Dale Sanders

Last updated

Dale Sanders
Born (1953-05-13) 13 May 1953 (age 71) [1]
Alma mater
Awards FRS (2001)
Scientific career
Institutions
Thesis The regulation of ion transport in characean cells  (1978)
Website

Dale Sanders, FRS (born 13 May 1953) is a plant biologist and former Director of the John Innes Centre. [2] The centre is an institute for research in plant sciences and microbiology, in Norwich, England.

Contents

Education

Sanders was educated at The Hemel Hempstead School. He gained a Bachelor of Arts degree from the University of York reading Biology from 1971 to 1974, graduating with 1st Class Honours. [1]

Sanders did his PhD alongside Professor Enid AC MacRobbie FRS at Darwin College, Cambridge in 1978, in the Department of Plant Sciences. In 1993, Sanders earned his Sc.D. from the University of Cambridge.

Research

Sanders’ research explores the transport of ions across plant cell membranes [3]  and the roles of ions in signalling and nutrient status.

Sanders’ first significant finding during his PhD was to provide unequivocal evidence that inorganic anion uptake in plants is powered by a proton gradient [4] and showed how transport is regulated through intracellular ion concentrations. [5]

In subsequent research as a post-doc at Yale University School of Medicine he pioneered the first methods to measure and interpret the interplay between control of intracellular pH and activity of the plasma membrane proton pump. Showing how the regulation of the proton pump is controlled by – and in turn controls – intracellular pH. [6] This work on a fungus served as a paradigm for understanding the interplay of membrane transport and cellular homeostasis in fungal and plant cells.

On taking an academic position at the University of York, Sanders developed novel electrophysiological approaches to plant cellular signalling and membrane transport.

The Sanders lab demonstrated a key link between changes in cytosolic free calcium and photosynthetic activity, and through many technical developments showed how membrane transport at the plant vacuole is energised and regulated in response to physiological demand.

Sanders also developed a unified mathematical theory that explained complex kinetics of solute uptake in plants, [7] [8] along with having created the first methodology to measure transient changes in intracellular calcium levels in higher plants, and discovered that light/dark changes in photosynthetic activity were highly dependent on cytosolic changes in calcium. [9]

In the days before extensive molecular biology, Sanders discovered that the vacuolar proton pump of plants was essentially similar to mitochondrial ATPases. [10] He also adapted electrophysiological techniques first developed for exploration of neuronal channel properties to determine that pumps at vacuolar membranes exhibit kinetic responses to ion gradients that would not be predicted through biochemical means. [11] [12] [13] Parallel to this, he discovered that vacuolar membranes exhibit electrically-driven ion release. [14]

Using both electrophysiological and biochemical approaches, Sanders was able to establish for the first time in plants that metabolites can act as triggers for release of calcium (a cellular signal) from vacuoles. [15] [16] [17] [18] [19] [20]

Sanders established principles for biofortification of cereal crops with essential human mineral nutrients, [21]  and molecularly characterised calcium permeable channels. [22] Sanders also discovered and characterised the first (and only) yeast calcium channel [23] [24] and demonstrated how cell marking can be used to distinguish cell types for patch clamp studies. [25]

Sanders also had influence in the investigation into the roles of plant cyclic nucleotide-gated channels that were explored at an early stage of discovery [26] and resulted in a major collaborative publication with another lab demonstrating a key role in plant-bacterial symbiosis signalling. [27]

On top of his extensive discoveries, he has also written influential reviews on calcium signalling in plants, which have 3,300 combined citations on Google Scholar. [28] [29] [30]

To further his work on calcium channels, he then discovered that the TPC1 channel is the major pathway for ion exchange across plant vacuolar membranes. [31] Their speculations that the TPC1 channel is involved in Calcium-induced calcium release were proven for the first time in plants in work from Sanders’ lab. [32] He then established the principal molecular and cellular mechanisms for plant tolerance to manganese toxicity. [33]

Sanders has discovered the major mechanism of zinc accumulation in plant vacuoles, [34] and more recently characterised the molecular properties of the transporter [35] and showed how the transporter could be used for nutritional benefit for human consumption of cereal grains. [36] On top of further collaborating with a Chinese lab to establish more generally the important role of zinc nutrition in rice. [37]

Sander’s current research focuses on how plant cells respond to changes in their environment [38]  and how they store the nutrients they acquire. In particular, his group work on how transport of chemical elements across cell membranes in plants is integrated with cellular signalling and nutritional status. [21]

Career

Sanders' research career began at the Yale University School of Medicine, first as a postdoctoral research fellow (1978–1979) and then as a postdoctoral research associate (1979–1983).

