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Piezo 1 is a [https://en.wikipedia.org/wiki/Mechanosensitive_channels mechanosensitive channel] which means, it can sense external mechanical forces such as fluid flow-induced shear stress,
Piezo 1 is a [https://en.wikipedia.org/wiki/Mechanosensitive_channels mechanosensitive channel] which means, it can sense external mechanical forces such as fluid flow-induced shear stress,
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osmotic stress, and pressure-induced membrane stretch [1]. Moreover, “studies have demonstrated wide expression of the Piezo1 channel that enables many different types of cells to sense a diversity of “outside-in” mechanical forces, including indentation, membrane stretch, shear stress, osmotic stress, ultrasound, and compression”. Since piezo 1 channel could also be activated by traction forces, there are two different mechanisms that have been proposed to explain the mechanical activation of piezo 1 channel. These mechanisms are called “force-from-lipids” and “force-from-filaments”. <ref name= "Adenosine"> DOI 10.3389/fphar.2019.01304</ref>
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osmotic stress, and pressure-induced membrane stretch [1]. Moreover, “studies have demonstrated wide expression of the Piezo1 channel that enables many different types of cells to sense a diversity of “outside-in” mechanical forces, including indentation, membrane stretch, shear stress, osmotic stress, ultrasound, and compression”. Since piezo 1 channel could also be activated by traction forces, there are two different mechanisms that have been proposed to explain the mechanical activation of piezo 1 channel. These mechanisms are called “force-from-lipids” and “force-from-filaments”. <ref name= "Adenosine"> DOI 10.3389/fphar.2019.01304</ref>
For the “force-from-lipids” mechanism, membrane tension is induced by mechanical forces. This membrane tension leads to a reorganization of lipids within and surrounding the channel proteins. This reorganization of lipids results into membrane lipid-channel protein interactions that induce the channel to open. We can note that a recent study (Lin et al., 2019)<ref name= "Lin"> DOI 10.1038/s41586-019-1499-2 </ref> gave support to this mechanism.
For the “force-from-lipids” mechanism, membrane tension is induced by mechanical forces. This membrane tension leads to a reorganization of lipids within and surrounding the channel proteins. This reorganization of lipids results into membrane lipid-channel protein interactions that induce the channel to open. We can note that a recent study (Lin et al., 2019)<ref name= "Lin"> DOI 10.1038/s41586-019-1499-2 </ref> gave support to this mechanism.
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The “force-from-filaments” mechanism proposes that conformational changes occur thanks to intercations between the channel and extracellular matrix or intracellular cytoskeletal proteins resulting in the channel opening<ref name= "Adenosine"> DOI 10.3389/fphar.2019.01304</ref>.
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The “force-from-filaments” mechanism proposes that conformational changes occur thanks to interactions between the channel and extracellular matrix or intracellular cytoskeletal proteins resulting in the channel opening<ref name= "Adenosine"> DOI 10.3389/fphar.2019.01304</ref>.
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The cells are able to perceive the stomach or bladder to fill, blood flowing and lungs inflate.
The cells are able to perceive the stomach or bladder to fill, blood flowing and lungs inflate.
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Piezo1 is a sensor of mechanical forces in [https://en.wikipedia.org/wiki/Endothelium endothelial], urothelial and renal epithelial cells. For instance, Piezo 1 is involved is shear stress sensing
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Piezo1 is a sensor of mechanical forces in [https://en.wikipedia.org/wiki/Endothelium endothelial], urothelial and renal epithelial cells. For instance, Piezo 1 is involved is shear stress sensing in blood vessel endothelial cells and is implicated in the development and physiological functions of the circulatory system, including the proper formation of blood, vessels, regulation of vascular tone and remodelling of small resistance arteries upon [https://en.wikipedia.org/wiki/Hypertension hypertension]. It’s also involved in red blood cell volume homeostasis. <ref name="Cell Press"/>
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in blood vessel endothelial cells and is implicated in the development and physiological functions of the circulatory system, including the proper formation of blood, vessels, regulation of vascular tone and remodelling of small resistance arteries upon [https://en.wikipedia.org/wiki/Hypertension hypertension]. It’s also involved in red blood cell volume homeostasis. <ref name="Cell Press"/>
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Piezo channel mediated cationic [non selective currents]. Indeed, monovalent (Na+, K+) and divalent (Ca2+, Mg2+) can flow through.
