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Using Schematic Models to Understand the Microscopic Basis for Inverted Solubility in γD-Crystallin | The Journal of Physical Chemistry B
IJMS | Free Full-Text | Insights to Human γD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations | HTML
Lysine and Arginine Content of Proteins: Computational Analysis Suggests a New Tool for Solubility Design | Molecular Pharmaceutics
Crystal cataracts: Human genetic cataract caused by protein crystallization | PNAS
Lanosterol Disrupts Aggregation of Human γD-Crystallin by Binding to the Hydrophobic Dimerization Interface | Journal of the American Chemical Society
Asparagus – Casanatura Vivaio
Detection of Protein-Protein Interactions among Lens Crystallins in a Mammalian Two-hybrid System Assay* - Journal of Biological Chemistry
Cumulative deamidations of the major lens protein γS‐crystallin increase its aggregation during unfolding and oxidation - Vetter - 2020 - Protein Science - Wiley Online Library
Congenital cataract: a guide to genetic and clinical management - Suzannah J. Bell, Ngozi Oluonye, Philippa Harding, Mariya Moosajee, 2020
Molecular Modeling: A Search for a Calpain Inhibitor as a New Treatment for Cataractogenesis | Journal of Medicinal Chemistry
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Crystal structure of the cataract‐causing P23T γD‐crystallin mutant - Ji - 2013 - Proteins: Structure, Function, and Bioinformatics - Wiley Online Library
Full article: World occurrence and related problems caused by Megninia ginglymura (Mégnin) (Acari: Analgidae) in commercial poultry farms – a review
Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants - ScienceDirect
Annales des Sciences Naturelles. Zoologia; biologia. 328 EUG. DAOAY DE DEES supra processu aculeiformi Yalidiusculo, antrorsumvergente; in parte qiiarta marginis interioris carina rotundata parum pro- miiiente et prope apicem iii margine
Page:Macovei-Dictionario Encyclopedic de Interlingua-1 de 4.pdf/36 - Wikisource
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A novel locus of coralliform cataract mapped to chromosome 2p24-pter | Journal of Human Genetics
IJMS | Free Full-Text | Cataract-Associated New Mutants S175G/H181Q of βΒ2-Crystallin and P24S/S31G of γD-Crystallin Are Involved in Protein Aggregation by Structural Changes | HTML
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Plants | Free Full-Text | Integrative Taxonomic, Ecological and Genotyping Study of Charophyte Populations from the Egyptian Western-Desert Oases and Sinai Peninsula | HTML
Role of Conformational Flexibility in Monte Carlo Simulations of Many-Protein Systems | Journal of Chemical Theory and Computation
Surface Exposed Free Cysteine Suppresses Crystallization of Human γD-Crystallin - ScienceDirect
An alternative structural isoform in amyloid‐like aggregates formed from thermally denatured human γD‐crystallin - Moran - 2014 - Protein Science - Wiley Online Library