After a stint as a visiting research fellow in the University of Biological Sciences at the University of Sydney (1983), Sanders moved into the biology department at the University of York in 1983, first as a lecturer (1983–1989), a reader (1989–1992), a professor (1992–2010), also acting as the head of department (2004–2010). [39]

In 2010 Sanders moved to the John Innes Centre, Norwich, as director and group leader, [40] establishing new collaborations with the Chinese Academy of Sciences. [41]

Awards and honours

Sanders was elected a Fellow of the Royal Society in 2001. [42]

Throughout his career Sanders has received a number of additional awards and honours, including:

Related Research Articles

<span class="mw-page-title-main">Vacuole</span> Membrane-bound organelle in cells containing fluid

A vacuole is a membrane-bound organelle which is present in plant and fungal cells and some protist, animal, and bacterial cells. Vacuoles are essentially enclosed compartments which are filled with water containing inorganic and organic molecules including enzymes in solution, though in certain cases they may contain solids which have been engulfed. Vacuoles are formed by the fusion of multiple membrane vesicles and are effectively just larger forms of these. The organelle has no basic shape or size; its structure varies according to the requirements of the cell.

In cellular biology, active transport is the movement of molecules or ions across a cell membrane from a region of lower concentration to a region of higher concentration—against the concentration gradient. Active transport requires cellular energy to achieve this movement. There are two types of active transport: primary active transport that uses adenosine triphosphate (ATP), and secondary active transport that uses an electrochemical gradient. This process is in contrast to passive transport, which allows molecules or ions to move down their concentration gradient, from an area of high concentration to an area of low concentration, without energy.

<span class="mw-page-title-main">Sodium–potassium pump</span> Enzyme found in the membrane of all animal cells

The sodium–potassium pump is an enzyme found in the membrane of all animal cells. It performs several functions in cell physiology.

<span class="mw-page-title-main">Aquaporin</span> Water channel protein in cell membranes

Aquaporins, also called water channels, are channel proteins from a larger family of major intrinsic proteins that form pores in the membrane of biological cells, mainly facilitating transport of water between cells. The cell membranes of a variety of different bacteria, fungi, animal and plant cells contain aquaporins through which water can flow more rapidly into and out of the cell than by diffusing through the phospholipid bilayer. Aquaporins have six membrane-spanning alpha helical domains with both carboxylic and amino terminals on the cytoplasmic side. Two hydrophobic loops contain conserved asparagine–proline–alanine which form a barrel surrounding a central pore-like region that contains additional protein density. Because aquaporins are usually always open and are prevalent in just about every cell type, this leads to a misconception that water readily passes through the cell membrane down its concentration gradient. Water can pass through the cell membrane through simple diffusion because it is a small molecule, and through osmosis, in cases where the concentration of water outside of the cell is greater than that of the inside. However, because water is a polar molecule this process of simple diffusion is relatively slow, and in tissues with high water permeability the majority of water passes through aquaporin.

A membrane transport protein is a membrane protein involved in the movement of ions, small molecules, and macromolecules, such as another protein, across a biological membrane. Transport proteins are integral transmembrane proteins; that is they exist permanently within and span the membrane across which they transport substances. The proteins may assist in the movement of substances by facilitated diffusion, active transport, osmosis, or reverse diffusion. The two main types of proteins involved in such transport are broadly categorized as either channels or carriers. Examples of channel/carrier proteins include the GLUT 1 uniporter, sodium channels, and potassium channels. The solute carriers and atypical SLCs are secondary active or facilitative transporters in humans. Collectively membrane transporters and channels are known as the transportome. Transportomes govern cellular influx and efflux of not only ions and nutrients but drugs as well.

<span class="mw-page-title-main">Antiporter</span> Class of transmembrane transporter protein

An antiporter is an integral membrane protein that uses secondary active transport to move two or more molecules in opposite directions across a phospholipid membrane. It is a type of cotransporter, which means that uses the energetically favorable movement of one molecule down its electrochemical gradient to power the energetically unfavorable movement of another molecule up its electrochemical gradient. This is in contrast to symporters, which are another type of cotransporter that moves two or more ions in the same direction, and primary active transport, which is directly powered by ATP.

