A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria.

Supek, F; Supekova, L; Nelson, H; Nelson, N

doi:10.1073/pnas.93.10.5105

Cited by 325Fungal and yeast genetics researchHeavy Metal Exposure and ToxicityTrace Elements in Health

A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria.

Open access

Supek, F, Supekova, L, Nelson, H, Nelson, N·1996·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.93.10.5105PMC PMC39414

Open this paper in CoChat — free account

Abstract

A novel Saccharomyces cerevisiae mutant, unable to grow in the presence of 12.5 mM EGTA, was isolated by replica plating. The phenotype of the mutant is caused by a single amino acid change (Gly149 to Arg) in the essential yeast gene CDC1. The mutant could be suppressed by overexpression of the SMF1 gene, which was isolated as an extragenic high-copy suppressor. The SMF1 gene codes for a highly hydrophobic protein and its deletion renders the yeast cells sensitive to low manganese concentration. In accordance with this observation, the smf1 null mutant exhibits reduced Mn2+ uptake at micromolar concentrations. Using a specific antibody, we demonstrated that Smf1p is located in the yeast plasma membrane. These results suggest that Smf1p is involved in high-affinity Mn2+ uptake. This assumption was also tested by overexpressing the SMF1 gene in the temperature-sensitive mutant of the mitochondrial processing peptidase (MAS1). SMF1 overexpression as well as addition of 1 mM Mn2+ to the growth medium complemented this mutation. This also suggests that in vivo Mas1p is a manganese-dependent peptidase. The yeast Smf1p resembles a protein from Drosophila and mammalian macrophages. The latter was implicated in conferring resistance to mycobacteria. A connection between Mn2+ transport and resistance or sensitivity to mycobacteria is discussed.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1073/pnas.93.10.5105

