| scholarly article | Q13442814 |
| P2093 | author name string | K Krishna Sharma | |
| Puttur Santhoshkumar | |||
| Brian P Mooney | |||
| Rama Kannan | |||
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| Non-native protein aggregation kinetics | Q34664257 | ||
| Absence of low-molecular-weight alpha crystallin in nuclear region of old human lenses | Q35029980 | ||
| Understanding the α-crystallin cell membrane conjunction. | Q35633311 | ||
| Protein aggregation and amyloidosis: confusion of the kinds? | Q36376624 | ||
| Degradation of an old human protein: age-dependent cleavage of γS-crystallin generates a peptide that binds to cell membranes | Q36385933 | ||
| Conserved F84 and P86 residues in alphaB-crystallin are essential to effectively prevent the aggregation of substrate proteins | Q36458096 | ||
| Profiling of lens protease involved in generation of αA-66-80 crystallin peptide using an internally quenched protease substrate | Q36747988 | ||
| Functional elements in molecular chaperone alpha-crystallin: identification of binding sites in alpha B-crystallin | Q36887880 | ||
| Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activity | Q37042024 | ||
| Protein-protein interactions and lens transparency | Q37153581 | ||
| Principles, approaches, and challenges for predicting protein aggregation rates and shelf life | Q37236306 | ||
| Lens aging: effects of crystallins | Q37346358 | ||
| Protein aggregation--pathways and influencing factors | Q37699481 | ||
| Structural features and cytotoxicity of amyloid oligomers: implications in Alzheimer's disease and other diseases with amyloid deposits | Q37997321 | ||
| Deletion of (54)FLRAPSWF(61) residues decreases the oligomeric size and enhances the chaperone function of alphaB-crystallin | Q38922305 | ||
| Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions | Q39610788 | ||
| 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation | Q40113962 | ||
| Rapid refolding studies on the chaperone-like alpha-crystallin. Effect of alpha-crystallin on refolding of beta- and gamma-crystallins | Q41681266 | ||
| Human insoluble lens protein II. Isolation and characterization of a 9600 dalton polypeptide | Q41860225 | ||
| How aggregation and conformational scrambling of unfolded states govern fluorescence emission spectra | Q43079457 | ||
| Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure | Q43735123 | ||
| Changes in human lens proteins during nuclear cataract formation | Q43826494 | ||
| Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone | Q45232847 | ||
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| Human lens high-molecular-weight alpha-crystallin aggregates | Q47230734 | ||
| Identification of 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid binding sequences in alpha-crystallin | Q47982302 | ||
| Isotope-labeled cross-linkers and Fourier transform ion cyclotron resonance mass spectrometry for structural analysis of a protein/peptide complex | Q48511507 | ||
| C-Terminal truncation affects subunit exchange of human alphaA-crystallin with alphaB-crystallin. | Q53524194 | ||
| The cataract-causing mutation G98R in human alphaA-crystallin leads to folding defects and loss of chaperone activity. | Q54450888 | ||
| P433 | issue | 21 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 3638-3650 | |
| P577 | publication date | 2013-05-16 | |
| P1433 | published in | Biochemistry | Q764876 |
| P1476 | title | The αA66-80 peptide interacts with soluble α-crystallin and induces its aggregation and precipitation: a contribution to age-related cataract formation | |
| P478 | volume | 52 |
| Q40664616 | Age-related cleavages of crystallins in human lens cortical fiber cells generate a plethora of endogenous peptides and high molecular weight complexes. |
| Q35885459 | Lys-315 at the Interfaces of Diagonal Subunits of δ-Crystallin Plays a Critical Role in the Reversibility of Folding and Subunit Assembly |
| Q91609310 | Molecular Processes Implicated in Human Age-Related Nuclear Cataract |
| Q93193465 | RETRACTED: Peptide-induced formation of protein aggregates and amyloid fibrils in human and guinea pig αA-crystallins under physiological conditions of temperature and pH |
| Q27311458 | Role of αA-crystallin-derived αA66-80 peptide in guinea pig lens crystallin aggregation and insolubilization |
| Q38796772 | Small molecules, both dietary and endogenous, influence the onset of lens cataracts. |
| Q34118100 | The critical role of the central hydrophobic core (residues 71-77) of amyloid-forming αA66-80 peptide in α-crystallin aggregation: a systematic proline replacement study |
| Q38404383 | Therapeutic potential of α-crystallin |
| Q46423889 | Using chiral peptide substitutions to probe the structure function relationship of a key residue of Aβ42. |
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