<span class="mw-page-title-main">Cotransporter</span> Type of membrane transport proteins

Cotransporters are a subcategory of membrane transport proteins (transporters) that couple the favorable movement of one molecule with its concentration gradient and unfavorable movement of another molecule against its concentration gradient. They enable coupled or cotransport and include antiporters and symporters. In general, cotransporters consist of two out of the three classes of integral membrane proteins known as transporters that move molecules and ions across biomembranes. Uniporters are also transporters but move only one type of molecule down its concentration gradient and are not classified as cotransporters.

<span class="mw-page-title-main">Electrochemical gradient</span> Gradient of electrochemical potential, usually for an ion that can move across a membrane

An electrochemical gradient is a gradient of electrochemical potential, usually for an ion that can move across a membrane. The gradient consists of two parts:

<span class="mw-page-title-main">Guard cell</span> Paired cells that control the stomatal aperture

Guard cells are specialized plant cells in the epidermis of leaves, stems and other organs that are used to control gas exchange. They are produced in pairs with a gap between them that forms a stomatal pore. The stomatal pores are largest when water is freely available and the guard cells become turgid, and closed when water availability is critically low and the guard cells become flaccid. Photosynthesis depends on the diffusion of carbon dioxide (CO2) from the air through the stomata into the mesophyll tissues. Oxygen (O2), produced as a byproduct of photosynthesis, exits the plant via the stomata. When the stomata are open, water is lost by evaporation and must be replaced via the transpiration stream, with water taken up by the roots. Plants must balance the amount of CO2 absorbed from the air with the water loss through the stomatal pores, and this is achieved by both active and passive control of guard cell turgor pressure and stomatal pore size.

The sodium-calcium exchanger (often denoted Na+/Ca2+ exchanger, exchange protein, or NCX) is an antiporter membrane protein that removes calcium from cells. It uses the energy that is stored in the electrochemical gradient of sodium (Na+) by allowing Na+ to flow down its gradient across the plasma membrane in exchange for the countertransport of calcium ions (Ca2+). A single calcium ion is exported for the import of three sodium ions. The exchanger exists in many different cell types and animal species. The NCX is considered one of the most important cellular mechanisms for removing Ca2+.

<span class="mw-page-title-main">Inorganic pyrophosphatase</span> Group of proteins having inorganic pyrophosphatase activity

Inorganic pyrophosphatase is an enzyme that catalyzes the conversion of one ion of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism, calcium absorption and bone formation, and DNA synthesis, as well as other biochemical transformations.

<span class="mw-page-title-main">P-type ATPase</span>

The P-type ATPases, also known as E1-E2 ATPases, are a large group of evolutionarily related ion and lipid pumps that are found in bacteria, archaea, and eukaryotes. P-type ATPases are α-helical bundle primary transporters named based upon their ability to catalyze auto- (or self-) phosphorylation (hence P) of a key conserved aspartate residue within the pump and their energy source, adenosine triphosphate (ATP). In addition, they all appear to interconvert between at least two different conformations, denoted by E1 and E2. P-type ATPases fall under the P-type ATPase (P-ATPase) Superfamily (TC# 3.A.3) which, as of early 2016, includes 20 different protein families.

<span class="mw-page-title-main">ATP6V0C</span> Protein-coding gene in the species Homo sapiens

V-type proton ATPase 16 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0C gene.

<span class="mw-page-title-main">ATP6V1G2</span>

V-type proton ATPase subunit G 2 is an enzyme that in humans is encoded by the ATP6V1G2 gene.

<span class="mw-page-title-main">ATP6V0E1</span> Protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit e 1 is an enzyme that in humans is encoded by the ATP6V0E1 gene.