Piezo channel mediated cationic [non selective currents]. Indeed, monovalent (Na+, K+) and divalent (Ca2+, Mg2+) can flow through.
However, Piezo 1 is implicated in [excitatory channels] because cation can enter into the cell and lead to membrane [depolarisation] or [calcium dependent signalling pathway] (if Ca2+ enter).
However, Piezo 1 is implicated in [excitatory channels] because cation can enter into the cell and lead to membrane [depolarisation] or [calcium dependent signalling pathway] (if Ca2+ enter).
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When calcium dependent signalling pathway is activated, NO can be released by endothelial cells and lead to vasodilation but also, some channels can also
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When calcium-dependent signalling pathway is activated, NO can be released by endothelial cells and lead to vasodilation but also, some channels can also
be activated in red blood cells.
be activated in red blood cells.
Piezo has a wide variety of functions, but we will focus on the vascularisation.
Piezo has a wide variety of functions, but we will focus on the vascularisation.
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A deficit in Piezo1’s expression can lead to a cobblestone-like appearance of endothelial cells’ organisation, instead of its standard linear appearance.
A deficit in Piezo1’s expression can lead to a cobblestone-like appearance of endothelial cells’ organisation, instead of its standard linear appearance.
The subcellular localisation of piezo1 is also determining. In static conditions, its repartition is even on the membrane, but when a mechanical stimulus arises, piezo1 accumulates at the cell’s apical. This process characterises endothelial cells’ alignment toward frictional force.
The subcellular localisation of piezo1 is also determining. In static conditions, its repartition is even on the membrane, but when a mechanical stimulus arises, piezo1 accumulates at the cell’s apical. This process characterises endothelial cells’ alignment toward frictional force.
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However, piezo1 is also able to drive endothelial cell migration without shear stress, through endothelial nitric oxide synthase, a protein with major roles in vascular biology. <ref name= "vascularisation"> DOI 10.1038/nature13701</ref>
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However, piezo1 is also able to drive endothelial cell migration without shear stress, through endothelial [https://en.wikipedia.org/wiki/Nitric_oxide_synthasenitric oxide synthase], a protein with major roles in vascular biology. <ref name= "vascularisation"> DOI 10.1038/nature13701</ref>
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Piezo 1 has a central domain which is composed of <scene name='86/868186/Cedohihctd/1'>one CTD, one cap (or CED), 3 inner helice (IH) and 3 outer helice (OH).</scene>
Piezo 1 has a central domain which is composed of <scene name='86/868186/Cedohihctd/1'>one CTD, one cap (or CED), 3 inner helice (IH) and 3 outer helice (OH).</scene>
This central domain is surrounded by 3 extended arms called <scene name='86/868186/Blade/1'>blades</scene> extending out from the central pore in a rotatory manner <ref name ="Alexandra"> Zhou, Z. (2019). Structural Analysis of Piezo1 Ion Channel Reveals the Relationship between Amino Acid Sequence Mutations and Human Diseases. 139–155. DOI 10.4236/jbm.2019.712012 </ref>.
This central domain is surrounded by 3 extended arms called <scene name='86/868186/Blade/1'>blades</scene> extending out from the central pore in a rotatory manner <ref name ="Alexandra"> Zhou, Z. (2019). Structural Analysis of Piezo1 Ion Channel Reveals the Relationship between Amino Acid Sequence Mutations and Human Diseases. 139–155. DOI 10.4236/jbm.2019.712012 </ref>.
