ArticleRSC advances2019
Enhancement of protein stability by an additional disulfide bond designed in human neuroglobin.
Article in RSC advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 21 citations in OpenAlex.
- Insights into the Function of a Conserved Cys120 in Human Neuroglobin in Oxidative Stress Regulation of Breast Cancer Cells.Biomolecules · 2026Article
- Site-specific incorporation ofCommunications biology · 2024Article
- Stabilization ofMembranes · 2023Article
- Improved single-cell genome amplification by a high-efficiency phi29 DNA polymerase.Frontiers in bioengineering and biotechnology · 2023Article
- Engineering globins for efficient biodegradation of malachite green: two case studies of myoglobin and neuroglobin.RSC advances · 2022Article
- Evidence for a synergistic effect of post-translational modifications and genomic composition of eEF-1α on the adaptation ofEcology and evolution · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human neuroglobin (Ngb) forms an intramolecular disulfide bond between Cys46 and Cys55, with a third Cys120 near the protein surface, which is a promising protein model for heme protein design. In order to protect the free Cys120 and to enhance the protein stability, we herein developed a strategy by designing an additional disulfide bond between Cys120 and Cys15
Identifiers
What OpenQuestion holds
Registered trials
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