Cites

41 of 41 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Homologous proteins in yeast, flies, and zebrafish also transport iron and similar divalent cations.
“Homologous proteins in yeast, 63 flies, 64 and zebrafish 65 also transport iron and similar divalent cations.”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [63]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572 · see citing works
Transformation of intact yeast cells treated with alkali cations
Ito, H., Fukuda, Y., Murata, K., & Kimura, A. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.1.163-168.1983 · Cited by 7,518 · see citing works
Getting started with yeast
Sherman, F. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)94004-v · Cited by 4,078 · see citing works
Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast.
Rothstein, R. (1991) · Methods in Enzymology · doi:10.1016/0076-6879(91)94022-5 · Cited by 1,283 · see citing works
Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg
Vidal, S. M., Malo, D., Vogan, K., Skamene, E., & Gros, P. (1993) · Cell · doi:10.1016/0092-8674(93)90135-d · Cited by 1,104 · see citing works
ZINC PROTEINS: Enzymes, Storage Proteins, Transcription Factors, and Replication Proteins
Coleman, J. E. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.004341 · Cited by 980 · see citing works
The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.
Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., Sipe, D. M., & Kaplan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90346-8 · Cited by 670 · see citing works
Molecular characterization of a copper transport protein in S. cerevisiae: An unexpected role for copper in iron transport
Dancis, A., Yuan, D. S., Haile, D., Askwith, C., Eide, D., Moehle, C., Kaplan, J., & Klausner, R. D. (1994) · Cell · doi:10.1016/0092-8674(94)90345-x · Cited by 659 · see citing works
A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast
Goud, B., Salminen, A., Walworth, N. C., & Novick, P. (1988) · Cell · doi:10.1016/0092-8674(88)90093-1 · Cited by 585 · see citing works
The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family
Rudolph, H. K., Antebi, A., Fink, G. R., Buckley, C. M. F., Dorman, T. E., LeVitre, J., Davidow, L. S., Mao, J.-I., & Moir, D. T. (1989) · Cell · doi:10.1016/0092-8674(89)90410-8 · Cited by 536 · see citing works
Calcineurin-dependent growth control in Saccharomyces cerevisiae mutants lacking PMC1, a homolog of plasma membrane Ca2+ ATPases
Cunningham, K. W., & Fink, G. R. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.124.3.351 · Cited by 432 · see citing works
The Interrelations between the Transport of Sodium and Calcium in Mitochondria of Various Mammalian Tissues
Crompton, M., Moser, R., Lüdi, H., & Carafoli, E. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb11993.x · Cited by 397 · see citing works
Mitochondrial protein import: Identification of processing peptidase and of PEP, a processing enhancing protein
Hawlitschek, G., Schneider, H., Schmidt, B., Tropschug, M., Hartl, F. U., & Neupert, W. (1988) · Cell · doi:10.1016/0092-8674(88)90096-7 · Cited by 395 · see citing works
Genetics of Resistance to Infection with Salmonella typhimurium in Mice
Plant, J. E., & Glynn, A. A. (1976) · The Journal of Infectious Diseases · doi:10.1093/infdis/133.1.72 · Cited by 320 · see citing works
Purification and properties of H+-translocating, Mg2+-adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae.
Uchida, E., Ohsumi, Y., & Anraku, Y. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)71211-1 · Cited by 313 · see citing works
[2] Micromanipulation and dissection of asci
Sherman, F., & Hicks, J. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)94005-w · Cited by 305 · see citing works
Mechanisms involved in mycobacterial growth inhibition by gamma interferon-activated bone marrow macrophages: role of reactive nitrogen intermediates
Flesch, I. E. A., & Kaufmann, S. H. E. (1991) · Infection and Immunity · doi:10.1128/iai.59.9.3213-3218.1991 · Cited by 280 · see citing works
[40] H+-ATPase from plasma membranes of Saccharomyces cerevisiae and Avena sativa roots: Purification and reconstitution
Serrano, R. (1988) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(88)57102-1 · Cited by 264 · see citing works
Calcium transport driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae.
Ohsumi, Y., & Anraku, Y. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)81935-8 · Cited by 252 · see citing works
Regulation of Leishmania populations within the host. II. genetic control of acute susceptibility of mice to Leishmania donovani infection.
Dj, B. (1977) · PubMed · Cited by 225 · see citing works
Import of proteins into yeast mitochondria: the purified matrix processing protease contains two subunits which are encoded by the nuclear MAS1 and MAS2 genes.
Yang, M., Jensen, R. E., Yaffe, M. P., Oppliger, W., & Schatz, G. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03271.x · Cited by 221 · see citing works
MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease.
Witte, C., Jensen, R. E., Yaffe, M. P., & Schatz, G. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02961.x · Cited by 185 · see citing works
Classical mutagenesis techniques
Lawrence, C. W. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)50963-0 · Cited by 173 · see citing works
Killing of Mycobacterium microti by immunologically activated macrophages
Walker, L., & Lowrie, D. B. (1981) · Nature · doi:10.1038/293069a0 · Cited by 160 · see citing works
[43] Analysis of mitochondrial function and assembly
Yaffe, M. P. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)94046-f · Cited by 158 · see citing works
Processing peptidase of Neurospora mitochondria. Two-step cleavage of imported ATPase subunit 9
SCHMIDT, B., Wächter, E., Sebald, W., & Neupert, W. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08505.x · Cited by 157 · see citing works
Iron Uptake by the Yeast Saccharomyces cerevisiae: Involvement of a Reduction Step
Lesuisse, E., Raguzzi, F., & Crichton, R. R. (1987) · Microbiology · doi:10.1099/00221287-133-11-3229 · Cited by 157 · see citing works
The processing peptidase of yeast mitochondria: the two co‐operating components MPP and PEP are structurally related.
Pollock, R. A., Hartl, F. U., Cheng, M. Y., Ostermann, J., Horwich, A. L., & Neupert, W. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03225.x · Cited by 153 · see citing works
Mutational analysis of yeast vacuolar H(+)-ATPase.
Noumi, T., Beltrán, C., Nelson, H. R., & Nelson, N. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.5.1938 · Cited by 153 · see citing works
[21] Recovery of plasmids from yeast into Escherichia coli: Shuttle vectors
Strathern, J. N., & Higgins, D. R. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)94024-7 · Cited by 146 · see citing works
Malvolio, the Drosophila homologue of mouse NRAMP-1 (Bcg), is expressed in macrophages and in the nervous system and is required for normal taste behaviour.
Rodrigues, V., Cheah, P. Y., Ray, K., & Chia, W. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07303.x · Cited by 136 · see citing works
Regulation of calcium fluxes in rat pancreatic islets: Calcium extrusion by sodium-calcium countertransport
Herchuelz, A., Sener, A., & Malaisse, W. J. (1980) · The Journal of Membrane Biology · doi:10.1007/bf01868981 · Cited by 115 · see citing works
NH2-terminal sequence of macrophage-expressed natural resistance-associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain.
Barton, C. H., White, J. K., Roach, T. I. A., & Blackwell, J. M. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.179.5.1683 · Cited by 92 · see citing works
Relationship between superoxide dismutase and pathogenic mechanisms of Listeria monocytogenes
Welch, D. F., Sword, C. P., Brehm, S. P., & Dusanic, D. G. (1979) · Infection and Immunity · doi:10.1128/iai.23.3.863-872.1979 · Cited by 82 · see citing works
[38] Plasma membrane ATPase from the yeast Schizosaccharomyces pombe
Dufour, J., Amory, A., & Goffeau, A. (1988) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(88)57100-8 · Cited by 72 · see citing works
Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein.
West, A. H., Clark, D. J., Martin, J., Neupert, W., Hartl, F. U., & Horwich, A. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35810-1 · Cited by 72 · see citing works
ATP-driven Ca2+/H+ antiport in acid vesicles from Dictyostelium.
Rooney, E. K., & Gross, J. D. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.17.8025 · Cited by 69 · see citing works
Calcium homeostasis and transport are affected by disruption of cta3, a novel gene encoding Ca2(+)-ATPase in Schizosaccharomyces pombe.
Ghislain, M., Goffeau, A., Halachmi, D., & Eilam, Y. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44766-1 · Cited by 58 · see citing works
Isolation and Characterization of Human NRAMP cDNA
Kishi, F. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2572 · Cited by 41 · see citing works
Mutations in the Saccharomyces cerevisiae CDC1 gene affect double-strand-break-induced intrachromosomal recombination.
Halbrook, J., & Hoekstra, M. F. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.12.8037 · Cited by 20 · see citing works
Mutations in the Saccharomyces cerevisiae CDC1 Gene Affect Double-Strand-Break-Induced Intrachromosomal Recombination
Halbrook, J., & Hoekstra, M. F. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.12.8037-8050.1994 · Cited by 8 · see citing works

