molliq.2020.113348 · 2020 · External reference
Elucidation of dietary polyphenolics as potential inhibitor of microtubule affinity regulating kinase 4: in silico and in vitro studies
10.1038/s41598-017-09941-4 · 2017 · External reference
Structural and stability characteristics of a monothiol glutaredoxin: glutaredoxin-like protein 1 from Plasmodium falciparum
10.1016/j.bbapap.2008.03.012 · 2008 · External reference
Glyoxal Induced Transition of Transferrin to Aggregates: Spectroscopic, Microscopic and Molecular Docking Insight
10.2174/1389201020666190731122806 · 2019 · External reference
