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Cupello, A.; Scarrone, S.

doi:10.1023/a:1007616229260

Cited by 4 publications

(2 citation statements)

References 18 publications

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“…NEAT domain proteins to shuttle heme to the inner membrane-associated transport protein complex. 216,217 Within the last five years, efforts have refocused on MPPs as potential antibacterials. Notably, in P. aeruginosa it was shown that GaPPIX inhibits growth by targeting cytochromes and likely interfers with cellular respiration.…”

Section: Targeting Heme Uptake Pathwaysmentioning

confidence: 99%

Iron Acquisition in Mycobacterium tuberculosis

Chao¹,

Sieminski²,

Owens

et al. 2018

Chem. Rev.

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The highly contagious disease tuberculosis (TB) is caused by the bacterium Mycobacterium tuberculosis (Mtb), which has been evolving drug resistance at an alarming rate. Like all human pathogens, Mtb requires iron for growth and virulence. Consequently, Mtb iron transport is an emerging drug target. However, the development of anti-TB drugs aimed at these metabolic pathways have been restricted by the dearth of information on Mtb iron acquisition. In this review, we describe the multiple strategies utilized by Mtb to acquire ferric iron and heme-iron. Mtb iron uptake is a complex process, requiring biosynthesis and subsequent export of Mtb siderophores, followed by ferric iron scavenging and ferric-siderophore import into Mtb. Additionally, Mtb possesses two possible heme uptake pathways, and an Mtb-specific mechanism of heme degradation that yields iron and novel heme-degradation products. We conclude with perspectives for potential therapeutics that could directly target Mtb heme and iron uptake machineries. We also highlight how hijacking Mtb heme and iron acquisition pathways for drug import may facilitate drug transport through the notoriously impregnable Mtb cell-wall.

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Section: Targeting Heme Uptake Pathwaysmentioning

confidence: 99%

Iron Acquisition in Mycobacterium tuberculosis

Chao¹,

Sieminski²,

Owens

et al. 2018

Chem. Rev.

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“…Purified synaptosomes were prepared from rat brain essentially by the same procedure described in previous reports [5][6][7] by the Ficoll 400 discontinuous gradient procedure of Cotman and Matthews [8]. Purified synaptosomes were then osmotically shocked with distilled water (8 ml per synaptosomes obtained from 1 g of tissue).…”

Section: Preparation Of Membranes Samples From Rat Brain Subcellular mentioning

confidence: 99%

Binding of Paroxetine to the Serotonin Transporter in Membranes from Different Cells, Subcellular Fractions and Species

et al. 2008

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The binding of [(3)H]-paroxetine to membrane serotonin transporter (SERT) has been studied in membranes from different sources and subcellular fractions. From rat were membranes from venous blood platelets, brain total cortex, brain microsomes, brain crude and purified synaptosomes. Membranes were obtained from venous blood platelets from human volunteers and from brain cortex tissue from neurosurgery (cerebral lobectomies following craniocerebral injuries). The main finding was that the K (D) of paroxetine binding to the SERT was the same for platelet and nerve ending (synaptosomal) membranes. That parameter was significantly lower in membranes from brain microsomes and cortex total tissue. No species related difference was found, where comparison was possible, between human and rat tissue. The equality of K (D) of paroxetine binding to blood platelet membranes and to membranes from nerve endings appears to encourage the use of such membranes as a model for brain SERT. Binding at two different temperatures for several of the fractions suggests that paroxetine-SERT interaction is entropy-driven.

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