Agranoff, D; Monahan, IM; Mangan, JA; Butcher, PD; Krishna, S (1999) Mycobacterium tuberculosis expresses a novel pH-dependent divalent cation transporter belonging to the Nramp family. JOURNAL OF EXPERIMENTAL MEDICINE, 190 (5). 717 - 724 (8). ISSN 0022-1007 https://doi.org/10.1084/jem.190.5.717
SGUL Authors: Butcher, Philip David Krishna, Sanjeev Monahan, Irene Margaret

Preview

["document_typename_application/pdf; charset=binary" not defined] Published Version Download (221kB) | Preview

Item Type:	Article
Additional Information:	PubMed ID: 10477555
Keywords:	Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, Cation Transport Proteins, Cations, Divalent, DNA Primers, Female, Hydrogen-Ion Concentration, Ion Transport, Iron-Binding Proteins, Membrane Proteins, Molecular Sequence Data, Mycobacterium tuberculosis, Oocytes, RNA, Bacterial, RNA, Messenger, Sequence Homology, Amino Acid, Xenopus laevis, Science & Technology, Life Sciences & Biomedicine, Immunology, Medicine, Research & Experimental, Research & Experimental Medicine, bacillus Calmette-Guerin, Xenopus oocyte, metal ion, phagosome, intracellular pathogen, METAL-ION HOMEOSTASIS, NATURAL-RESISTANCE, INTRACELLULAR INFECTIONS, XENOPUS-OOCYTES, PROTEIN, GENE, IRON, SUSCEPTIBILITY, PATHOGENS, MEMBRANE, bacillus Calmette-Guerin, Xenopus oocyte, metal ion, phagosome, intracellular pathogen
SGUL Research Institute / Research Centre:	Academic Structure > Infection and Immunity Research Institute (INII)
Journal or Publication Title:	JOURNAL OF EXPERIMENTAL MEDICINE
ISSN:	0022-1007
Related URLs:	Author
Dates:	Date Event 6 September 1999 Published
Web of Science ID:	WOS:000082534500012
	Download EPMC Full text (PDF)
	Download EPMC Full text (HTML)
URI:	https://openaccess.sgul.ac.uk/id/eprint/1638
Publisher's version:	https://doi.org/10.1084/jem.190.5.717

Actions (login required)

Edit Item