<span class="mw-page-title-main">Proton ATPase</span> Class of enzymes

In the field of enzymology, a proton ATPase, or H+-ATPase, is an enzyme that catalyzes the following chemical reaction:

The potassium (K+) uptake permease (KUP) family (TC# 2.A.72) is a member of the APC superfamily of secondary carriers. Proteins of the KUP/HAK/KT family include the KUP (TrkD) protein of E. coli and homologues in both Gram-positive and Gram-negative bacteria. High affinity (20 μM) K+ uptake systems (Hak1, TC# 2.A.72.2.1) of the yeast Debaryomyces occidentalis as well as the fungus, Neurospora crassa, and several homologues in plants have been characterized. Arabidopsis thaliana and other plants possess multiple KUP family paralogues. While many plant proteins cluster tightly together, the Hak1 proteins from yeast as well as the two Gram-positive and Gram-negative bacterial proteins are distantly related on the phylogenetic tree for the KUP family. All currently classified members of the KUP family can be found in the Transporter Classification Database.

Members of the H+, Na+-translocating Pyrophosphatase (M+-PPase) Family (TC# 3.A.10) are found in the vacuolar (tonoplast) membranes of higher plants, algae, and protozoa, and in both bacteria and archaea. They are therefore ancient enzymes.

<span class="mw-page-title-main">Roger M. Spanswick</span>

Roger Morgan Spanswick was a Professor of Biological and Environmental Engineering at Cornell University and an important figure in the history of plant membrane biology.

<span class="mw-page-title-main">Philip A. Rea</span> British biochemist, science writer and educator

Philip A. Rea is a British biochemist, science writer and educator, who is currently Professor of Biology and Rebecka and Arie Belldegrun Distinguished Director of the Vagelos Program in Life Sciences & Management at the University of Pennsylvania. His major contributions as a biochemist have been in the areas of membrane transport and xenobiotic detoxification, and as a science writer and educator in understanding the intersection between the life sciences and their implementation. In 2005, he and Mark V. Pauly founded the Roy and Diana Vagelos Program in Life Sciences & Management between the School of Arts and Sciences and Wharton School at the University of Pennsylvania, which he continues to co-direct in his capacity as Belldegrun Distinguished Director. Rea's work on serendipity in science has been featured in The Wall Street Journal. Additionally, he has served as a subject matter expert for 'The Scientist.

