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Low molecular weight cadmium-and copper-binding proteins from rat kidneys.

Biological trace element research

Zelazowski AJ, Szymańska JA.
PMID: 24272895
Biol Trace Elem Res. 1980 Jun;2(2):137-48. doi: 10.1007/BF02798592.

Three isoforms of rat kidney cadmium- and copper-binding proteins [(Cd, Cu)-BP 1, 2, and 3] were isolated. They contained from 75.0 up to 89.0 μg Cd/mg protein, from 7.5 up to 28.0 μg Cu/mg, and from 1.5 up to...

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Zelazowski AJ, Szymańska JA. Low molecular weight cadmium-and copper-binding proteins from rat kidneys. Biol Trace Elem Res. 1980;2(2):137-48doi: 10.1007/BF02798592.
Zelazowski, A. J., & Szymańska, J. A. (1980). Low molecular weight cadmium-and copper-binding proteins from rat kidneys. Biological trace element research, 2(2), 137-48. https://doi.org/10.1007/BF02798592
Zelazowski, A J, and Szymańska, J A. "Low molecular weight cadmium-and copper-binding proteins from rat kidneys." Biological trace element research vol. 2,2 (1980): 137-48. doi: https://doi.org/10.1007/BF02798592
Zelazowski AJ, Szymańska JA. Low molecular weight cadmium-and copper-binding proteins from rat kidneys. Biol Trace Elem Res. 1980 Jun;2(2):137-48. doi: 10.1007/BF02798592. PMID: 24272895.
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The possible role of metallothioneins in copper tolerance of Silene cucubalus.

Planta

Lolkema PC, Donker MH, Schouten AJ, Ernst WH.
PMID: 24254053
Planta. 1984 Sep;162(2):174-9. doi: 10.1007/BF00410215.

Growth and copper-binding of a copper-tolerant and a copper-sensitive population of Silene cucubalus (L.) Wib. have been studied. The copper-tolerant plants showed a much lower uptake and a proportionally higher transport of copper from root to shoot. A copper-binding...

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Lolkema PC, Donker MH, Schouten AJ, et al. The possible role of metallothioneins in copper tolerance of Silene cucubalus. Planta. 1984;162(2):174-9doi: 10.1007/BF00410215.
Lolkema, P. C., Donker, M. H., Schouten, A. J., & Ernst, W. H. (1984). The possible role of metallothioneins in copper tolerance of Silene cucubalus. Planta, 162(2), 174-9. https://doi.org/10.1007/BF00410215
Lolkema, P C, et al. "The possible role of metallothioneins in copper tolerance of Silene cucubalus." Planta vol. 162,2 (1984): 174-9. doi: https://doi.org/10.1007/BF00410215
Lolkema PC, Donker MH, Schouten AJ, Ernst WH. The possible role of metallothioneins in copper tolerance of Silene cucubalus. Planta. 1984 Sep;162(2):174-9. doi: 10.1007/BF00410215. PMID: 24254053.
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Neuroprotective alpha-cleavage of the human prion protein significantly impacts Cu(ii) coordination at its His111 site.

Dalton transactions (Cambridge, England : 2003)

Sánchez-López C, Fernández CO, Quintanar L.
PMID: 29417110
Dalton Trans. 2018 Jul 17;47(28):9274-9282. doi: 10.1039/c7dt03400h.

The cellular prion protein (PrPC) is a copper binding protein that undergoes post-translational modifications, such as endoproteolytic alpha cleavage, which occurs in the vicinity of the His111 Cu binding site. Alpha cleavage processing of PrPC is considered to be...

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Sánchez-López C, Fernández CO, Quintanar L. Neuroprotective alpha-cleavage of the human prion protein significantly impacts Cu(ii) coordination at its His111 site. Dalton Trans. 2018;47(28):9274-9282doi: 10.1039/c7dt03400h.
Sánchez-López, C., Fernández, C. O., & Quintanar, L. (2018). Neuroprotective alpha-cleavage of the human prion protein significantly impacts Cu(ii) coordination at its His111 site. Dalton transactions (Cambridge, England : 2003), 47(28), 9274-9282. https://doi.org/10.1039/c7dt03400h
Sánchez-López, Carolina, et al. "Neuroprotective alpha-cleavage of the human prion protein significantly impacts Cu(ii) coordination at its His111 site." Dalton transactions (Cambridge, England : 2003) vol. 47,28 (2018): 9274-9282. doi: https://doi.org/10.1039/c7dt03400h
Sánchez-López C, Fernández CO, Quintanar L. Neuroprotective alpha-cleavage of the human prion protein significantly impacts Cu(ii) coordination at its His111 site. Dalton Trans. 2018 Jul 17;47(28):9274-9282. doi: 10.1039/c7dt03400h. PMID: 29417110.
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The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.

