Results 21 to 30 of about 15,579 (272)

Where Do You Get Your Protein? Or: Biochemical Realization [PDF]

open access: yes, 2020
Biochemical kinds such as proteins pose interesting problems for philosophers of science, as they can be studied from the points of view of both biology and chemistry.
Tahko, Tuomas E.
core   +3 more sources

Crystalline confinement [PDF]

open access: yesProceedings of 31st International Symposium on Lattice Field Theory LATTICE 2013 — PoS(LATTICE 2013), 2014
We show that exotic phases arise in generalized lattice gauge theories known as quantum link models in which classical gauge fields are replaced by quantum operators. While these quantum models with discrete variables have a finite-dimensional Hilbert space per link, the continuous gauge symmetry is still exact.
Banerjee D.   +3 more
openaire   +3 more sources

Therapeutic Potential of α-Crystallins in Retinal Neurodegenerative Diseases

open access: yesAntioxidants, 2021
The chaperone and anti-apoptotic activity of α-crystallins (αA- and αB-) and their derivatives has received increasing attention due to their tremendous potential in preventing cell death.
Ashutosh S. Phadte   +2 more
doaj   +1 more source

New insight into cataract formation -- enhanced stability through mutual attraction [PDF]

open access: yes, 2007
Small-angle neutron scattering experiments and molecular dynamics simulations combined with an application of concepts from soft matter physics to complex protein mixtures provide new insight into the stability of eye lens protein mixtures.
A. Stradner   +12 more
core   +2 more sources

αA-crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of α-crystallin and induces lens protein aggregation. [PDF]

open access: yesPLoS ONE, 2011
The eye lens is composed of fiber cells that are filled with α-, β- and γ-crystallins. The primary function of crystallins is to maintain the clarity of the lens through ordered interactions as well as through the chaperone-like function of α-crystallin.
Puttur Santhoshkumar   +2 more
doaj   +1 more source

Interaction of βA3-Crystallin with Deamidated Mutants of αA- and αB-Crystallins.

open access: yesPLoS ONE, 2015
Interaction among crystallins is required for the maintenance of lens transparency. Deamidation is one of the most common post-translational modifications in crystallins, which results in incorrect interaction and leads to aggregate formation.
Ekta Tiwary   +4 more
doaj   +1 more source

Strain-independent increases of crystallin proteins in the retina of type 1 diabetic rats. [PDF]

open access: yesPLoS ONE, 2013
Diabetic retinopathy is the leading cause of vision loss in working-age individuals in the United States and is expected to continue growing with the increased prevalence of diabetes. Streptozotocin-induced hyperglycemia in rats is the most commonly used
Erich A Heise   +5 more
doaj   +1 more source

Local variation in absolute water content of human and rabbit eye lenses measured by Raman microspectroscopy [PDF]

open access: yes, 1989
Raman spectra were obtained from fresh, fixed and sliced rabbit lenses and from human lens slices. For all lenses and lens slices the ratio R, defined as the Raman intensity at 3390 cm−1 divided by the Raman intensity at 2935 cm−1, was measured at ...
Bot, Annet C.C.   +4 more
core   +4 more sources

Analysis of the data on titration of native and peroxynitrite modified αA- and αB-crystallins by Cu2+-ions

open access: yesData in Brief, 2020
The interaction of αA- and αB-crystallins with Cu2+ ion modulates their structure and chaperone-like activity which is important for lens transparency. Theoretical analysis of the dependences of fluorescence intensity of native αA- and αB-crystallins and
Maryam Ghahramani   +4 more
doaj   +1 more source

Into the Light: Diurnality has Evolved Multiple Times in Geckos [PDF]

open access: yes, 2015
Geckos are the only major lizard group consisting mostly of nocturnal species. Nocturnality is presumed to have evolved early in gecko evolution and geckos possess numerous adaptations to functioning in low light and at low temperatures. However, not all
Bauer, Aaron M.   +3 more
core   +2 more sources

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