References

  1. 1 2 "SANDERS, Prof. Dale". Who's Who 2014, A & C Black, an imprint of Bloomsbury Publishing plc, 2014; online edn, Oxford University Press.(subscription required)
  2. 1 2 "Dale Sanders announced as new director for John Innes Centre". Archived from the original on 31 December 2010.
  3. ↑ Dodd, Antony N.; Kudla, Jörg; Sanders, Dale (2010). "The language of calcium signaling". Annual Review of Plant Biology. 61: 593–620. doi:10.1146/annurev-arplant-070109-104628. ISSN   1545-2123. PMID   20192754.
  4. ↑ Sanders, Dale (1 June 1980). "The mechanism of Cl− transport at the plasma membrane ofChara corallina I. Cotransport with H+". The Journal of Membrane Biology. 53 (2): 129–141. doi:10.1007/BF01870581. ISSN   1432-1424. S2CID   20260325.
  5. ↑ Sanders, D.; Hansen, U. P.; Slayman, C. L. (1 September 1981). "Role of the plasma membrane proton pump in pH regulation in non-animal cells". Proceedings of the National Academy of Sciences. 78 (9): 5903–5907. Bibcode:1981PNAS...78.5903S. doi: 10.1073/pnas.78.9.5903 . ISSN   0027-8424. PMC   348903 . PMID   6458045.
  6. ↑ Sanders, D; Slayman, C L (1 September 1982). "Control of intracellular pH. Predominant role of oxidative metabolism, not proton transport, in the eukaryotic microorganism Neurospora". Journal of General Physiology. 80 (3): 377–402. doi:10.1085/jgp.80.3.377. ISSN   0022-1295. PMC   2228685 . PMID   6292329.
  7. ↑ Ballarin-Denti, A.; den Hollander, J. A.; Sanders, D.; Slayman, C. W.; Slayman, C. L. (21 November 1984). "Kinetics and pH-dependence of glycine-proton symport in Saccharomyces cerevisiae". Biochimica et Biophysica Acta (BBA) - Biomembranes. 778 (1): 1–16. doi:10.1016/0005-2736(84)90442-5. ISSN   0005-2736. PMID   6093875.
  8. ↑ Sanders, Dale (1 February 1986). "Generalized kinetic analysis of ion-driven cotransport systems: II. Random ligand binding as a simple explanation for non-Michaelian kinetics". The Journal of Membrane Biology. 90 (1): 67–87. doi:10.1007/BF01869687. ISSN   1432-1424. PMID   2422385. S2CID   9688689.
  9. ↑ Miller, Anthony J.; Sanders, Dale (March 1987). "Depletion of cytosolic free calcium induced by photosynthesis". Nature. 326 (6111): 397–400. Bibcode:1987Natur.326..397M. doi:10.1038/326397a0. ISSN   1476-4687. S2CID   4366974.
  10. ↑ Rea, Philip A.; Griffith, Christopher J.; Manolson, Morris F.; Sanders, Dale (2 November 1987). "Irreversible inhibition of H+-ATPase of higher plant tonoplast by chaotropic anions: evidence for peripheral location of nucleotide-binding subunits". Biochimica et Biophysica Acta (BBA) - Biomembranes. 904 (1): 1–12. doi:10.1016/0005-2736(87)90080-0. ISSN   0005-2736.
  11. ↑ Davies, Julia M.; Rea, Philip A.; Sanders, Dale (14 January 1991). "Vacuolar proton-pumping pyrophosphatase inBeta vulgaris shows vectorial activation by potassium". FEBS Letters. 278 (1): 66–68. doi: 10.1016/0014-5793(91)80085-H . ISSN   0014-5793. PMID   1847114. S2CID   30539428.
  12. ↑ Davies, J M; Poole, R J; Rea, P A; Sanders, D (15 December 1992). "Potassium transport into plant vacuoles energized directly by a proton-pumping inorganic pyrophosphatase". Proceedings of the National Academy of Sciences of the United States of America. 89 (24): 11701–11705. Bibcode:1992PNAS...8911701D. doi: 10.1073/pnas.89.24.11701 . ISSN   0027-8424. PMC   50624 . PMID   1334545.
  13. ↑ Davies, J. M.; Hunt, I.; Sanders, D. (30 August 1994). "Vacuolar H(+)-pumping ATPase variable transport coupling ratio controlled by pH". Proceedings of the National Academy of Sciences. 91 (18): 8547–8551. Bibcode:1994PNAS...91.8547D. doi: 10.1073/pnas.91.18.8547 . ISSN   0027-8424. PMC   44643 . PMID   8078920.
  14. ↑ Marshall, Jacqueline; Corzo, Alfonso; Leigh, Roger A.; Sanders, Dale (1994). "Membrane potential-dependent calcium transport in right-side-out plasma membrane vesicles from Zea mays L. roots". The Plant Journal. 5 (5): 683–694. doi:10.1111/j.1365-313X.1994.00683.x. ISSN   1365-313X.