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Each of these blade, deflecting at an angle of 100° perpendicular to the membrane, contains 6 tandems transmenbranaire helical unites (THUs) constitute
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Each of these blade, deflecting at an angle of 100° perpendicular to the membrane, contains 6 tandems transmembranar helical unites (THUs) constitute
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of 4 transmembrane domains <ref name= "Article six"> DOI 10.1038/nature25743</ref> <ref name="Alexandra"/>. These blades are not planar: instead they lie on a spherically curved surface with the membrane bulging into the cytoplasm <ref name= "Piezo Senses Tension "> DOI 10.1016/j.cub.2018.02.078</ref>
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of 4 transmembrane domains <ref name= "Article six"> DOI 10.1038/nature25743</ref> <ref name="Alexandra"/>. These blades are not planar: instead, they lie on a spherically curved surface with the membrane bulging into the cytoplasm <ref name= "Piezo Senses Tension "> DOI 10.1016/j.cub.2018.02.078</ref>
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These blades flexibles are inside the membrane and force the membrane to curve. That why, they are considered as mechanotransduction modules, force
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These blades flexibles are inside the membrane and force the membrane to curve. That why, they are considered as mechanotransduction modules, force sensors and transducers to gate the central pore. These 3 blades propeller architecture is mechanically interesting because 3 blades are the minimum
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sensors and transducers to gate the central pore. These 3 blades propeller architecture is mechanically interesting because 3 blades are the minimum
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for omnidirectional sensitivity <ref name="Piezo Senses Tension "/> <ref> DOI 10.7554/eLife.33660 </ref>
for omnidirectional sensitivity <ref name="Piezo Senses Tension "/> <ref> DOI 10.7554/eLife.33660 </ref>
==='''[https://en.wikipedia.org/wiki/Gating_(electrophysiology) Gating mechanism]'''===
==='''[https://en.wikipedia.org/wiki/Gating_(electrophysiology) Gating mechanism]'''===
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Piezo 1 possesses delicate force sensing and mechanotransduction mechanisms. Here, we explain how Piezo channels senses and transduces mechanical force
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Piezo 1 possesses delicate force sensing and mechanotransduction mechanisms. Here, we explain how Piezo channels sense and transduce mechanical force
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to gate the central ion conducting pore.
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to gate the central ion-conducting pore.
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Piezo 1 can sense membrane tension through changes in the local curvature of the membrane and channel oppen in response to this change thanks to
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Piezo 1 can sense membrane tension through changes in the local curvature of the membrane and channel open in response to this change thanks to this structure. <ref name ="Piezo Senses Tension"/>
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this structure. <ref name ="Piezo Senses Tension"/>
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Indeed, mPiezo trimer is non-planar conformation inside lipid bilayer, it produces a local dome-shaped deformation of the membrane. In cells, this membrane curvature project towards the cytoplasm and some electrostatics interactions stabilize the trimeric assembly in its curved conformation.
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Indeed, mPiezo trimer is non planar conformation inside lipid bilayer, it produces a local dome shaped deformation of the membrane. In cells, this
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membrane curvature project towards the cytoplasm and some electrostatics interactions stabilize the trimeric assembly in its curved conformation.
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<ref name = "nv article"> DOI 10.7554/eLife.33660</ref>
<ref name = "nv article"> DOI 10.7554/eLife.33660</ref>
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The structure of Piezo1 offers a plausible explanation for the origin of its tension gating. Indeed, if the semi spherical dome becomes flatter
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The structure of Piezo1 offers a plausible explanation for the origin of its tension gating. Indeed, if the semi-spherical dome becomes flatter when Piezo opens, then the channel membrane system will expand thanks to the flexibility of the blades.
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when Piezo open, then the channel membrane system will expand thanks to the flexibility of the blades.
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However, because flattening does not constrain the pore to open wide, expansion and pore diameter are decoupled such that Piezo can exhibit is small conductance and cation selecticity, properties that are essential to its function.<ref name ="Piezo Senses Tension"/> <ref name="Fanny"> DOI 10.1038/s41586-019-1499-2</ref>
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However, because flattening does not constrain the pore to open wide, expension and pore diameter are decoupled such that Piezo can exhibit is
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small conductance and cation selecticity, propreties that are essential to its function.<ref name ="Piezo Senses Tension"/> <ref name="Fanny"> DOI 10.1038/s41586-019-1499-2</ref>
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image gating ?? ou morphing ??
image gating ?? ou morphing ??