The Journal of biological chemistry

Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O.
PMID: 34822841
J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23.

The Escherichia coli yobA-yebZ-yebY (AZY) operon encodes the proteins YobA, YebZ, and YebY. YobA and YebZ are homologs of the CopC periplasmic copper-binding protein and the CopD putative copper importer, respectively, whereas YebY belongs to the uncharacterized Domain of...

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Hadley RC, Zhitnitsky D, Livnat-Levanon N, et al. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021;298(1):101445doi: 10.1016/j.jbc.2021.101445.
Hadley, R. C., Zhitnitsky, D., Livnat-Levanon, N., Masrati, G., Vigonsky, E., Rose, J., Ben-Tal, N., Rosenzweig, A. C., & Lewinson, O. (2021). The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. The Journal of biological chemistry, 298(1), 101445. https://doi.org/10.1016/j.jbc.2021.101445
Hadley, Rose C, et al. "The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery." The Journal of biological chemistry vol. 298,1 (2021): 101445. doi: https://doi.org/10.1016/j.jbc.2021.101445
Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23. PMID: 34822841; PMCID: PMC8689200.
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The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.

The Journal of biological chemistry

Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O.
PMID: 34822841
J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23.

The Escherichia coli yobA-yebZ-yebY (AZY) operon encodes the proteins YobA, YebZ, and YebY. YobA and YebZ are homologs of the CopC periplasmic copper-binding protein and the CopD putative copper importer, respectively, whereas YebY belongs to the uncharacterized Domain of...

Cite
Hadley RC, Zhitnitsky D, Livnat-Levanon N, et al. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021;298(1):101445doi: 10.1016/j.jbc.2021.101445.
Hadley, R. C., Zhitnitsky, D., Livnat-Levanon, N., Masrati, G., Vigonsky, E., Rose, J., Ben-Tal, N., Rosenzweig, A. C., & Lewinson, O. (2021). The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. The Journal of biological chemistry, 298(1), 101445. https://doi.org/10.1016/j.jbc.2021.101445
Hadley, Rose C, et al. "The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery." The Journal of biological chemistry vol. 298,1 (2021): 101445. doi: https://doi.org/10.1016/j.jbc.2021.101445
Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23. PMID: 34822841; PMCID: PMC8689200.
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The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.

The Journal of biological chemistry

Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O.
PMID: 34822841
J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23.

The Escherichia coli yobA-yebZ-yebY (AZY) operon encodes the proteins YobA, YebZ, and YebY. YobA and YebZ are homologs of the CopC periplasmic copper-binding protein and the CopD putative copper importer, respectively, whereas YebY belongs to the uncharacterized Domain of...

Cite
Hadley RC, Zhitnitsky D, Livnat-Levanon N, et al. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021;298(1):101445doi: 10.1016/j.jbc.2021.101445.
Hadley, R. C., Zhitnitsky, D., Livnat-Levanon, N., Masrati, G., Vigonsky, E., Rose, J., Ben-Tal, N., Rosenzweig, A. C., & Lewinson, O. (2021). The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. The Journal of biological chemistry, 298(1), 101445. https://doi.org/10.1016/j.jbc.2021.101445
Hadley, Rose C, et al. "The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery." The Journal of biological chemistry vol. 298,1 (2021): 101445. doi: https://doi.org/10.1016/j.jbc.2021.101445
Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23. PMID: 34822841; PMCID: PMC8689200.
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The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.

The Journal of biological chemistry

Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O.
PMID: 34822841
J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23.

The Escherichia coli yobA-yebZ-yebY (AZY) operon encodes the proteins YobA, YebZ, and YebY. YobA and YebZ are homologs of the CopC periplasmic copper-binding protein and the CopD putative copper importer, respectively, whereas YebY belongs to the uncharacterized Domain of...

