ReviewArchives of biochemistry and biophysics2012
Allostery and the dynamic oligomerization of porphobilinogen synthase.
Review in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 48 citations in OpenAlex.
- Frataxin Traps Low Abundance Quaternary Structure to Stimulate Human Fe-S Cluster Biosynthesis.Biochemistry · 2025Article
- Biochemical and molecular characterization of a novel porphobilinogen synthase from Corynebacterium glutamicum.World journal of microbiology & biotechnology · 2023Article
- More indications for redox-sensitive cysteine residues of the Arabidopsis 5-aminolevulinate dehydratase.Frontiers in plant science · 2023Article
- Moonlighting Proteins in the Fuzzy Logic of Cellular Metabolism.Molecules (Basel, Switzerland) · 2020Review
- Mitochondria and Iron: current questions.Expert review of hematology · 2017Review
- The Remarkable Character of Porphobilinogen Synthase.Accounts of chemical research · 2016Article
- From structural biology to designing therapy for inborn errors of metabolism.Journal of inherited metabolic disease · 2016Review
- Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain.Scientific reports · 2016Article
- First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Compounds identified by virtual docking to a tetrameric EGFR extracellular domain can modulate Grb2 internalization.BMC cancer · 2015Article
- Two classes of bacterial IMPDHs according to their quaternary structures and catalytic properties.PloS one · 2015Article
- wALADin benzimidazoles differentially modulate the function of porphobilinogen synthase orthologs.Journal of medicinal chemistry · 2014Article
- Allosteric modulation of protein oligomerization: an emerging approach to drug design.Frontiers in chemistry · 2014Review
- Development of a fluorescent monoclonal antibody-based assay to measure the allosteric effects of synthetic peptides on self-oligomerization of AGR2 protein.Protein science : a publication of the Protein Society · 2013Article
- Erythroid heme biosynthesis and its disorders.Cold Spring Harbor perspectives in medicine · 2013Review
- A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics.Archives of biochemistry and biophysics · 2013Article
- Environmental contaminants perturb fragile protein assemblies and inhibit normal protein function.Current chemical biology · 2013Article
- Impact of quaternary structure dynamics on allosteric drug discovery.Current topics in medicinal chemistry · 2013Article
- Structural basis for morpheein-type allosteric regulation of Escherichia coli glucosamine-6-phosphate synthase: equilibrium between inactive hexamer and active dimer.The Journal of biological chemistry · 2012Article
- One ring to rule them all: trafficking of heme and heme synthesis intermediates in the metazoans.Biochimica et biophysica acta · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The structural basis for allosteric regulation of porphobilinogen synthase (PBGS) is modulation of a quaternary structure equilibrium between octamer and hexamer (via dimers), which is represented schematically as 8mer ⇔ 2mer ⇔ 2mer∗⇔ 6mer∗. The "∗" represents a reorientation between two domains of each subunit that occurs in the dissociated state because it is sterically forbidden in the larger multimers. Allosteric effectors of PBGS are both intrinsic and extrinsic and are phylogenetically variable. In some species this equilibrium is modulated intrinsically by magnesium which binds at a site specific to the 8mer. In other species this equilibrium is modulated intrinsically by pH with the guanidinium group of an arginine being spatially equivalent to the allosteric magnesium ion. In humans, disease associated variants all shift the equilibrium toward the 6mer∗ relative to wild type. The 6mer∗ has a surface cavity that is not present in the 8mer and is proposed as a small molecule allosteric binding site. In silico and in vitro approaches have revealed species-specific allosteric PBGS inhibitors that stabilize the 6mer∗. Some of these inhibitors are drugs in clinical use leading to the hypothesis that extrinsic allosteric inhibition of human PBGS could be a mechanism for drug side effects.
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.