  15. ↑ https://academic.oup.com/plcell/article-abstract/5/8/931/5984579.{{cite web}}: Missing or empty |title= (help)
  16. ↑ Allen, G. J.; Sanders, D. (September 1995). "Calcineurin, a Type 2B Protein Phosphatase, Modulates the Ca2+-Permeable Slow Vacuolar Ion Channel of Stomatal Guard Cells". The Plant Cell. 7 (9): 1473–1483. doi:10.1105/tpc.7.9.1473. ISSN   1532-298X. PMC   160973 . PMID   12242407.
  17. ↑ Muir, Shelagh R.; Sanders, Dale (1996). "Pharmacology of Ca2+ release from red beet microsomes suggests the presence of ryanodine receptor homologs in higher plants". FEBS Letters. 395 (1): 39–42. doi:10.1016/0014-5793(96)01000-9. ISSN   1873-3468. PMID   8849685. S2CID   28729727.
  18. ↑ https://academic.oup.com/plphys/article/114/4/1511/6071160?login=true.{{cite web}}: Missing or empty |title= (help)
  19. ↑ Navazio, Lorella; Bewell, Michael A.; Siddiqua, Ashia; Dickinson, George D.; Galione, Antony; Sanders, Dale (18 July 2000). "Calcium release from the endoplasmic reticulum of higher plants elicited by the NADP metabolite nicotinic acid adenine dinucleotide phosphate". Proceedings of the National Academy of Sciences. 97 (15): 8693–8698. Bibcode:2000PNAS...97.8693N. doi: 10.1073/pnas.140217897 . ISSN   0027-8424. PMC   27010 . PMID   10890899.
  20. ↑ Dodd, Antony N.; Gardner, Michael J.; Hotta, Carlos T.; Hubbard, Katharine E.; Dalchau, Neil; Love, John; Assie, Jean-Maurice; Robertson, Fiona C.; Jakobsen, Mia Kyed; Gonçalves, Jorge; Sanders, Dale (14 December 2007). "The Arabidopsis Circadian Clock Incorporates a cADPR-Based Feedback Loop". Science. 318 (5857): 1789–1792. Bibcode:2007Sci...318.1789D. doi: 10.1126/science.1146757 . PMID   18084825. S2CID   41796911.
  21. 1 2 Palmgren, Michael G.; Clemens, Stephan; Williams, Lorraine E.; Krämer, Ute; Borg, Søren; Schjørring, Jan K.; Sanders, Dale (1 September 2008). "Zinc biofortification of cereals: problems and solutions". Trends in Plant Science. 13 (9): 464–473. doi:10.1016/j.tplants.2008.06.005. ISSN   1360-1385. PMID   18701340.
  22. ↑ Allen, G. J.; Sanders, D. (1 May 1994). "Two Voltage-Gated, Calcium Release Channels Coreside in the Vacuolar Membrane of Broad Bean Guard Cells". The Plant Cell: 685–694. doi:10.1105/tpc.6.5.685. ISSN   1040-4651. PMC   160468 . PMID   12244254.
  23. ↑ Fischer, Marc; Schnell, Norbert; Chattaway, Jayne; Davies, Paul; Dixon, Graham; Sanders, Dale (15 December 1997). "The Saccharomyces cerevisiae CCH1 gene is involved in calcium influx and mating". FEBS Letters. 419 (2): 259–262. doi:10.1016/S0014-5793(97)01466-X. ISSN   0014-5793. PMID   9428646. S2CID   12716755.
  24. ↑ Peiter, Edgar; Fischer, Marc; Sidaway, Kate; Roberts, Stephen K.; Sanders, Dale (24 October 2005). "The Saccharomyces cerevisiae Ca2+ channel Cch1pMid1p is essential for tolerance to cold stress and iron toxicity". FEBS Letters. 579 (25): 5697–5703. doi:10.1016/j.febslet.2005.09.058. ISSN   0014-5793. PMID   16223494. S2CID   36582092.
  25. ↑ Maathuis, Frans J. M.; May, Sean T.; Graham, Neil S.; Bowen, Helen C.; Jelitto, Till C.; Trimmer, Paul; Bennett, Malcolm J.; Sanders, Dale; White, Philip J. (1998). "Cell marking in Arabidopsis thaliana and its application to patch–clamp studies". The Plant Journal. 15 (6): 843–851. doi:10.1046/j.1365-313X.1998.00256.x. ISSN   1365-313X. PMID   9807822.
  26. ↑ Sunkar, Ramanjulu; Kaplan, Boaz; Bouché, Nicolas; Arazi, Tzahi; Dolev, Dvora; Talke, Ina N.; Maathuis, Frans J. M.; Sanders, Dale; Bouchez, David; Fromm, Hillel (2000). "Expression of a truncated tobacco NtCBP4 channel in transgenic plants and disruption of the homologous Arabidopsis CNGC1 gene confer Pb2+ tolerance". The Plant Journal. 24 (4): 533–542. doi: 10.1111/j.1365-313X.2000.00901.x . ISSN   1365-313X. PMID   11115134.