Cite
Hadley RC, Zhitnitsky D, Livnat-Levanon N, et al. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021;298(1):101445doi: 10.1016/j.jbc.2021.101445.
Hadley, R. C., Zhitnitsky, D., Livnat-Levanon, N., Masrati, G., Vigonsky, E., Rose, J., Ben-Tal, N., Rosenzweig, A. C., & Lewinson, O. (2021). The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. The Journal of biological chemistry, 298(1), 101445. https://doi.org/10.1016/j.jbc.2021.101445
Hadley, Rose C, et al. "The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery." The Journal of biological chemistry vol. 298,1 (2021): 101445. doi: https://doi.org/10.1016/j.jbc.2021.101445
Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23. PMID: 34822841.
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The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.

The Journal of biological chemistry

Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O.
PMID: 34822841
J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23.

The Escherichia coli yobA-yebZ-yebY (AZY) operon encodes the proteins YobA, YebZ, and YebY. YobA and YebZ are homologs of the CopC periplasmic copper-binding protein and the CopD putative copper importer, respectively, whereas YebY belongs to the uncharacterized Domain of...

Cite
Hadley RC, Zhitnitsky D, Livnat-Levanon N, et al. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021;298(1):101445doi: 10.1016/j.jbc.2021.101445.
Hadley, R. C., Zhitnitsky, D., Livnat-Levanon, N., Masrati, G., Vigonsky, E., Rose, J., Ben-Tal, N., Rosenzweig, A. C., & Lewinson, O. (2021). The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. The Journal of biological chemistry, 298(1), 101445. https://doi.org/10.1016/j.jbc.2021.101445
Hadley, Rose C, et al. "The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery." The Journal of biological chemistry vol. 298,1 (2021): 101445. doi: https://doi.org/10.1016/j.jbc.2021.101445
Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23. PMID: 34822841.
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The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.

The Journal of biological chemistry

Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O.
PMID: 34822841
J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23.

The Escherichia coli yobA-yebZ-yebY (AZY) operon encodes the proteins YobA, YebZ, and YebY. YobA and YebZ are homologs of the CopC periplasmic copper-binding protein and the CopD putative copper importer, respectively, whereas YebY belongs to the uncharacterized Domain of...

Cite
Hadley RC, Zhitnitsky D, Livnat-Levanon N, et al. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021;298(1):101445doi: 10.1016/j.jbc.2021.101445.
Hadley, R. C., Zhitnitsky, D., Livnat-Levanon, N., Masrati, G., Vigonsky, E., Rose, J., Ben-Tal, N., Rosenzweig, A. C., & Lewinson, O. (2021). The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. The Journal of biological chemistry, 298(1), 101445. https://doi.org/10.1016/j.jbc.2021.101445
Hadley, Rose C, et al. "The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery." The Journal of biological chemistry vol. 298,1 (2021): 101445. doi: https://doi.org/10.1016/j.jbc.2021.101445
Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23. PMID: 34822841.
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APEX2-based Proximity Labeling of Atox1 Identifies CRIP2 as a Nuclear Copper-binding Protein that Regulates Autophagy Activation.

Angewandte Chemie (International ed. in English)

Chen L, Li N, Zhang M, Sun M, Bian J, Yang B, Li Z, Wang J, Li F, Shi X, Wang Y, Yuan F, Zou P, Shan C, Wang J.
PMID: 34550632
Angew Chem Int Ed Engl. 2021 Nov 22;60(48):25346-25355. doi: 10.1002/anie.202108961. Epub 2021 Oct 27.

Mammalian cell nuclei contain copper, and cancer cells are known to accumulate aberrantly high copper levels, yet the mechanisms underlying nuclear accumulation and copper's broader functional significance remain poorly understood. Here, by combining APEX2-based proximity labeling focused on the...

