ArticleProceedings of the National Academy of Sciences of the United States of America2018
Human hydroxymethylbilane synthase: Molecular dynamics of the pyrrole chain elongation identifies step-specific residues that cause AIP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- Oral Nutritional Supplement with β-hydroxy-β-methylbutyrate (HMB) Improves Nutrition, Physical Performance and Ameliorates Intramuscular Adiposity in Pre-Frail Older Adults: A Randomized Controlled Trial.The journal of nutrition, health & aging · 2021Trial
- Milestones in the Elucidation of Heme Biosynthesis.Chemical reviews · 2026Review
- FiTMuSiC: leveraging structural and (co)evolutionary data for protein fitness prediction.Human genomics · 2024Article
- Systematically testing human HMBS missense variants to reveal mechanism and pathogenic variation.American journal of human genetics · 2023Article
- Uncovering the Kinetic Characteristics and Degradation Preference of PROTAC Systems with Advanced Theoretical Analyses.JACS Au · 2023Article
- Systematically testing human HMBS missense variants to reveal mechanism and pathogenic variation.bioRxiv : the preprint server for biology · 2023Article
- Functional and structural analysis of a novel splice siteFrontiers in genetics · 2023Article
- Genetic analysis of acute intermittent porphyria caused by novel classical splicing variant in the insertion region of 29-residue specific to humanFrontiers in molecular biosciences · 2023Article
- Characterisation of a common hotspot variant in acute intermittent porphyria sheds light on the mechanism of hydroxymethylbilane synthase function.FEBS open bio · 2022Article
- Acute intermittent porphyria: prevalence of pathogenicAnnals of translational medicine · 2022Article
- Article
- The crystal structures of the enzyme hydroxymethylbilane synthase, also known as porphobilinogen deaminase.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Two Novel Hydroxymethylbilane Synthase Splicing Mutations Predispose to Acute Intermittent Porphyria.International journal of molecular sciences · 2021Article
- Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism.iScience · 2021Article
- Crystal structures of hydroxymethylbilane synthase complexed with a substrate analog: a single substrate-binding site for four consecutive condensation steps.The Biochemical journal · 2021Article
- Acute Intermittent Porphyria: An Overview of Therapy Developments and Future Perspectives Focusing on Stabilisation of HMBS and Proteostasis Regulators.International journal of molecular sciences · 2021Review
- Screening of Reference Genes for RT-qPCR in Chicken Adipose Tissue and Adipocytes.Frontiers in physiology · 2021Article
- Recent advances in the epidemiology and genetics of acute intermittent porphyria.Intractable & rare diseases research · 2020Review
- Article
- Recent advances on porphyria genetics: Inheritance, penetrance & molecular heterogeneity, including new modifying/causative genes.Molecular genetics and metabolism · 2019Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Hydroxymethylbilane synthase (HMBS), the third enzyme in the heme biosynthetic pathway, catalyzes the head-to-tail condensation of four molecules of porphobilinogen (PBG) to form the linear tetrapyrrole 1-hydroxymethylbilane (HMB). Mutations in human
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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.