Flagged first, then by citations

Research works printed but not linked: 4

[8]Rooney, E. K. & Gross, J. D. (1992) Proc. Natl. Acad. Sci. USA 89, 8025-8029.
[13]Noumi, T., Beltrán, C., Nelson, H. & Nelson, N. (1991) Proc. Natl. Acad. Sci. USA 88, 1938–1942.
[17]Maniatis, T., Fritsch, E. F. & Sambrook, J. (1984) Molecular Cloning: A Laboratory Manual (Cold Spring Harbor Lab. Press, Plainview, NY), pp. 88–148.
[19]Sanger, F., Nicklen, S. & Coulson, A. R. (1977) Proc. Natl. Acad. Sci. USA 74, 5463–5467.

Sorted by citations

Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166 · see citing works
Molecular mechanisms of plant metal tolerance and homeostasis
Clemens, S. (2001) · Planta · doi:10.1007/s004250000458 · Cited by 1,417 · see citing works
EIN2, a Bifunctional Transducer of Ethylene and Stress Responses in Arabidopsis
Alonso, J. M., Hirayama, T., Roman, G., Nourizadeh, S., & Ecker, J. R. (1999) · Science · doi:10.1126/science.284.5423.2148 · Cited by 1,297 · see citing works
Phylogenetic Relationships within Cation Transporter Families of Arabidopsis
Mäser, P., Thomine, S., Schroeder, J. I., Ward, J. M., Hirschi, K. D., Sze, H., Talke, I. N., Anna Amtmann, A., Maathuis, F. J. M., Sanders, D., et al. (2001) · PLANT PHYSIOLOGY · doi:10.1104/pp.126.4.1646 · Cited by 1,257 · see citing works
The ZIP family of metal transporters
Guerinot, M. L. (2000) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(00)00138-3 · Cited by 1,200 · see citing works
Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F., & Andrews, N. C. (1997) · Nature Genetics · doi:10.1038/ng0897-383 · Cited by 1,159 · see citing works
Cadmium and iron transport by members of a plant metal transporter family in Arabidopsis with homology to Nramp genes
Thomine, S., Wang, R., Ward, J. M., Crawford, N. M., & Schroeder, J. I. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.9.4991 · Cited by 905 · see citing works
The IRT1 protein from Arabidopsis thaliana is a metal transporter with a broad substrate range
Korshunova, Y. O., Eide, D., Clark, W. G., Guerinot, M. L., & Pakrasi, H. B. (1999) · Plant Molecular Biology · doi:10.1023/a:1026438615520 · Cited by 801 · see citing works
Variations in the NRAMP1 Gene and Susceptibility to Tuberculosis in West Africans
Bellamy, R., Ruwende, C., Corrah, T., McAdam, K. P. W. J., Whittle, H. C., & Hill, A. V. S. (1998) · New England Journal of Medicine · doi:10.1056/nejm199803053381002 · Cited by 731 · see citing works
Emerging mechanisms for heavy metal transport in plants
Williams, L. E., Pittman, J. K., & Hall, J. L. (2000) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(00)00133-4 · Cited by 631 · see citing works
Mobilization of vacuolar iron by AtNRAMP3 and AtNRAMP4 is essential for seed germination on low iron
Lanquar, V., Lelièvre, F., Bolte, S., Hamès, C., Alcon, C., Neumann, D., Vansuyt, G., Curie, C., Schröder, A., Krämer, U., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600864 · Cited by 631 · see citing works
Forging a field: the golden age of iron biology.
Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623 · see citing works
The OsNRAMP1 iron transporter is involved in Cd accumulation in rice
Takahashi, R., Ishimaru, Y., Senoura, T., Shimo, H., Ishikawa, S., Arao, T., Nakanishi, H., & Nishizawa, N. K. (2011) · Journal of Experimental Botany · doi:10.1093/jxb/err136 · Cited by 591 · see citing works
Involvement of NRAMP1 from Arabidopsis thaliana in iron transport
Curie, C., Alonso, J. M., Jean, M. L., Ecker, J. R., & Briat, J. (2000) · Biochemical Journal · doi:10.1042/bj3470749 · Cited by 552 · see citing works
Characterizing the role of rice NRAMP5 in Manganese, Iron and Cadmium Transport
Ishimaru, Y., Takahashi, R., Bashir, K., Shimo, H., Senoura, T., Sugimoto, K., Ono, K., Yano, M., Ishikawa, S., Arao, T., et al. (2012) · Scientific Reports · doi:10.1038/srep00286 · Cited by 541 · see citing works
The NRAMP family of metal-ion transporters
Nevo, Y., & Nelson, N. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.007 · Cited by 513 · see citing works
High-Affinity Manganese Uptake by the Metal Transporter NRAMP1 Is Essential for Arabidopsis Growth in Low Manganese Conditions
Cailliatte, R., Schikora, A., Briat, J., Mari, S., & Curie, C. (2010) · The Plant Cell · doi:10.1105/tpc.109.073023 · Cited by 499 · see citing works
Altered selectivity in an Arabidopsis metal transporter
Rogers, E. E., Eide, D. J., & Guerinot, M. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.210214197 · Cited by 467 · see citing works
Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron.
Canonne-Hergaux, F., Gruenheid, S., Ponka, P., & Gros, P. (1999) · Blood · doi:10.1182/blood.v93.12.4406 · Cited by 451 · see citing works
Natural Resistance to Infection with Intracellular Pathogens: The Nramp1 Protein Is Recruited to the Membrane of the Phagosome
Gruenheid, S., Pinner, E., Desjardins, M., & Gros, P. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.4.717 · Cited by 428 · see citing works
Expression Profiles of Arabidopsis thaliana in Mineral Deficiencies Reveal Novel Transporters Involved in Metal Homeostasis
Henri Wintz, A., Fox, T. C., Wu, Y., Feng, V., Chen, W., Chang, H., Zhu, T., & Vulpe, C. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309338200 · Cited by 431 · see citing works
Divalent-metal transport by NRAMP proteins at the interface of host–pathogen interactions
Forbes, J. R., & Gros, P. (2001) · Trends in Microbiology · doi:10.1016/s0966-842x(01)02098-4 · Cited by 424 · see citing works
Vacuolar and Plasma Membrane Proton-Adenosinetriphosphatases
Nelson, N., & Harvey, W. R. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.2.361 · Cited by 420 · see citing works
Iron homeostasis: insights from genetics and animal models
Andrews, N. C. (2000) · Nature Reviews Genetics · doi:10.1038/35042073 · Cited by 418 · see citing works
Managing the manganese: molecular mechanisms of manganese transport and homeostasis
Pittman, J. K. (2005) · New Phytologist · doi:10.1111/j.1469-8137.2005.01453.x · Cited by 377 · see citing works
Natural Resistance to Intracellular Infections