==='''Ion conducting pore'''===
==='''Ion conducting pore'''===
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The <scene name='86/868186/Ion_conducting_pore/1'>central pore axis</scene> of piezo1 is lined with the <scene name='86/868186/Ced/1'>extracellular cap domain</scene>, inner helix and cytosolic <scene name='86/868186/Ctd/1'>CTD</scene>. The extracellular cations can approach
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The <scene name='86/868186/Ion_conducting_pore/1'>central pore axis</scene> of piezo1 is lined with the <scene name='86/868186/Ced/1'>extracellular cap domain</scene>, inner helix and cytosolic <scene name='86/868186/Ctd/1'>CTD</scene>. The extracellular cations can approach the pore entry “vertically through the internal cavity along the threefold axis of the cap domain”, they can also approach laterally through spaces (gaps) between the flexible linkers which connect the cap with inner and outer helices.[2] The <scene name='86/868186/Ion_conducting_pore/1'>ion conduction pathway</scene> is situated below the <scene name='86/868186/Ced/1'>cap</scene>, and is
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the pore entry “vertically through the internal cavity along the threefold axis of the cap domain”, they can also approach laterally through spaces (gaps) between the flexible linkers which connect the cap with inner and outer helices.[2] The <scene name='86/868186/Ion_conducting_pore/1'>ion conduction pathway</scene> is situated below the <scene name='86/868186/Ced/1'>cap</scene>, and is
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lined by the three inner transmembrane helices. The possible access for lipids or other hydrophobic molecules through the pore could be “two lateral openings between the inner helices separated by a ‘seal’ formed by K2479 and F2480”. These openings are approximately 11 Å wide and 16 Å tall.
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lined by the three inner transmembrane helices. The possible access for lipids or other hydrophobic molecules through the pore could be “two lateral openings between the inner helices separated by a ‘seal’ formed by K2479 and F2480”. These openings are approximately 11 Å wide and 16 Å tall.
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==='''CTD and Beam'''===
==='''CTD and Beam'''===

Revision as of 22:48, 9 January 2021

Piezo 1

Drag the structure with the mouse to rotate

References

  1. 1.0 1.1 1.2 Zhao Q, Wu K, Geng J, Chi S, Wang Y, Zhi P, Zhang M, Xiao B. Ion Permeation and Mechanotransduction Mechanisms of Mechanosensitive Piezo Channels. Neuron. 2016 Mar 16;89(6):1248-1263. doi: 10.1016/j.neuron.2016.01.046. Epub 2016, Feb 25. PMID:26924440 doi:http://dx.doi.org/10.1016/j.neuron.2016.01.046
  2. 2.0 2.1 Parpaite T, Coste B. Piezo channels. Curr Biol. 2017 Apr 3;27(7):R250-R252. doi: 10.1016/j.cub.2017.01.048. PMID:28376327 doi:http://dx.doi.org/10.1016/j.cub.2017.01.048
  3. 3.0 3.1 Wei L, Mousawi F, Li D, Roger S, Li J, Yang X, Jiang LH. Adenosine Triphosphate Release and P2 Receptor Signaling in Piezo1 Channel-Dependent Mechanoregulation. Front Pharmacol. 2019 Nov 6;10:1304. doi: 10.3389/fphar.2019.01304. eCollection, 2019. PMID:31780935 doi:http://dx.doi.org/10.3389/fphar.2019.01304
  4. Lin YC, Guo YR, Miyagi A, Levring J, MacKinnon R, Scheuring S. Force-induced conformational changes in PIEZO1. Nature. 2019 Sep;573(7773):230-234. doi: 10.1038/s41586-019-1499-2. Epub 2019 Aug, 21. PMID:31435018 doi:http://dx.doi.org/10.1038/s41586-019-1499-2
