ArticleThe protein journal2007
Alpha-crystallin assisted refolding of enzyme substrates: optimization of external parameters.
Article in The protein journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed.
- Insights into the dual nature of αB-crystallin chaperone activity from the p.P39L mutant at the N-terminal region.Scientific reports · 2024Article
- Structural and functional studies of D109A human αB-crystallin contributing to the development of cataract and cardiomyopathy diseases.PloS one · 2021Article
- Identification of histidine residues involved in Zn(2+) binding to αA- and αB-crystallin by chemical modification and MALDI TOF mass spectrometry.The protein journal · 2012Article
- Article
- Hydroimidazolone modification of human alphaA-crystallin: Effect on the chaperone function and protein refolding ability.Biochimica et biophysica acta · 2010Article
- Structure/function studies of dogfish alpha-crystallin, comparison with bovine alpha-crystallin.Molecular vision · 2009Article
- Chemical modulation of the chaperone function of human alphaA-crystallin.Journal of biochemistry · 2008Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
alpha-Crystallin is known to act as a molecular chaperone by preventing the aggregation of partially unfolded substrate proteins. It is also known to assist the refolding of a number of denatured enzymes, but the activity yield is often less than 20%. In this paper, we have tried to tune the refolding ability of alpha-crystallin in vitro by optimizing various external parameters. We wanted to find out the best possible condition under which it can exhibit maximum refolding capacity. We found that under suitable condition in vitro alpha-crystallin can refold denatured malate dehydrogenase, carbonic anhydrase and lactate dehydrogenase to recover more than 40% activity. We also measured the effect of several external factors such as nucleotides, osmolytes, electrolytes, temperature etc. on the in vitro alpha-crystallin mediated reactivation of above stated enzymes. We found that nucleotides and electrolytes had little effect on the refolding ability of alpha-crystallin. However, in presence of different osmolytes, we found that its ability to reactivate denatured substrate proteins enhanced significantly. Refolding in presence of pre-incubated alpha-crystallin reveals that hydrophobicity had stronger influence on the refolding capacity of alpha-crystallin than its oligomeric size.
Indexed as
Identifiers
17211683What 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.