ArticleACS omega2022
Insights into the Distribution and Functional Properties of l-Asparaginase in the Archaeal Domain and Characterization of
Article in ACS omega, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
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Who cites it
4 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- Article
- Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production.International journal of molecular sciences · 2023Review
- The effects of nature-inspired amino acid substitutions on structural and biochemical properties of the E. coli L-asparaginase EcAIII.Protein science : a publication of the Protein Society · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
l-Asparaginase catalyzes the hydrolysis of l-asparagine to aspartic acid and ammonia and is used in the medical and food industries. In this investigation, from the proteomes of 176 archaeal organisms (with completely sequenced genomes), 116 homologs of l-asparaginase were obtained from 86 archaeal organisms segregated into Asp1, Asp2, IaaA, Asp2like1, and Asp2like2 families based on the conserved domain. The similarities and differences in the structure of selected representatives from each family are discussed. From the two novel archaeal l-asparaginase families Asp2like1 and Asp2like2, a representative of Asp2like1 family
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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.