  5. Li J, Hou B, Tumova S, Muraki K, Bruns A, Ludlow MJ, Sedo A, Hyman AJ, McKeown L, Young RS, Yuldasheva NY, Majeed Y, Wilson LA, Rode B, Bailey MA, Kim HR, Fu Z, Carter DA, Bilton J, Imrie H, Ajuh P, Dear TN, Cubbon RM, Kearney MT, Prasad KR, Evans PC, Ainscough JF, Beech DJ. Piezo1 integration of vascular architecture with physiological force. Nature. 2014 Nov 13;515(7526):279-82. doi: 10.1038/nature13701. Epub 2014 Aug 10. PMID:25119035 doi:http://dx.doi.org/10.1038/nature13701
  6. 6.0 6.1 Zhou, Z. (2019). Structural Analysis of Piezo1 Ion Channel Reveals the Relationship between Amino Acid Sequence Mutations and Human Diseases. 139–155. DOI 10.4236/jbm.2019.712012
  7. Zhao Q, Zhou H, Chi S, Wang Y, Wang J, Geng J, Wu K, Liu W, Zhang T, Dong MQ, Wang J, Li X, Xiao B. Structure and mechanogating mechanism of the Piezo1 channel. Nature. 2018 Feb 22;554(7693):487-492. doi: 10.1038/nature25743. Epub 2018 Jan, 22. PMID:29469092 doi:http://dx.doi.org/10.1038/nature25743
  8. 8.0 8.1 8.2 8.3 Liang X, Howard J. Structural Biology: Piezo Senses Tension through Curvature. Curr Biol. 2018 Apr 23;28(8):R357-R359. doi: 10.1016/j.cub.2018.02.078. PMID:29689211 doi:http://dx.doi.org/10.1016/j.cub.2018.02.078
  9. Guo YR, MacKinnon R. Structure-based membrane dome mechanism for Piezo mechanosensitivity. Elife. 2017 Dec 12;6. pii: 33660. doi: 10.7554/eLife.33660. PMID:29231809 doi:http://dx.doi.org/10.7554/eLife.33660
  10. Guo YR, MacKinnon R. Structure-based membrane dome mechanism for Piezo mechanosensitivity. Elife. 2017 Dec 12;6. pii: 33660. doi: 10.7554/eLife.33660. PMID:29231809 doi:http://dx.doi.org/10.7554/eLife.33660
  11. Lin YC, Guo YR, Miyagi A, Levring J, MacKinnon R, Scheuring S. Force-induced conformational changes in PIEZO1. Nature. 2019 Sep;573(7773):230-234. doi: 10.1038/s41586-019-1499-2. Epub 2019 Aug, 21. PMID:31435018 doi:http://dx.doi.org/10.1038/s41586-019-1499-2
  12. 12.0 12.1 Ge J, Li W, Zhao Q, Li N, Chen M, Zhi P, Li R, Gao N, Xiao B, Yang M. Architecture of the mammalian mechanosensitive Piezo1 channel. Nature. 2015 Nov 5;527(7576):64-9. doi: 10.1038/nature15247. Epub 2015 Sep 21. PMID:26390154 doi:http://dx.doi.org/10.1038/nature15247
  13. 13.0 13.1 13.2 13.3 Zhao Q, Zhou H, Chi S, Wang Y, Wang J, Geng J, Wu K, Liu W, Zhang T, Dong MQ, Wang J, Li X, Xiao B. Structure and mechanogating mechanism of the Piezo1 channel. Nature. 2018 Feb 22;554(7693):487-492. doi: 10.1038/nature25743. Epub 2018 Jan, 22. PMID:29469092 doi:http://dx.doi.org/10.1038/nature25743
  14. doi: https://dx.doi.org/10.4236/jbm.2019.712012
  15. Ge J, Li W, Zhao Q, Li N, Chen M, Zhi P, Li R, Gao N, Xiao B, Yang M. Architecture of the mammalian mechanosensitive Piezo1 channel. Nature. 2015 Nov 5;527(7576):64-9. doi: 10.1038/nature15247. Epub 2015 Sep 21. PMID:26390154 doi:http://dx.doi.org/10.1038/nature15247
  16. 16.0 16.1 Albuisson J, Murthy SE, Bandell M, Coste B, Louis-Dit-Picard H, Mathur J, Feneant-Thibault M, Tertian G, de Jaureguiberry JP, Syfuss PY, Cahalan S, Garcon L, Toutain F, Simon Rohrlich P, Delaunay J, Picard V, Jeunemaitre X, Patapoutian A. Dehydrated hereditary stomatocytosis linked to gain-of-function mutations in mechanically activated PIEZO1 ion channels. Nat Commun. 2013;4:1884. doi: 10.1038/ncomms2899. PMID:23695678 doi:http://dx.doi.org/10.1038/ncomms2899
  17. Andolfo I, Alper SL, De Franceschi L, Auriemma C, Russo R, De Falco L, Vallefuoco F, Esposito MR, Vandorpe DH, Shmukler BE, Narayan R, Montanaro D, D'Armiento M, Vetro A, Limongelli I, Zuffardi O, Glader BE, Schrier SL, Brugnara C, Stewart GW, Delaunay J, Iolascon A. Multiple clinical forms of dehydrated hereditary stomatocytosis arise from mutations in PIEZO1. Blood. 2013 May 9;121(19):3925-35, S1-12. doi: 10.1182/blood-2013-02-482489. Epub, 2013 Mar 11. PMID:23479567 doi:http://dx.doi.org/10.1182/blood-2013-02-482489
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