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Chen L, Li N, Zhang M, et al. APEX2-based Proximity Labeling of Atox1 Identifies CRIP2 as a Nuclear Copper-binding Protein that Regulates Autophagy Activation. Angew Chem Int Ed Engl. 2021;60(48):25346-25355doi: 10.1002/anie.202108961.
Chen, L., Li, N., Zhang, M., Sun, M., Bian, J., Yang, B., Li, Z., Wang, J., Li, F., Shi, X., Wang, Y., Yuan, F., Zou, P., Shan, C., & Wang, J. (2021). APEX2-based Proximity Labeling of Atox1 Identifies CRIP2 as a Nuclear Copper-binding Protein that Regulates Autophagy Activation. Angewandte Chemie (International ed. in English), 60(48), 25346-25355. https://doi.org/10.1002/anie.202108961
Chen, Lin, et al. "APEX2-based Proximity Labeling of Atox1 Identifies CRIP2 as a Nuclear Copper-binding Protein that Regulates Autophagy Activation." Angewandte Chemie (International ed. in English) vol. 60,48 (2021): 25346-25355. doi: https://doi.org/10.1002/anie.202108961
Chen L, Li N, Zhang M, Sun M, Bian J, Yang B, Li Z, Wang J, Li F, Shi X, Wang Y, Yuan F, Zou P, Shan C, Wang J. APEX2-based Proximity Labeling of Atox1 Identifies CRIP2 as a Nuclear Copper-binding Protein that Regulates Autophagy Activation. Angew Chem Int Ed Engl. 2021 Nov 22;60(48):25346-25355. doi: 10.1002/anie.202108961. Epub 2021 Oct 27. PMID: 34550632.
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The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.

The Journal of biological chemistry

Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O.
PMID: 34822841
J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23.

The Escherichia coli yobA-yebZ-yebY (AZY) operon encodes the proteins YobA, YebZ, and YebY. YobA and YebZ are homologs of the CopC periplasmic copper-binding protein and the CopD putative copper importer, respectively, whereas YebY belongs to the uncharacterized Domain of...

Cite
Hadley RC, Zhitnitsky D, Livnat-Levanon N, et al. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021;298(1):101445doi: 10.1016/j.jbc.2021.101445.
Hadley, R. C., Zhitnitsky, D., Livnat-Levanon, N., Masrati, G., Vigonsky, E., Rose, J., Ben-Tal, N., Rosenzweig, A. C., & Lewinson, O. (2021). The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. The Journal of biological chemistry, 298(1), 101445. https://doi.org/10.1016/j.jbc.2021.101445
Hadley, Rose C, et al. "The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery." The Journal of biological chemistry vol. 298,1 (2021): 101445. doi: https://doi.org/10.1016/j.jbc.2021.101445
Hadley RC, Zhitnitsky D, Livnat-Levanon N, Masrati G, Vigonsky E, Rose J, Ben-Tal N, Rosenzweig AC, Lewinson O. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J Biol Chem. 2021 Nov 23;298(1):101445. doi: 10.1016/j.jbc.2021.101445. Epub 2021 Nov 23. PMID: 34822841.
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Analysis of Copper-Binding Proteins in Rice Radicles Exposed to Excess Copper and Hydrogen Peroxide Stress.

Frontiers in plant science

Zhang H, Xia Y, Chen C, Zhuang K, Song Y, Shen Z.
PMID: 27582750
Front Plant Sci. 2016 Aug 17;7:1216. doi: 10.3389/fpls.2016.01216. eCollection 2016.

Copper (Cu) is an essential micronutrient for plants, but excess Cu can inactivate and disturb the protein function due to unavoidable binding to proteins at the cellular level. As a redox-active metal, Cu toxicity is mediated by the formation...

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Zhang H, Xia Y, Chen C, et al. Analysis of Copper-Binding Proteins in Rice Radicles Exposed to Excess Copper and Hydrogen Peroxide Stress. Front Plant Sci. 2016;7:1216doi: 10.3389/fpls.2016.01216.
Zhang, H., Xia, Y., Chen, C., Zhuang, K., Song, Y., & Shen, Z. (2016). Analysis of Copper-Binding Proteins in Rice Radicles Exposed to Excess Copper and Hydrogen Peroxide Stress. Frontiers in plant science, 71216. https://doi.org/10.3389/fpls.2016.01216
Zhang, Hongxiao, et al. "Analysis of Copper-Binding Proteins in Rice Radicles Exposed to Excess Copper and Hydrogen Peroxide Stress." Frontiers in plant science vol. 7 (2016): 1216. doi: https://doi.org/10.3389/fpls.2016.01216
Zhang H, Xia Y, Chen C, Zhuang K, Song Y, Shen Z. Analysis of Copper-Binding Proteins in Rice Radicles Exposed to Excess Copper and Hydrogen Peroxide Stress. Front Plant Sci. 2016 Aug 17;7:1216. doi: 10.3389/fpls.2016.01216. eCollection 2016. PMID: 27582750; PMCID: PMC4987373.
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