  27. ↑ Charpentier, Myriam; Sun, Jongho; Martins, Teresa Vaz; Radhakrishnan, Guru V.; Findlay, Kim; Soumpourou, Eleni; Thouin, Julien; Véry, Anne-Aliénor; Sanders, Dale; Morris, Richard J.; Oldroyd, Giles E. D. (27 May 2016). "Nuclear-localized cyclic nucleotide–gated channels mediate symbiotic calcium oscillations". Science. 352 (6289): 1102–1105. Bibcode:2016Sci...352.1102C. doi:10.1126/science.aae0109. PMID   27230377. S2CID   206646218.
  28. ↑ https://academic.oup.com/plcell/article/11/4/691/6008482?login=true.{{cite web}}: Missing or empty |title= (help)
  29. ↑ https://academic.oup.com/plcell/article/14/suppl_1/S401/6009910?login=true.{{cite web}}: Missing or empty |title= (help)
  30. ↑ Dodd, Antony N.; Kudla, Jörg; Sanders, Dale (2 June 2010). "The Language of Calcium Signaling". Annual Review of Plant Biology. 61 (1): 593–620. doi:10.1146/annurev-arplant-070109-104628. ISSN   1543-5008. PMID   20192754.
  31. ↑ Peiter, Edgar; Maathuis, Frans J. M.; Mills, Lewis N.; Knight, Heather; Pelloux, Jérôme; Hetherington, Alistair M.; Sanders, Dale (March 2005). "The vacuolar Ca2+-activated channel TPC1 regulates germination and stomatal movement". Nature. 434 (7031): 404–408. Bibcode:2005Natur.434..404P. doi:10.1038/nature03381. ISSN   1476-4687. PMID   15772667. S2CID   4418276.
  32. ↑ https://academic.oup.com/plcell/article/29/6/1460/6099382.{{cite journal}}: Cite journal requires |journal= (help); Missing or empty |title= (help)
  33. ↑ Peiter, Edgar; Montanini, Barbara; Gobert, Anthony; Pedas, Pai; Husted, Søren; Maathuis, Frans J. M.; Blaudez, Damien; Chalot, Michel; Sanders, Dale (15 May 2007). "A secretory pathway-localized cation diffusion facilitator confers plant manganese tolerance". Proceedings of the National Academy of Sciences. 104 (20): 8532–8537. Bibcode:2007PNAS..104.8532P. doi: 10.1073/pnas.0609507104 . ISSN   0027-8424. PMC   1895984 . PMID   17494768.
  34. ↑ https://academic.oup.com/plcell/article/15/12/2911/6009975?login=true.{{cite journal}}: Cite journal requires |journal= (help); Missing or empty |title= (help)
  35. ↑ Podar, Dorina; Scherer, Judith; Noordally, Zeenat; Herzyk, Pawel; Nies, Dietrich; Sanders, Dale (1 January 2012). "Metal Selectivity Determinants in a Family of Transition Metal Transporters *". Journal of Biological Chemistry. 287 (5): 3185–3196. doi: 10.1074/jbc.M111.305649 . ISSN   0021-9258. PMC   3270973 . PMID   22139846.
  36. ↑ Menguer, Paloma K.; Vincent, Thomas; Miller, Anthony J.; Brown, James K. M.; Vincze, Eva; Borg, Søren; Holm, Preben Bach; Sanders, Dale; Podar, Dorina (2018). "Improving zinc accumulation in cereal endosperm using HvMTP1, a transition metal transporter". Plant Biotechnology Journal. 16 (1): 63–71. doi:10.1111/pbi.12749. ISSN   1467-7652. PMC   5785336 . PMID   28436146.
  37. ↑ Gao, Shaopei; Xiao, Yunhua; Xu, Fan; Gao, Xiaokai; Cao, Shouyun; Zhang, Fengxia; Wang, Guodong; Sanders, Dale; Chu, Chengcai (2019). "Cytokinin-dependent regulatory module underlies the maintenance of zinc nutrition in rice". New Phytologist. 224 (1): 202–215. doi: 10.1111/nph.15962 . ISSN   1469-8137. PMID   31131881. S2CID   167211152.
  38. ↑ Sanders, Dale (2020). "The salinity challenge". New Phytologist. 225 (3): 1047–1048. doi:10.1111/nph.16357. ISSN   1469-8137. PMC   6973154 . PMID   31894589.
  39. ↑ "Dale Sanders Laboratory". www.york.ac.uk. Retrieved 20 July 2020.
  40. ↑ "Professor Dale Sanders". John Innes Centre. 30 November 2018. Retrieved 20 July 2020.[ permanent dead link ]
  41. ↑ JIC and Chinese Academy of Sciences collaborate on new Centre of Excellence Archived 19 January 2015 at the Wayback Machine
  42. ↑ "Dale Sanders | Royal Society". royalsociety.org. Retrieved 20 July 2020.
  43. ↑ "Dale Sanders receives China International Science and Technology Cooperation Award". John Innes Centre. 11 November 2021. Retrieved 13 December 2021.
  44. ↑ "Prestigious Chinese award for Professor Dale Sanders". John Innes Centre. 18 January 2021. Retrieved 13 December 2021.
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