ArticleCellular and molecular life sciences : CMLS2018
Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX.
Article in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 27 citations in OpenAlex.
- Salt Stress Mitigation and Field-Relevant Biostimulant Activity of Prosystemin Protein Fragments: Novel Tools for Cutting-Edge Solutions in Agriculture.Plants (Basel, Switzerland) · 2025Article
- Dual targeting carbonic anhydrase inhibitors as promising therapeutic approach: a structural overview.Frontiers in molecular biosciences · 2025Review
- Discovery of Carbonic Anhydrase 9 as a Novel CLEC2 Ligand in a Cellular Interactome Screen.Cells · 2024Article
- Article
- α-CAs from Photosynthetic Organisms.International journal of molecular sciences · 2022Review
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- The Amazing World of IDPs in Human Diseases II.Biomolecules · 2022Article
- Biochemical and Structural Insights into the Winged Helix Domain of P150, the Largest Subunit of the Chromatin Assembly Factor 1.International journal of molecular sciences · 2022Article
- Not Only Systemin: Prosystemin Harbors Other Active Regions Able to Protect Tomato Plants.Frontiers in plant science · 2022Article
- Intrinsically disordered features of carbonic anhydrase IX proteoglycan-like domain.Cellular and molecular life sciences : CMLS · 2021Review
- The Amazing World of IDPs in Human Diseases.Biomolecules · 2021Article
- Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions.Journal of enzyme inhibition and medicinal chemistry · 2020Review
- Biophysical Characterization of Cancer-Related Carbonic Anhydrase IX.International journal of molecular sciences · 2020Article
- Structural comparison of protiated, H/D-exchanged and deuterated human carbonic anhydrase IX.Acta crystallographica. Section D, Structural biology · 2019Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human carbonic anhydrase IX (hCA IX) is a tumour-associated enzyme present in a limited number of normal tissues, but overexpressed in several malignant human tumours. It is a transmembrane protein, where the extracellular region consists of a greatly investigated catalytic CA domain and a much less investigated proteoglycan-like (PG) domain. Considering its important role in tumour biology, here, we report for the first time the full characterization of the PG domain, providing insights into its structural and functional features. In particular, this domain has been produced at high yields in bacterial cells and characterized by means of biochemical, biophysical and molecular dynamics studies. Results show that it belongs to the family of intrinsically disordered proteins, being globally unfolded with only some local residual polyproline II secondary structure. The observed conformational flexibility may have several important roles in tumour progression, facilitating interactions of hCA IX with partner proteins assisting tumour spreading and progression.
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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.