ReviewCurrent pharmaceutical design2013
Targeting UDP-galactopyranose mutases from eukaryotic human pathogens.
Review in Current pharmaceutical design, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 22 citations in OpenAlex.
- Proteomics ofJournal of fungi (Basel, Switzerland) · 2023Article
- Recent Advances in Chemotherapeutics for Leishmaniasis: Importance of the Cellular Biochemistry of the Parasite and Its Molecular Interaction with the Host.Pathogens (Basel, Switzerland) · 2023Review
- Genome Sequence and Adaptation Analysis of the Human and Rice Pathogenic StrainPathogens (Basel, Switzerland) · 2021Article
- The Glycan Structure ofMolecules (Basel, Switzerland) · 2020Review
- Galactofuranose-Related Enzymes: Challenges and Hopes.International journal of molecular sciences · 2020Review
- Molecular Dynamics Simulations of Substrate Release from Trypanosoma cruzi UDP-Galactopyranose Mutase.Journal of chemical information and modeling · 2019Article
- Identification of eukaryotic UDP-galactopyranose mutase inhibitors using the ThermoFAD assay.Biochemical and biophysical research communications · 2017Article
- Multiple functionalities of reduced flavin in the non-redox reaction catalyzed by UDP-galactopyranose mutase.Archives of biochemistry and biophysics · 2017Review
- Deciphering the sugar biosynthetic pathway and tailoring steps of nucleoside antibiotic A201A unveils a GDP-l-galactose mutase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics.Biochemistry · 2014Article
- Article
- Substrate-dependent dynamics of UDP-galactopyranose mutase: Implications for drug design.Protein science : a publication of the Protein Society · 2013Article
- UDP-galactopyranose mutases from Leishmania species that cause visceral and cutaneous leishmaniasis.Archives of biochemistry and biophysics · 2013Article
- Identification of the NAD(P)H binding site of eukaryotic UDP-galactopyranose mutase.Journal of the American Chemical Society · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
UDP-Galactopyranose mutase (UGM) is a unique flavin-dependent enzyme that catalyzes the conversion of UDP-galactopyranose(UDP-Galp) to UDP-galactofuranose (UDP-Galf). The product of this reaction is the precursor to Galf, a major component of the cell wall and of cell surface glycoproteins and glycolipids in many eukaryotic and prokaryotic human pathogens. The function of UGM is important in the virulence of fungi, parasites, and bacteria. Its role in virulence and its absence in humans suggest that UGM is an ideal drug target. Significant structural and mechanistic information has been accumulated on the prokaryotic UGMs; however, in the past few years the research interest has shifted to UGMs from eukaryotic human pathogens such as fungi and protozoan parasites. It has become clear that UGMs from prokaryotic and eukaryotic organisms have different structural and mechanistic features. The amino acid sequence identity between these two classes of enzymes is low, resulting in differences in oligomeric states, substrate binding, active site flexibility, and interaction with redox partners. However, the unique role of the flavin cofactor in catalysis is conserved among this enzyme family. In this review, recent findings on eukaryotic UGMs are discussed and presented in comparison with prokaryotic UGMs.
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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.