Jabado, N., Jankowski, A., Dougaparsad, S., Picard, V., Grinstein, S., & Gros, P. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.9.1237 · Cited by 372 · see citing works
Constitutive immune mechanisms: mediators of host defence and immune regulation
Paludan, S. R., Pradeu, T., Masters, S. L., & Mogensen, T. H. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-0391-5 · Cited by 363 · see citing works
MOLECULAR BIOLOGY OF CATION TRANSPORT IN PLANTS
Fox, T. C., & Guerinot, M. L. (1998) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.49.1.669 · Cited by 358 · see citing works
Differential Metal Selectivity and Gene Expression of Two Zinc Transporters from Rice
Ramesh, S. A., Shin, R., Eide, D. J., & Schachtman, D. P. (2003) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.026815 · Cited by 350 · see citing works
Tcn1p/Crz1p, a calcineurin-dependent transcription factor that differentially regulates gene expression in Saccharomyces cerevisiae
Matheos, D. P., Kingsbury, T. J., Ahsan, U. S., & Cunningham, K. W. (1997) · Genes & Development · doi:10.1101/gad.11.24.3445 · Cited by 332 · see citing works
Arabidopsis IRT2 gene encodes a root‐periphery iron transporter
Vert, G., Briat, J., & Curie, C. (2001) · The Plant Journal · doi:10.1046/j.1365-313x.2001.01018.x · Cited by 317 · see citing works
Metal ion transporters and homeostasis
Nelson, N. (1999) · The EMBO Journal · doi:10.1093/emboj/18.16.4361 · Cited by 316 · see citing works
The Iron Transport Protein NRAMP2 Is an Integral Membrane Glycoprotein That Colocalizes with Transferrin in Recycling Endosomes
Gruenheid, S., Canonne‐Hergaux, F., Gauthier, S., Hackam, D. J., Grinstein, S., & Gros, P. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.5.831 · Cited by 302 · see citing works
How Saccharomyces cerevisiae copes with toxic metals and metalloids
Wysocki, R., & Tamás, M. J. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00217.x · Cited by 300 · see citing works
Mn-euvering manganese: the role of transporter gene family members in manganese uptake and mobilization in plants
Socha, A. L., & Guerinot, M. L. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00106 · Cited by 299 · see citing works
THE MOLECULAR BIOLOGY OF METAL ION TRANSPORT INSACCHAROMYCES CEREVISIAE
Eide, D. J. (1998) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.18.1.441 · Cited by 292 · see citing works
Manganese homeostasis in Bacillus subtilis is regulated by MntR, a bifunctional regulator related to the diphtheria toxin repressor family of proteins
Que, Q., & Helmann, J. D. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01811.x · Cited by 282 · see citing works
Iron Acquisition and Transcriptional Regulation
Kaplan, C. D., & Kaplan, J. (2009) · Chemical Reviews · doi:10.1021/cr9001676 · Cited by 275 · see citing works
Functional characterization of NRAMP3 and NRAMP4 from the metal hyperaccumulator Thlaspi caerulescens
Oomen, R. J. F. J., Wu, J., Lelièvre, F., Blanchet, S., Richaud, P., Barbier‐Brygoo, H., Aarts, M. G. M., & Thomine, S. (2009) · New Phytologist · doi:10.1111/j.1469-8137.2008.02694.x · Cited by 270 · see citing works
Regulation of Cation Balance inSaccharomyces cerevisiae
Cyert, M., & Philpott, C. C. (2013) · Genetics · doi:10.1534/genetics.112.147207 · Cited by 253 · see citing works
Metals in fungal virulence
Gerwien, F., Skrahina, V., Kasper, L., Hube, B., & Brunke, S. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux050 · Cited by 246 · see citing works
Zn(II) metabolism in prokaryotes
Blencowe, D. K., & Morby, A. P. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00041-x · Cited by 247 · see citing works
SLC11A1 (formerly NRAMP1) and disease resistance. Microreview
Blackwell, J. M., Goswami, T., Evans, C. A., Sibthorpe, D., Papo, N., White, J. K., Searle, S., Miller, E. N., Peacock, C. S., Mohammed, H., et al. (2001) · Cellular Microbiology · doi:10.1046/j.1462-5822.2001.00150.x · Cited by 242 · see citing works
Identification of the Escherichia coli K‐12 Nramp orthologue (MntH) as a selective divalent metal ion transporter
Makui, H., Roig, E. A., Cole, S. T., Helmann, J. D., Gros, P., & Cellier, M. F. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01774.x · Cited by 237 · see citing works
Human NRAMP2/DMT1, Which Mediates Iron Transport across Endosomal Membranes, Is Localized to Late Endosomes and Lysosomes in HEp-2 Cells
Tabuchi, M., Yoshimori, T., Yamaguchi, K., Yoshida, T., & Kishi, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001478200 · Cited by 236 · see citing works
AtIREG2 Encodes a Tonoplast Transport Protein Involved in Iron-dependent Nickel Detoxification in Arabidopsis thaliana Roots
Schaaf, G., Honsbein, A., Meda, A. R., Kirchner, S., Wipf, D., & von Wirén, N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601062200 · Cited by 236 · see citing works
Manganese transport in eukaryotes: The role of DMT1
Au, C., Benedetto, A., & Aschner, M. (2008) · NeuroToxicology · doi:10.1016/j.neuro.2008.04.022 · Cited by 231 · see citing works
Transition metal homeostasis: from yeast to human disease
Bleackley, M. R., & MacGillivray, R. T. A. (2011) · BioMetals · doi:10.1007/s10534-011-9451-4 · Cited by 232 · see citing works
Susceptibility to mycobacterial infections: the importance of host genetics
Bellamy, R. (2003) · Genes and Immunity · doi:10.1038/sj.gene.6363915 · Cited by 227 · see citing works
Transition Metal Transport in Yeast
Ho, A. V., Ward, D. M., & Kaplan, J. (2002) · Annual Review of Microbiology · doi:10.1146/annurev.micro.56.012302.160847 · Cited by 225 · see citing works
The G185R Mutation Disrupts Function of the Iron Transporter Nramp2
Su, M. A., Trenor, C. C., Fleming, J. C., Fleming, M. D., & Andrews, N. C. (1998) · Blood · doi:10.1182/blood.v92.6.2157 · Cited by 220 · see citing works
OsZIP5 is a plasma membrane zinc transporter in rice
Lee, S., Jeong, H. J., Kim, S. A., Lee, J., Guerinot, M. L., & An, G. (2010) · Plant Molecular Biology · doi:10.1007/s11103-010-9637-0 · Cited by 223 · see citing works
Iron and copper transport in yeast and its relevance to human disease
Askwith, C. C., & Kaplan, J. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01192-x · Cited by 220 · see citing works
