ArticleProtein science : a publication of the Protein Society2005
Solution structure of (gamma)S-crystallin by molecular fragment replacement NMR.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains.Biophysical journal · 2019Article
- Crystal Structure of Chicken γS-Crystallin Reveals Lattice Contacts with Implications for Function in the Lens and the Evolution of the βγ-Crystallins.Structure (London, England : 1993) · 2017Article
- γ-Crystallins of the chicken lens: remnants of an ancient vertebrate gene family in birds.The FEBS journal · 2016Article
- Solution properties of γ-crystallins: hydration of fish and mammal γ-crystallins.Protein science : a publication of the Protein Society · 2014Article
- Solution properties of γ-crystallins: compact structure and low frictional ratio are conserved properties of diverse γ-crystallins.Protein science : a publication of the Protein Society · 2014Article
- Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.Structure (London, England : 1993) · 2013Article
- Exploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic tools.The journal of physical chemistry. B · 2013Article
- Structure and dynamics of the fish eye lens protein, γM7-crystallin.Biochemistry · 2013Article
- Age-dependent racemization of serine residues in a human chaperone protein.Protein science : a publication of the Protein Society · 2013Article
- Structural analysis of the mutant protein D26G of human γS-crystallin, associated with Coppock cataract.Molecular vision · 2013Article
- A role for γS-crystallin in the organization of actin and fiber cell maturation in the mouse lens.The FEBS journal · 2012Article
- Racemization of two proteins over our lifespan: deamidation of asparagine 76 in γS crystallin is greater in cataract than in normal lenses across the age range.Investigative ophthalmology & visual science · 2012Article
- An improved algorithm for MFR fragment assembly.Journal of biomolecular NMR · 2012Article
- ¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V.Biomolecular NMR assignments · 2012Article
- The mutation V42M distorts the compact packing of the human gamma-S-crystallin molecule, resulting in congenital cataract.PloS one · 2012Article
- Characterization of a transient unfolding intermediate in a core mutant of γS-crystallin.Journal of molecular biology · 2011Article
- Separating instability from aggregation propensity in γS-crystallin variants.Biophysical journal · 2011Article
- A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin.Journal of molecular biology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The solution structure of murine gammaS-crystallin (gammaS) has been determined by multidimensional triple resonance NMR spectroscopy, using restraints derived from two sets of dipolar couplings, recorded in different alignment media, and supplemented by a small number of NOE distance restraints. gammaS consists of two topologically similar domains, arranged with an approximate twofold symmetry, and each domain shows close structural homology to closely related (approximately 50% sequence identity) domains found in other members of the gamma-crystallin family. Each domain consists of two four-strand "Greek key" beta-sheets. Although the domains are tightly anchored to one another by the hydrophobic surfaces of the two inner Greek key motifs, the N-arm, the interdomain linker and several turn regions show unexpected flexibility and disorder in solution. This may contribute entropic stabilization to the protein in solution, but may also indicate nucleation sites for unfolding or other structural transitions. The method used for solving the gammaS structure relies on the recently introduced molecular fragment replacement method, which capitalizes on the large database of protein structures previously solved by X-ray crystallography and NMR.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.