The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Selective inhibition of prolyl 4-hydroxylases by bipyridinedicarboxylates
Abstract
Collagen is the most abundant protein in animals. A variety of indications are associated with the overproduction of collagen, including fibrotic diseases and cancer metastasis. The stability of collagen relies on the posttranslational modification of proline residues to form (2S,4R)-4-hydroxyproline. This modification is catalyzed by collagen prolyl 4-hydroxylases (CP4Hs), which are Fe(II)- and α-ketoglutarate (AKG)-dependent dioxygenases located in the lumen of the endoplasmic reticulum. Human CP4Hs are validated targets for treatment of both fibrotic diseases and metastatic breast cancer. Herein, we report on 2,2′-bipyridinedicarboxylates as inhibitors of a human CP4H. Although most 2,2′-bipyridinedicarboxylates are capable of inhibition via iron sequestration, the 4,5′- and 5,5′-dicarboxylates were found to be potent competitive inhibitors of CP4H, and the 5,5′-dicarboxylate was selective in its inhibitory activity. Our findings clarify a strategy for developing CP4H inhibitors of clinical utility.
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In the citing paper
“Recently, we reported that certain dicarboxylate derivatives of 2,2′-bipyridine (bipy) and other biheteroaryl compounds are specific inhibitors of human CP4H.20,21”
From Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center (2016) · cites this paper as [20]
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In the citing paper
“Whereas bipy itself does not serve as an activator of CP4H,20,22”
From Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center (2016) · cites this paper as [20]
In the citing paper
“Bipy-4,5′-dicarboxylate (bipy45′DC) and bipy-5,5′-dicarboxylate (bipy55′DC) are potent inhibitors of human CP4H1 and thought to inhibit the enzyme by competing with α-ketoglutarate.20”
From Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center (2016) · cites this paper as [20]
In the citing paper
“These biheteroaryl dicarboxylates compete with α-ketoglutarate for binding to the active-site iron.”
From Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center (2016) · cites this paper as [20]
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Citations
Cites
1 retracted
RETRACTED: Collagen Prolyl Hydroxylases Are Essential for Breast Cancer Metastasis
Gilkes, D. M., Chaturvedi, P., Bajpai, S., Wong, C. C., Wei, H., Pitcairn, S., Hubbi, M. E., Wirtz, D., & Semenza, G. L. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3963 · Cited by 296
RetractedMolecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin
Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323
Collagen Structure and Stability
Shoulders, M. D., & Raines, R. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.032207.120833 · Cited by 3,923
Self-citationCollagen density promotes mammary tumor initiation and progression
Provenzano, P. P., Inman, D. R., Eliceiri, K. W., Knittel, J. G., Yan, L., Rueden, C. T., White, J. G., & Keely, P. J. (2008) · BMC Medicine · doi:10.1186/1741-7015-6-11 · Cited by 1,361
Aligned Collagen Is a Prognostic Signature for Survival in Human Breast Carcinoma
Conklin, M. W., Eickhoff, J. C., Riching, K. M., Pehlke, C. A., Eliceiri, K. W., Provenzano, P. P., Friedl, A., & Keely, P. J. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.076 · Cited by 1,321
Collagens, modifying enzymes and their mutations in humans, flies and worms
Myllyharju, J., & Kivirikko, K. I. (2003) · Trends in Genetics · doi:10.1016/j.tig.2003.11.004 · Cited by 1,235
Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes
Hausinger, R. P. (2004) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230490440541 · Cited by 937
Enzymatic Assembly of Overlapping DNA Fragments
Gibson, D. G. (2011) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-385120-8.00015-2 · Cited by 763
Therapy for Fibrotic Diseases: Nearing the Starting Line
Friedman, S. L., Sheppard, D., Duffield, J. S., & Violette, S. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3004700 · Cited by 655
Gorres, K. L., & Raines, R. T. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409231003627991 · Cited by 591
Self-citation
Research works printed but not linked: 1
- Job, 1928, Annali di Chimica Applicata, 9
Cited by
Collagen Prolyl 4-Hydroxylase as a Therapeutic Target: Miniperspective
Vasta, J. D., & Raines, R. T. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00822 · Cited by 82
Self-citationSelective Inhibition of Collagen Prolyl 4-Hydroxylase in Human Cells
Vasta, J. D., Andersen, K. A., Deck, K. M., Nizzi, C. P., Eisenstein, R. S., & Raines, R. T. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00749 · Cited by 41
Self-citationHuman Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center
Vasta, J. D., & Raines, R. T. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00251 · Cited by 36
Self-citation
Metadata
- Authors
- Vasta, J. D., & Raines, R. T.
- Venue
- Bioorganic & Medicinal Chemistry
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 23
- Issue
- 13
- Pages
- 3081-3090
- ISSN
- 0968-0896
- PMC
- PMC4552733
- Cited by
- 16
- References
- 36
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (am, 339 d)
- Funders
- NIH (R01 AR044276, T32 GM007215, P41 GM103399)
- NSF (CHE-9974839)
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- Vasta, J. D., & Raines, R. T. (2015). Selective inhibition of prolyl 4-hydroxylases by bipyridinedicarboxylates. Bioorganic & Medicinal Chemistry. https://doi.org/10.1016/j.bmc.2015.05.003
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