Manganese Efficiency in Barley: Identification and Characterization of the Metal Ion Transporter HvIRT1
Pedas, P., Ytting, C. K., Fuglsang, A. T., Jahn, T. P., Schjoerring, J. K., & Husted, S. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.118851 · Cited by 218 · see citing works
Overexpression of the Saccharomyces cerevisiaeMagnesium Transport System Confers Resistance to Aluminum Ion
MacDiarmid, C. W., & Gardner, R. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1727 · Cited by 217 · see citing works
Saccharomyces cerevisiae Expresses Three Functionally Distinct Homologues of the Nramp Family of Metal Transporters
Portnoy, M. E., Liu, X. F., & Culotta, V. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.21.7893-7902.2000 · Cited by 218 · see citing works
Poplar metal tolerance protein 1 confers zinc tolerance and is an oligomeric vacuolar zinc transporter with an essential leucine zipper motif
Blaudez, D., Kohler, A., Martin, F., Sanders, D., & Chalot, M. (2003) · The Plant Cell · doi:10.1105/tpc.017541 · Cited by 200 · see citing works
Host Resistance to Intracellular Infection: Mutation of Natural Resistance-associated Macrophage Protein 1 (Nramp1) Impairs Phagosomal Acidification
Hackam, D. J., Rotstein, O. D., Zhang, W.-J., Gruenheid, S., Gros, P., & Grinstein, S. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.2.351 · Cited by 202 · see citing works
A Homolog of Mammalian, Voltage-Gated Calcium Channels Mediates Yeast Pheromone-Stimulated Ca 2+ Uptake and Exacerbates the cdc1 (Ts) Growth Defect
Paidhungat, M., & Garrett, S. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6339 · Cited by 191 · see citing works
Molecular characterization of a rice metal tolerance protein, OsMTP1
Yuan, L., Yang, S., Liu, B., Zhang, M., & Wu, K. (2011) · Plant Cell Reports · doi:10.1007/s00299-011-1140-9 · Cited by 186 · see citing works
Negative Control of Heavy Metal Uptake by the Saccharomyces cerevisiae BSD2 Gene
Liu, X. F., Supek, F., Nelson, N., & Culotta, V. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.18.11763 · Cited by 184 · see citing works
The soybean NRAMP homologue, GmDMT1, is a symbiotic divalent metal transporter capable of ferrous iron transport
Kaiser, B. N., Moreau, S., Castelli, J. M., Thomson, R., Lambert, A., Bogliolo, S., Puppo, A., & Day, D. A. (2003) · The Plant Journal · doi:10.1046/j.1365-313x.2003.01802.x · Cited by 181 · see citing works
Manganese Transport and Trafficking: Lessons Learned from Saccharomyces cerevisiae
Culotta, V., Yang, M., & Hall, M. D. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.7.1159-1165.2005 · Cited by 179 · see citing works
OsYSL6 Is Involved in the Detoxification of Excess Manganese in Rice
Sasaki, A., Yamaji, N., Xia, J., & Feng, J. X. (2011) · PLANT PHYSIOLOGY · doi:10.1104/pp.111.186031 · Cited by 175 · see citing works
A Comparative Inventory of Metal Transporters in the Green Alga Chlamydomonas reinhardtii and the Red Alga Cyanidioschizon merolae
Hanikenne, M., Krämer, U., Demoulin, V., & Baurain, D. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.054189 · Cited by 174 · see citing works
The Saccharomyces cerevisiae High Affinity Phosphate Transporter Encoded by PHO84 Also Functions in Manganese Homeostasis
Jensen, L. T., Ajua-Alemanji, M., & Culotta, V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307413200 · Cited by 173 · see citing works
Fungal–Metal Interactions: A Review of Toxicity and Homeostasis
Robinson, J. R., Isikhuemhen, O. S., & Anike, F. N. (2021) · Journal of Fungi · doi:10.3390/jof7030225 · Cited by 180 · see citing works
Manganese Deficiency in Chlamydomonas Results in Loss of Photosystem II and MnSOD Function, Sensitivity to Peroxides, and Secondary Phosphorus and Iron Deficiency
Allen, M. D., Kropat, J., Tottey, S., Campo, J. A. D., & Merchant, S. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.088609 · Cited by 166 · see citing works
Macrophage NRAMP1 and its role in resistance to microbial infections
Govoni, G. R., & Gros, P. (1998) · Inflammation Research · doi:10.1007/s000110050330 · Cited by 163 · see citing works
The Nramp1 Protein and Its Role in Resistance to Infection and Macrophage Function
Canonne‐Hergaux, F., Gruenheid, S., Govoni, G., & Gros, P. (1999) · Proceedings of the Association of American Physicians · doi:10.1046/j.1525-1381.1999.99236.x · Cited by 159 · see citing works
Localisation of Nramp1 in macrophages: Modulation with activation and infection
Searle, S., Bright, N. A., Roach, T. I. A., Atkinson, P. G. P., Barton, C. H., Meloen, R. H., & Blackwell, J. M. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.19.2855 · Cited by 158 · see citing works
Cloning and characterization of the OsNramp family from Oryza sativa, a new family of membrane proteins possibly implicated in the transport of metal ions
Belouchi, A., Kwan, T., & Gros, P. (1997) · Plant Molecular Biology · doi:10.1023/a:1005723304911 · Cited by 157 · see citing works
Role of Iron inNramp1-Mediated Inhibition of Mycobacterial Growth
Zwilling, B. S., Kuhn, D. E., Wikoff, L., Brown, D., & Lafuse, W. (1999) · Infection and Immunity · doi:10.1128/iai.67.3.1386-1392.1999 · Cited by 155 · see citing works
Natural-resistance-associated macrophage protein 1 is an H+/bivalent cation antiporter
GOSWAMI, T., BHATTACHARJEE, A., BABAL, P., SEARLE, S., MOORE, E., LI, M., & BLACKWELL, J. M. (2001) · Biochemical Journal · doi:10.1042/bj3540511 · Cited by 218 · see citing works
Yeast SMF1 Mediates H+-coupled Iron Uptake with Concomitant Uncoupled Cation Currents
Chen, X., Peng, J., Cohen, A., Nelson, H. R., Nelson, N., & Hediger, M. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.35089 · Cited by 146 · see citing works
Post-translation Control of Nramp Metal Transport in Yeast
Liu, X. F., & Culotta, V. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4863 · Cited by 145 · see citing works
Regulation of Transition Metal Transport across the Yeast Plasma Membrane
Radisky, D. C., & Kaplan, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4481 · Cited by 145 · see citing works
The Family of SMF Metal Ion Transporters in Yeast Cells
