2018
DOI: 10.1016/j.compbiolchem.2018.09.002
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In-silico screening of small molecule inhibitors against Lactate Dehydrogenase (LDH) of Cryptosporidium parvum

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Cited by 11 publications
(5 citation statements)
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“…Also, more hydrogen bonding interactions for greater stability of the mangiferin with the LDH protein were generated. These results are similar and in agreement with those of Dhal et al (2018) , who reported in silico screening of small molecule inhibitors against LDH of Cryptosporidium parvum . Mahapatra and Das (2020) observed similar results after performing in silico docking, molecular dynamics modeling, and the binding of gentianine to the LDH, which acts as a crucial enzyme for the parasite’s survival.…”
Section: Discussionsupporting
confidence: 92%
See 1 more Smart Citation
“…Also, more hydrogen bonding interactions for greater stability of the mangiferin with the LDH protein were generated. These results are similar and in agreement with those of Dhal et al (2018) , who reported in silico screening of small molecule inhibitors against LDH of Cryptosporidium parvum . Mahapatra and Das (2020) observed similar results after performing in silico docking, molecular dynamics modeling, and the binding of gentianine to the LDH, which acts as a crucial enzyme for the parasite’s survival.…”
Section: Discussionsupporting
confidence: 92%
“…Also, we have discovered that mangiferin is promising as an inhibitor. These results are similar and in agreement with those of Dhal et al (2018) and Sun et al (2015) , who performed molecular docking to screen for novel inhibitors of LDH enzymes.…”
Section: Discussionsupporting
confidence: 89%
“…The lactate dehydrogenase and isomerase glucose-6-phosphate in Cryptosporidium (CpLDH and CpGPI) have been found to be associated with the parasitophorous vacuole membrane formation and energy dynamics (Madern et al 2004 ; H. Zhang et al 2015 ). Therefore, LDH, GPI, and other glycolysis pathway members could be potential therapeutic targets (Dhal et al 2018 ; Eltahan et al 2018 ).…”
Section: Novel Drug Targetsmentioning
confidence: 99%
“…LDH structure is well preserved across species, with very minor alterations in amino acid sequences [5] , and the structural affinity of LDH provides a justification for developing small-molecule inhibitors to modify its catalytic action in cells. LDH’s active pocket contains catalytically active residues such as His193, Asp168, Arg171, Thr246, and Arg106 [6] . LDH possesses five isozymes where the fifth form or LDH-5, also known as LDHA is upregulated in most of the tumor cells, thus inhibiting LDHA decreases tumor development and invasiveness [7] .…”
Section: Introductionmentioning
confidence: 99%