Targeted next generation sequencing in patients with inborn errors of metabolism [PDF]
, 2018 BACKGROUND: Next-generation sequencing (NGS) technology has allowed the promotion of genetic diagnosis and are becoming increasingly inexpensive and faster.
Armstrong i Morón, Judith +9 more
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Library of Apicomplexan Metabolic Pathways: a manually curated database for metabolic pathways of apicomplexan parasites. [PDF]
, 2012 The Library of Apicomplexan Metabolic Pathways (LAMP, http://www.llamp.net) is a web database that provides near complete mapping from genes to the central metabolic functions for some of the prominent intracellular parasites of the phylum Apicomplexa ...
Gonzalez-Galarza, FF +4 more
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Glutarate regulates T cell metabolism and anti-tumour immunity [PDF]
, 2023 T cell function and fate can be influenced by several metabolites: in some cases, acting through enzymatic inhibition of α-ketoglutarate-dependent dioxygenases, in others, through post-translational modification of lysines in important targets.
Antrobus, Robin +16 more
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Expression, Lipoylation and Structure Determination of Recombinant Pea H‐Protein in Escherichia coli [PDF]
European Journal of Biochemistry, 1996 A synthetic gene encoding the entire mature H protein of the glycine decarboxylase complex from pea (Pisum sativum L.) was constructed and expressed in Escherichia coli. The recombinant H protein, which after the induction period constituted more than half of the E. coli protein, was found in a soluble form.
D, Macherel +5 more
openaire +2 more sources
Defining Caenorhabditis elegans as a model system to investigate lipoic acid metabolism [PDF]
, 2020 Lipoic acid (LA) is a sulfur-containing cofactor that covalently binds to a variety of cognate enzymes that are essential for redox reactions in all three domains of life.
de Mendoza, Diego +2 more
core +1 more source
Crystal structure of lipoate‐bound lipoate ligase 1, LipL1, from Plasmodium falciparum [PDF]
, 2017 Plasmodium falciparum lipoate protein ligase 1 (PfLipL1) is an ATP‐dependent ligase that belongs to the biotin/lipoate A/B protein ligase family (PFAM PF03099).
Afanador, Gustavo A. +2 more
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The Amidase Domain of Lipoamidase Specifically Inactivates Lipoylated Proteins In Vivo
PLoS ONE, 2009 In the 1950s, Reed and coworkers discovered an enzyme activity in Streptococcus faecalis (Enterococcus faecalis) extracts that inactivated the Escherichia. coli and E. faecalis pyruvate dehydrogenase complexes through cleavage of the lipoamide bond. The enzyme that caused this lipoamidase activity remained unidentified until Jiang and Cronan discovered
Maroya D Spalding, Sean T Prigge
openaire +4 more sources
Distinctive phosphoinositide- and Ca²⁺-binding properties of normal and cognitive performance–linked variant forms of KIBRA C2 domain [PDF]
, 2018 Kidney- and brain-expressed protein (KIBRA), a multifunctional scaffold protein with around 20 known binding partners, is involved in memory and cognition, organ size control via the Hippo pathway, cell polarity, and membrane trafficking.
Bagby, S +8 more
core +2 more sources
Identification and Solution Structures of a Single Domain Biotin/Lipoyl Attachment Protein from Bacillus subtilis [PDF]
Journal of Biological Chemistry, 2006 Protein biotinylation and lipoylation are post-translational modifications, in which biotin or lipoic acid is covalently attached to specific proteins containing biotin/lipoyl attachment domains. All the currently reported natural proteins containing biotin/lipoyl attachment domains are multidomain proteins and can only be modified by either biotin or ...
Gaofeng, Cui +5 more
openaire +2 more sources
, 2015 Apicomplexan parasites are responsible for numerous important human diseases including toxoplasmosis, cryptosporidiosis, and most importantly malaria.
Agrawal, Swati +10 more
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