Cohen, A., Nelson, H. R., & Nelson, N. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004611200 · Cited by 141 · see citing works
Infection Genomics:Nramp1as a Major Determinant of Natural Resistance to Intracellular Infections
Skamene, E., Schurr, E., & Gros, P. (1998) · Annual Review of Medicine · doi:10.1146/annurev.med.49.1.275 · Cited by 139 · see citing works
Manganese Superoxide Dismutase in Saccharomyces cerevisiae Acquires Its Metal Co-factor through a Pathway Involving the Nramp Metal Transporter, Smf2p
Luk, E., & Culotta, V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108923200 · Cited by 137 · see citing works
Understanding the multiple functions of Nramp1
Blackwell, J. M., Searle, S., Goswami, T., & Miller, E. N. (2000) · Microbes and Infection · doi:10.1016/s1286-4579(00)00295-1 · Cited by 136 · see citing works
Identification of mutations allowing Natural Resistance Associated Macrophage Proteins (NRAMP) to discriminate against cadmium
Pottier, M., Oomen, R. J. F. J., Picco, C., Giraudat, J., Scholz‐Starke, J., Richaud, P., Carpaneto, A., & Thomine, S. (2015) · The Plant Journal · doi:10.1111/tpj.12914 · Cited by 136 · see citing works
Genome-wide association study and candidate gene analysis of rice cadmium accumulation in grain in a diverse rice collection
Zhao, J., Wu, Y., Zhang, S., Yang, T., Liu, Q., Dong, J., Fu, H., Mao, X., & Liu, B. (2018) · Rice · doi:10.1186/s12284-018-0254-x · Cited by 135 · see citing works
Manganese Homeostasis in Saccharomyces cerevisiae
Reddi, A. R., Jensen, L. T., & Culotta, V. (2009) · Chemical Reviews · doi:10.1021/cr900031u · Cited by 134 · see citing works
Recent progress in structure–function analyses of Nramp proton-dependent metal-ion transportersThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB — Membrane Proteins in Health and Disease.
Courville, P., Chaloupka, R., & Cellier, M. F. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-193 · Cited by 132 · see citing works
Mycobacterium tuberculosis Expresses a Novel Ph-Dependent Divalent Cation Transporter Belonging to the Nramp Family
Agranoff, D. D., Monahan, I. M., Mangan, J. A., Butcher, P. D., & Krishna, S. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.5.717 · Cited by 130 · see citing works
The Adhesion-Associated sca Operon in Streptococcus gordonii Encodes an Inducible High-Affinity ABC Transporter for Mn 2+ Uptake
Kolenbrander, P. E., Andersen, R. N., Baker, R. A., & Jenkinson, H. F. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.2.290-295.1998 · Cited by 124 · see citing works
Phenotypic deconstruction reveals involvement of manganese transportermalvolioin honey bee division of labor
Ben‐Shahar, Y., Dudek, N. L., & Robinson, G. E. (2004) · Journal of Experimental Biology · doi:10.1242/jeb.01151 · Cited by 123 · see citing works
SLC11 family of H + -coupled metal-ion transporters NRAMP1 and DMT1
Mackenzie, B., & Hediger, M. A. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1141-9 · Cited by 123 · see citing works
Kinetic properties of a micronutrient transporter from Pisum sativum indicate a primary function in Fe uptake from the soil
Garvin, D. F., Kochian, L. V., & Cohen, C. K. (2004) · Planta · doi:10.1007/s00425-003-1156-7 · Cited by 119 · see citing works
The many highways for intracellular trafficking of metals
Luk, E., Jensen, L. T., & Culotta, V. (2003) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-003-0482-3 · Cited by 118 · see citing works
The metal transporter PgIREG1 from the hyperaccumulator Psychotria gabriellae is a candidate gene for nickel tolerance and accumulation
Merlot, S., Hannibal, L., Martins, S., Martinelli, L., Amir, H., Lebrun, M., & Thomine, S. (2014) · Journal of Experimental Botany · doi:10.1093/jxb/eru025 · Cited by 119 · see citing works
Molecular Mechanism of Nramp-Family Transition Metal Transport
Bozzi, A. T., & Gaudet, R. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166991 · Cited by 114 · see citing works
Functional Complementation of the Yeast Divalent Cation Transporter Family SMF by NRAMP2, a Member of the Mammalian Natural Resistance-associated Macrophage Protein Family
Pinner, E., Gruenheid, S., Raymond, M., & Gros, P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.28933 · Cited by 115 · see citing works
Differential iron transport into phagosomes isolated from the RAW264.7 macrophage cell lines transfected with Nramp1Gly169 or Nramp1Asp169
Kuhn, D. E., Baker, B. D., Lafuse, W. P., & Zwilling, B. S. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.66.1.113 · Cited by 113 · see citing works
Expression of the two mRNA isoforms of the iron transporter Nrmap2/DMTI in mice and function of the iron responsive element
Tchernitchko, D., Bourgeois, M., Martin, M., & Beaumont, C. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630449 · Cited by 110 · see citing works
Attenuation of MHC Class II Expression in Macrophages Infected with Mycobacterium bovis Bacillus Calmette-Guerin Involves Class II Transactivator and Depends on the Nramp1 Gene
Wojciechowski, W., Sanctis, J. B. D., Skamene, E., & Radzioch, D. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.5.2688 · Cited by 109 · see citing works
Intracellular Distribution of Manganese by the Trans-Golgi Network Transporter NRAMP2 Is Critical for Photosynthesis and Cellular Redox Homeostasis
Alejandro, S., Cailliatte, R., Alcon, C., Dirick, L., Domergue, F., Correia, D., Castaings, L., Briat, J., Mari, S., & Curie, C. (2017) · The Plant Cell · doi:10.1105/tpc.17.00578 · Cited by 105 · see citing works
SMF-1, SMF-2 and SMF-3 DMT1 Orthologues Regulate and Are Regulated Differentially by Manganese Levels in C. elegans
Au, C., Benedetto, A., Anderson, J. G., Labrousse, A. M., Erikson, K. M., Ewbank, J. J., & Aschner, M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007792 · Cited by 103 · see citing works
Medicago truncatula Natural Resistance-Associated Macrophage Protein1 Is Required for Iron Uptake by Rhizobia-Infected Nodule Cells
Tejada‐Jiménez, M., Castro‐Rodríguez, R., Kryvoruchko, I., Lucas, M. M., Udvardi, M. K., Imperial, J., & González‐Guerrero, M. (2015) · PLANT PHYSIOLOGY · doi:10.1104/pp.114.254672 · Cited by 101 · see citing works

