ReviewGene2007
Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins.
Review in Gene, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed.
- Cyanobacterial α-carboxysome carbonic anhydrase is allosterically regulated by the Rubisco substrate RuBP.Science advances · 2024Article
- Architectural digest: Thermodynamic stability and domain structure of a consensus monomeric globin.Biophysical journal · 2023Article
- Review
- Rational design of photosynthetic reaction center protein maquettes.Frontiers in molecular biosciences · 2022Article
- The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly.Biophysical journal · 2020Article
- Stabilization of Modular Nanotransporters by Embedding Hemin in Them in a New Strain with Heme Receptor Expression.Doklady. Biochemistry and biophysics · 2020Article
- Replacement of the heme axial lysine as a test of conformational adaptability in the truncated hemoglobin THB1.Journal of inorganic biochemistry · 2019Article
- Replacement of the Distal Histidine Reveals a Noncanonical Heme Binding Site in a 2-on-2 Hemoglobin.Biochemistry · 2018Article
- Introduction of a covalent histidine-heme linkage in a hemoglobin: a promising tool for heme protein engineering.Journal of inorganic biochemistry · 2014Article
- Nitric oxide blocks cellular heme insertion into a broad range of heme proteins.Free radical biology & medicine · 2010Article
- Unique structure and stability of HmuY, a novel heme-binding protein of Porphyromonas gingivalis.PLoS pathogens · 2009Article
- Controlling complexity and water penetration in functional de novo protein design.Biochemical Society transactions · 2008Article
- Structural and thermodynamic encoding in the sequence of rat microsomal cytochrome b(5).Biopolymers · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The binding of a cofactor to a protein matrix often involves a reorganization of the polypeptide structure. b Hemoproteins provide multiple examples of this behavior. In this minireview, selected monomeric and single b heme proteins endowed with distinct topological properties are inspected for the extent of induced refolding upon heme binding. To complement the data reported in the literature, original results are presented on a two-on-two globin of cyanobacterial origin (Synechococcus sp. PCC 7002 GlbN) and on the heme-containing module of FixL, an oxygen-sensing protein with the mixed alpha/beta topology of PAS domains. GlbN had a stable apoprotein that was further stabilized and locally refolded by heme binding; in contrast, apoFixLH presented features of a molten globule. Sequence analyses (helicity, disorder, and polarity) and solvent accessibility calculations were performed to identify trends in the architecture of b hemoproteins. In several cases, the primary structure appeared biased toward a partially disordered binding pocket in the absence of the cofactor.
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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.