Background Protein crystallins co me in three types (α, β and γ) and are found predominantly in the eye, and particularly in the lens, where they are packed into a compact …
γ-Crystallins constitute the major protein component in the nucleus of the vertebrate eye lens. Present at very high concentrations, they exhibit extreme solubility and thermodynamic …
RP Barnwal, E Loh, KS Godin, J Yip… - Nucleic acids …, 2016 - academic.oup.com
Neisseria meningitidis causes bacterial meningitis and septicemia. It evades the host complement system by upregulating expression of immune evasion factors in response to …
IR Booth, S Miller, A Müller, L Lehtovirta-Morley - Cell Calcium, 2015 - Elsevier
Mechanosensitive channels are ubiquitous and highly studied. However, the evolution of the bacterial channels remains enigmatic. It can be argued that mechanosensitivity might be a …
P Aravind, A Mishra, SK Suman, MK Jobby… - Biochemistry, 2009 - ACS Publications
The βγ-crystallin superfamily consists of evolutionarily related proteins with domain topology similar to lens β-and γ-crystallins, formed from duplicated Greek key motifs. Ca2+ binding …
This review examines both recent and historical literature related to the biophysical chemistry of the proteins in the ageing eye, with a particular focus on cataract development …
The βγ-crystallin superfamily contains both β-and γ-crystallins of the vertebrate eye lens and the microbial calcium-binding proteins, all of which are characterized by a common double …
SS Srivastava, A Mishra, B Krishnan… - Journal of Biological …, 2014 - ASBMB
βγ-Crystallin-type double clamp (N/D)(N/D) XX (S/T) S motif is an established but sparsely investigated motif for Ca 2+ binding. A βγ-crystallin domain is formed of two Greek key …
KS Ghosh, P Chauhan - … Protein Complexes II: Structure and Function, 2019 - Springer
The crystallins (α, β and γ), major constituent proteins of eye lens fiber cells play their critical role in maintaining the transparency and refractive index of the lens. Under different stress …