Reference health
Phytoremediation of methylmercury pollution: <i>merB</i> expression in <i>Arabidopsis thaliana</i> confers resistance to organomercurials
27/27 checkable references clean · checked 2026-07-23
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
15 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 27 checked references that resolve
resolves10.1016/0009-2797(92)90053-N
The mechanism of Hg2+ toxicity in cultured human oral fibroblasts: The involvement of cellular thiols
resolves10.1021/ja01646a025
Spectrophotometric Study of the Reaction of Protein Sulfhydryl Groups with Organic Mercurials
resolves10.1073/pnas.93.8.3182
Mercuric ion reduction and resistance in transgenic Arabidopsis thaliana plants expressing a modified bacterial merA gene.
resolves10.1139/f72-240
Methylmercury in Northern Pike (<i>Esox lucius</i>): Distribution, Elimination, and Some Biochemical Characteristics of Contaminated Fish
resolves10.1128/aem.50.2.498-502.1985
Sulfate-Reducing Bacteria: Principal Methylators of Mercury in Anoxic Estuarine Sediment
resolves10.1128/aem.60.11.4072-4077.1994
Metabolic Pathways Leading to Mercury Methylation in
<i>Desulfovibrio desulfuricans</i>
LS
resolves10.1128/aem.60.4.1342-1346.1994
Enzymatic catalysis of mercury methylation by Desulfovibrio desulfuricans LS
resolves10.1128/aem.59.8.2479-2485.1993
Methylmercury Resistance in
<i>Desulfovibrio desulfuricans</i>
Strains in Relation to Methylmercury Degradation
resolves10.1021/bi00370a064
Mechanistic studies of a protonolytic organomercurial cleaving enzyme: bacterial organomercurial lyase
resolves10.1016/S0021-9258(18)34951-2
Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide.
resolves10.1146/annurev.mi.40.100186.003135
Organization, Expression, and Evolution of Genes for Mercury Resistance
resolves10.1128/jb.174.20.6377-6385.1992
Roles of the Tn21 merT, merP, and merC gene products in mercury resistance and mercury binding
resolves10.1016/0378-1119(84)90006-4
Physical and genetic map of the organomercury resistance (Omr) and inorganic mercury resistance (Hgr) loci of the IncM plasmid R831b
resolves10.1126/science.8091210
RPS2 of
<i>Arabidopsis thaliana</i>
: a Leucine-Rich Repeat Class of Plant Disease Resistance Genes
resolves10.1002/j.1460-2075.1985.tb02309.x
Divergence and differential expression of soybean actin genes.
resolves10.1038/227680a0
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
resolves10.1038/256495a0
Continuous cultures of fused cells secreting antibody of predefined specificity
resolves10.1007/BF02102358
Comparison of the nucleotide sequence of soybean 18S rRNA with the sequences of other small-subunit rRNAs
The 15 references without a DOI — listed, not checked
no DOI — not checkedKeating M. H. Mahaffey K. R. Schoeny R. Rice G. E. Bullock O. R. Ambrose R. B. Swartout J. & Nichols J. W. (1997) (U.S. Environmental Protection Agency Washington DC) 2 1–2:9.
no DOI — not checkedA J Carty, S F Malone The Chemistry of Mercury in Biological Systems, ed J O Nriagu (Elsevier Biomedical, Amsterdam), pp. 433–479 (1979).
no DOI — not checkedK H Falchuk, L J Goldwater, B L Vallee The Biochemistry and Toxicology of Mercury, ed C A McAuliffe (Macmillan, New York), pp. 261–284 (1977).
no DOI — not checkedA W Andren, J O Nriagu The Global Cycle of Mercury, ed J O Nriagu (Elsevier Biomedical, Amsterdam), pp. 1–21 (1979).
no DOI — not checkedMinamata Disease (Medical School of Kumamoto University, Kumamoto, Japan, 1968).
no DOI — not checkedS Jensen, A Jernelov Nordforsk Biocidinformation 10, 4 (1967).
no DOI — not checkedR B Meagher, C L Rugh, M K Kandasamy, G Gragson, N J Wang Fourth International Conference on the Biogeochemistry of Trace Elements, eds I K Ishndar, S E Hardy, A C Chang, G M Pierzynski (Ann Arbor Press, Berkeley, CA, 1998).
no DOI — not checkedD E Salt, M Blaylock, N P B A Kumar, V Dushenkov, B D Ensley, I Chet, I Raskin Biotechnology 13, 468–474 (1995).
no DOI — not checkedS R Kushner An Improved Method for Transformation of Escherichia coli with ColE1 Derived Plasmids, eds H W Boyer, S Nicosia (Elsevier/North–Holland, New York), pp. 17–23 (1978).
no DOI — not checkedC T Tolle M.S. thesis (Univ. of Georgia, Athens, GA, 1985).
no DOI — not checked, eds F Ausubel, R Kingston, D Moore, J Seidman, J Smith, K Struhl (Wiley, New York Current Protocols in Molecular Biology, 1988).
no DOI — not checkedJ Sambrook, E F Fritsch, T Maniatis Molecular Cloning: A Laboratory Manual (Cold Spring Harbor Lab. Press, 2nd Ed., Plainview, NY, 1989).
no DOI — not checkedT W Clarkson The Toxicology of Mercury and Its Compounds, eds C J Watras, J W Huckabee (Lewis, Ann Arbor, MI), pp. 631–642 (1994).
no DOI — not checkedA Cornish-Bowden Fundamentals of Enzyme Kinetics (Butterworth, Boston, 1979).
no DOI — not checkedL A Smith, J L Means, A Chen, B Alleman, C C Chapman, J S Tixier, S E Brauning, A R Gavaskar, M D Royer Remedial Options for Contaminated Sites (CRC, Boca Raton, FL, 1995).
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