Function Of Metal-Ion Homeostasis In The Cell Division Cycle, Mitochondrial Protein Processing, Sensitivity To Mycobacterial Infection And Brain Function
Supek, F., Supeková, Ľ., Nelson, H. R., & Nelson, N. (1997) · Journal of Experimental Biology · doi:10.1242/jeb.200.2.321 · Cited by 74 · see citing works
Functional characterization of the manganese transporter smf2 homologue gene, PsMnt, of Phanerochaete sordida YK-624 via homologous overexpression
Mori, T., Nagai, Y., Kawagishi, H., & Hirai, H. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny050 · Cited by 11 · see citing works
Mutants resistant to manganese in Saccharomyces cerevisiae
Bianchi, M. E., Carbone, M. L., Lucchini, G., & Magni, G. E. (1981) · Current Genetics · doi:10.1007/bf00420501 · Cited by 19 · see citing works
Manganese Superoxide Dismutase in Saccharomyces cerevisiae Acquires Its Metal Co-factor through a Pathway Involving the Nramp Metal Transporter, Smf2p
Luk, E., & Culotta, V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108923200 · Cited by 137 · see citing works
Genes Encoding Proteins of the Cation Diffusion Facilitator Family That Confer Manganese Tolerance
Delhaize, E., Kataoka, T., Hebb, D. M., White, R. G., & Ryan, P. R. (2003) · The Plant Cell · doi:10.1105/tpc.009134 · Cited by 261 · see citing works

Authors: Supek, F., Supekova, L., Nelson, H., & Nelson, N.
Affiliations: Roche Institute of Molecular Biology, Nutley, NJ 07110, USA.
ORCID: Nelson, H
Nelson, N
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1996-05-14
Volume: 93
Issue: 10
Pages: 5105-5110
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.93.10.5105
PMC: PMC39414
OpenAlex: W2015326313
Cited by: 325
References: 41
Citations by year: 2026: 1 · 2024: 4 · 2023: 7 · 2022: 10 · 2021: 11 · 2020: 9 · 2019: 8 · 2018: 6 · 2017: 8 · 2016: 3 · 2015: 10 · 2014: 9 · 2013: 5 · 2012: 5
FWCI: 10.74
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Heavy Metal Exposure and Toxicity
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Keywords: manganese transporter, manganese deficiency, plasma membrane proteins, mitochondrial processing peptidase, Mas receptor, extragenic suppressors, Saccharomyces cerevisiae mutants
MeSH terms: Mitochondrial Processing Peptidase, Amino Acid Sequence, Animals, Biological Transport, Active, Carrier Proteins, Fungal Proteins, Genes, Fungal, Genetic Complementation Test, Macrophages, Manganese, Membrane Proteins, Metalloendopeptidases, Molecular Sequence Data, Mycobacterium, Phenotype, Saccharomyces cerevisiae, Point Mutation

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria.

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks