{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,5]],"date-time":"2026-01-05T22:04:01Z","timestamp":1767650641486,"version":"3.44.0"},"reference-count":112,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,5,1]],"date-time":"2021-05-01T00:00:00Z","timestamp":1619827200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,5,1]],"date-time":"2021-05-01T00:00:00Z","timestamp":1619827200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Microvascular Research"],"published-print":{"date-parts":[[2021,5]]},"DOI":"10.1016\/j.mvr.2020.104124","type":"journal-article","created":{"date-parts":[[2021,1,14]],"date-time":"2021-01-14T20:09:57Z","timestamp":1610654997000},"page":"104124","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"special_numbering":"C","title":["Calcium\/protein kinase C signaling mechanisms in shear-induced mechanical responses of red blood cells"],"prefix":"10.1016","volume":"135","author":[{"given":"Elif","family":"Ugurel","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zeynep Busra","family":"Kisakurek","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yasemin","family":"Aksu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Evrim","family":"Goksel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Neslihan","family":"Cilek","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ozlem","family":"Yalcin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"3","key":"10.1016\/j.mvr.2020.104124_bb0010","doi-asserted-by":"crossref","first-page":"213","DOI":"10.3233\/CH-2010-1433","article-title":"Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia","volume":"50","author":"Almeida","year":"2012","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"10.1016\/j.mvr.2020.104124_bb0015","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1038\/307655a0","article-title":"Glycophorin is linked by band 4.1 to the human erythrocyte membrane skeleton","volume":"307","author":"Anderson","year":"1984","journal-title":"Nature"},{"key":"10.1016\/j.mvr.2020.104124_bb0020","doi-asserted-by":"crossref","first-page":"22360","DOI":"10.1074\/jbc.M513839200","article-title":"Rate of rupture and reattachment of the band 3-ankyrin bridge on the human erythrocyte membrane","volume":"281","author":"Anong","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"9","key":"10.1016\/j.mvr.2020.104124_bb9035","doi-asserted-by":"crossref","first-page":"1904","DOI":"10.1182\/blood-2009-02-203216","article-title":"Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion","volume":"114","author":"Anong","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.mvr.2020.104124_bb0025","doi-asserted-by":"crossref","first-page":"6295","DOI":"10.1021\/bi200770q","article-title":"The mechanosensitive ion channel Piezo1 is inhibited by the peptide GsMTx4","volume":"50","author":"Bae","year":"2011","journal-title":"Biochemistry"},{"issue":"1\u20132","key":"10.1016\/j.mvr.2020.104124_bb0030","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/S0014-5793(99)00822-4","article-title":"Deoxygenation and elevation of intracellular magnesium induce tyrosine phosphorylation of band 3 in human erythrocytes","volume":"455","author":"Barbul","year":"1999","journal-title":"FEBS Lett."},{"issue":"3","key":"10.1016\/j.mvr.2020.104124_bb0035","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.bcmd.2004.01.011","article-title":"Pharmacology of the human red cell voltage-dependent cation channel; part I. Activation by clotrimazole and analogues","volume":"32","author":"Barksmann","year":"2004","journal-title":"Blood Cells Mol. Dis."},{"key":"10.1016\/j.mvr.2020.104124_bb9025","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1055\/s-2003-44551","article-title":"Blood rheology and hemodynamics","volume":"29","author":"Baskurt","year":"2003","journal-title":"Semin. Thromb. Hemost."},{"key":"10.1016\/j.mvr.2020.104124_bb9010","first-page":"23","article-title":"Analyzing shear stress-elongation index curves: comparison of two approaches to simplify data presentation","volume":"31","author":"Baskurt","year":"2004","journal-title":"Clin. Hemorheol. Microcirc."},{"issue":"1","key":"10.1016\/j.mvr.2020.104124_bb0045","doi-asserted-by":"crossref","first-page":"99","DOI":"10.3233\/CH-2012-1616","article-title":"Data reduction methods for ektacytometry in clinical hemorheology","volume":"54","author":"Baskurt","year":"2013","journal-title":"Clin. Hemorheol. Microcirc."},{"issue":"2","key":"10.1016\/j.mvr.2020.104124_bb0050","doi-asserted-by":"crossref","first-page":"75","DOI":"10.3233\/CH-2009-1202","article-title":"New guidelines for hemorheological laboratory techniques","volume":"42","author":"Baskurt","year":"2009","journal-title":"Clinical Hemorheology and Microcirculation, IOS Press."},{"issue":"7","key":"10.1016\/j.mvr.2020.104124_bb0055","doi-asserted-by":"crossref","first-page":"777","DOI":"10.3109\/00365510903266069","article-title":"Parameterization of red blood cell elongation index\u2013shear stress curves obtained by ektacytometry","volume":"69","author":"Baskurt","year":"2009","journal-title":"Scand. J. Clin. Lab. Invest."},{"issue":"2","key":"10.1016\/j.mvr.2020.104124_bb0060","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.bioelechem.2008.04.006","article-title":"Evidence for a random entry of Ca2+ into human red cells","volume":"73","author":"Baunbaek","year":"2008","journal-title":"Bioelectrochem."},{"key":"10.1016\/j.mvr.2020.104124_bb9005","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev.cb.09.110193.000331","article-title":"The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane","volume":"9","author":"Bennett","year":"1993","journal-title":"Annu. Rev. Cell Biol."},{"issue":"21","key":"10.1016\/j.mvr.2020.104124_bb9040","doi-asserted-by":"crossref","first-page":"4516","DOI":"10.1021\/bi1003684","article-title":"Control of erythrocyte membrane-skeletal cohesion by the spectrin-membrane linkage","volume":"49","author":"Blanc","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.mvr.2020.104124_bb0070","doi-asserted-by":"crossref","first-page":"9848","DOI":"10.3390\/ijms14059848","article-title":"Calcium in red blood cells\u2014a perilous balance","volume":"14","author":"Bogdanova","year":"2013","journal-title":"Int. J. Mol. Sci."},{"issue":"3","key":"10.1016\/j.mvr.2020.104124_bb0080","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/0009-8981(86)90013-6","article-title":"Effect of parathyroid hormone and uremia on erythrocyte deformability","volume":"161","author":"Bogin","year":"1986","journal-title":"Clin. Chim. Acta"},{"issue":"5","key":"10.1016\/j.mvr.2020.104124_bb0090","doi-asserted-by":"crossref","first-page":"1602","DOI":"10.1182\/blood.V72.5.1602.1602","article-title":"Calcium transport and ultrastructure of red cells in beta-thalassemia intermedia","volume":"72","author":"Bookchin","year":"1988","journal-title":"Blood, Nov"},{"issue":"3","key":"10.1016\/j.mvr.2020.104124_bb0095","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.ceca.2008.11.001","article-title":"Preserved function of the plasma membrane calcium pump of red blood cells from diabetic subjects with high levels of glycated haemoglobin","volume":"45","author":"Bookchin","year":"2009","journal-title":"Cell Calcium"},{"key":"10.1016\/j.mvr.2020.104124_bb0100","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1182\/blood.V100.1.276","article-title":"Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes","volume":"100","author":"Bordin","year":"2002","journal-title":"Blood"},{"key":"10.1016\/j.mvr.2020.104124_bb9020","first-page":"803","article-title":"Parametrization of the deformation curve as a tool for standardization and interpretation of ektacytometric measurements","volume":"15","author":"Bronkhorst","year":"1995","journal-title":"Clin. Hemorheol."},{"issue":"8","key":"10.1016\/j.mvr.2020.104124_bb0105","doi-asserted-by":"crossref","first-page":"2752","DOI":"10.1021\/acs.jproteome.7b00025","article-title":"Quantitative analysis of human red blood cell proteome","volume":"16","author":"Bryk","year":"2017","journal-title":"J. Proteome Res."},{"issue":"1","key":"10.1016\/j.mvr.2020.104124_bb0115","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1146\/annurev.ph.49.030187.001141","article-title":"Red cell deformability and its relevance to blood flow","volume":"49","author":"Chien","year":"1987","journal-title":"Annu. Rev. Physiol."},{"key":"10.1016\/j.mvr.2020.104124_bb0120","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1172\/JCI110063","article-title":"Separate mechanisms of deformability loss in ATP-depleted and Ca-loaded erythrocytes","volume":"67","author":"Clark","year":"1981","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.mvr.2020.104124_bb0130","first-page":"244","article-title":"Regulation and post-translational modification of erythrocyte membrane and membrane-skeletal proteins","volume":"29","author":"Cohen","year":"1992","journal-title":"Semin. Hematol."},{"key":"10.1016\/j.mvr.2020.104124_bb0135","doi-asserted-by":"crossref","first-page":"979","DOI":"10.3389\/fphys.2017.00979","article-title":"Red blood cell passage of small capillaries is associated with transient Ca2+-mediated adaptations","volume":"8","author":"Danielczok","year":"2017","journal-title":"Front. Physiol."},{"key":"10.1016\/j.mvr.2020.104124_bb0140","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1161\/01.HYP.19.2.167","article-title":"Control of the erythrocyte free Ca2+ concentration in essential hypertension","volume":"19","author":"David-Dufilho","year":"1992","journal-title":"Hypertension"},{"issue":"3","key":"10.1016\/j.mvr.2020.104124_bb0145","first-page":"555","article-title":"Effects of calcium and A23187 on deformability and volume of human red blood cells","volume":"12","author":"Dodson","year":"1987","journal-title":"Blood Cells"},{"key":"10.1016\/j.mvr.2020.104124_bb0150","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0009447","article-title":"Local membrane deformations activate Ca2+-dependent K+ and anionic currents in intact human red blood cells","volume":"5","author":"Dyrda","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.mvr.2020.104124_bb0165","doi-asserted-by":"crossref","first-page":"2489","DOI":"10.1172\/JCI116857","article-title":"Effects of deoxygenation on active and passive Ca2+ transport and on the cytoplasmic Ca2+ levels of sickle cell anemia red cells","volume":"92","author":"Etzion","year":"1993","journal-title":"J. Clin. Invest."},{"issue":"1","key":"10.1016\/j.mvr.2020.104124_bb0170","doi-asserted-by":"crossref","first-page":"1744","DOI":"10.1038\/s41598-017-01591-w","article-title":"\u2018Gardos Channelopathy\u2019: a variant of hereditary Stomatocytosis with complex molecular regulation","volume":"7","author":"Fermo","year":"2017","journal-title":"Sci Rep."},{"issue":"22","key":"10.1016\/j.mvr.2020.104124_bb9030","doi-asserted-by":"crossref","first-page":"5998","DOI":"10.1182\/blood-2010-11-317024","article-title":"Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3","volume":"117","author":"Ferru","year":"2011","journal-title":"Blood"},{"key":"10.1016\/j.mvr.2020.104124_bb0175","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1124\/mol.106.023473","article-title":"State-dependent verapamil block of the cloned human Ca(v)3.1 T-type Ca2+ channel","volume":"70","author":"Freeze","year":"2006","journal-title":"Mol. Pharmacol."},{"issue":"3","key":"10.1016\/j.mvr.2020.104124_bb0185","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/0006-3002(58)90124-0","article-title":"The function of calcium in the potassium permeability of human erythrocytes","volume":"30","author":"Gardos","year":"1958","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.mvr.2020.104124_bb0190","first-page":"139","article-title":"The mechanism of ion transport in human erythrocytes","volume":"1","author":"Gardos","year":"1966","journal-title":"Acta. Biochim. Biophys. Acad. Sci. Hung."},{"key":"10.1016\/j.mvr.2020.104124_bb0195","doi-asserted-by":"crossref","first-page":"4561","DOI":"10.1021\/bi200154g","article-title":"Phosphorylation-dependent perturbations of the 4.1R-associated multiprotein complex of the erythrocyte membrane","volume":"50","author":"Gauthier","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.mvr.2020.104124_bb0200","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.bcmd.2010.02.006","article-title":"Altered phosphorylation of cytoskeleton proteins in sickle red blood cells: the role of protein kinase C, Rac GTPases, and reactive oxygen species","volume":"45","author":"George","year":"2010","journal-title":"Blood Cells Molecules and Diseases"},{"key":"10.1016\/j.mvr.2020.104124_bb0205","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/j.biopha.2018.07.157","article-title":"Chronic hyperglycemia mediated physiological alteration and metabolic distortion leads to organ dysfunction, infection, cancer progression and other pathophysiological consequences: an update on glucose toxicity","volume":"107","author":"Giri","year":"2018","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.mvr.2020.104124_bb0210","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0056759","article-title":"RBC-NOS-dependent S-nitrosylation of cytoskeletal proteins improves RBC deformability","volume":"8","author":"Grau","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.mvr.2020.104124_bb0220","doi-asserted-by":"crossref","unstructured":"Hardeman MR, Goedhart PT, Dobbe JGG, Lettinga KP. (1994). Laser assisted optical rotational cell analyser (L.O.R.C.A); 1. A new instrument for measurement of various structural hemorheological parameters. Clin Hemorheol., 14:605\u2013618.","DOI":"10.3233\/CH-1994-14416"},{"key":"10.1016\/j.mvr.2020.104124_bb0225","doi-asserted-by":"crossref","first-page":"673","DOI":"10.3389\/fphys.2017.00673","article-title":"Is increased intracellular calcium in red blood cells a common component in the molecular mechanism causing anemia?","volume":"8","author":"Hertz","year":"2017","journal-title":"Front. Physiol."},{"key":"10.1016\/j.mvr.2020.104124_bb0230","first-page":"187","article-title":"Erythrocyte spectrin\u2019s chimeric E2\/E3 ubiquitin conjugating\/ligating activity","volume":"51","author":"Hsu","year":"2005","journal-title":"Cell. Mol. Biol."},{"key":"10.1016\/j.mvr.2020.104124_bb0235","doi-asserted-by":"crossref","first-page":"656","DOI":"10.3389\/fphys.2018.00656","article-title":"Squeezing for life - properties of red blood cell deformability","volume":"9","author":"Huisjes","year":"2018","journal-title":"Front. Physiol."},{"key":"10.1016\/j.mvr.2020.104124_bb0240","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1016\/0006-291X(84)91218-X","article-title":"The interaction of calmodulin with human and avian spectrin","volume":"122","author":"Husain","year":"1984","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.mvr.2020.104124_bb0250","doi-asserted-by":"crossref","first-page":"11651","DOI":"10.1073\/pnas.94.21.11651","article-title":"A human intermediate conductance calcium-activated potassium channel","volume":"94","author":"Ishii","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.mvr.2020.104124_bb0260","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1016\/S0026-895X(25)09574-4","article-title":"Distinct effects of mutations in transmembrane segment IVS6 on block of L-type calcium channels by structurally similar phenylalkylamines","volume":"50","author":"Johnson","year":"1996","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.mvr.2020.104124_bb0265","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S0302-4598(00)00110-0","article-title":"The non-selective voltage-activated cation channel in the human red blood cell membrane: reconciliation between two conflicting reports and further characterisation","volume":"52","author":"Kaestner","year":"2000","journal-title":"Bioelectrochemistry"},{"issue":"5","key":"10.1016\/j.mvr.2020.104124_bb0270","first-page":"325","article-title":"Assessment of hemorheological deformability of human red cells exposed totert-butyl hydroperoxide, verapamil and ascorbate by ektacytometer","volume":"28","author":"Kim","year":"2008","journal-title":"The Korean Journal of Laboratory Medicine"},{"key":"10.1016\/j.mvr.2020.104124_bb0275","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1007\/BF01944610","article-title":"A23187 and red cells: changes in deformability, K+, Mg2+, Ca2+ and ATP","volume":"31","author":"Kirkpatrick","year":"1975","journal-title":"Experientia (Basel)"},{"key":"10.1016\/j.mvr.2020.104124_bb0280","doi-asserted-by":"crossref","first-page":"3772","DOI":"10.1021\/bi00467a025","article-title":"Effects of calmodulin on erythrocyte Ca2(+)-ATPase activation and oligomerization","volume":"29","author":"Kosk-Kosicka","year":"1990","journal-title":"Biochemistry"},{"issue":"5\u20136","key":"10.1016\/j.mvr.2020.104124_bb9000","first-page":"141","article-title":"Recovery time course of erythrocyte deformability following exposure to shear is dependent upon conditioning shear stress","volume":"54","author":"Kuck","year":"2018","journal-title":"Biorheology"},{"key":"10.1016\/j.mvr.2020.104124_bb0285","doi-asserted-by":"crossref","first-page":"36","DOI":"10.3389\/fphys.2019.00036","article-title":"Shear stress ameliorates superoxide impairment to erythrocyte deformability with concurrent nitric oxide synthase activation","volume":"10","author":"Kuck","year":"2019","journal-title":"Front. Physiol."},{"issue":"11","key":"10.1016\/j.mvr.2020.104124_bb0290","doi-asserted-by":"crossref","first-page":"118802","DOI":"10.1016\/j.bbamcr.2020.118802","article-title":"Calcium dynamically alters erythrocyte mechanical response to shear","volume":"1867","author":"Kuck","year":"2020","journal-title":"Biochim Biophys Acta Mol Cell Res."},{"key":"10.1016\/j.mvr.2020.104124_bb0295","first-page":"81","article-title":"Influence of the ionophore A23187 on the plastic behavior of normal erythrocytes","volume":"88","author":"Kuettner","year":"1977","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.mvr.2020.104124_bb0300","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0014-5793(81)80481-4","article-title":"Inhibition of calcium-activated potassium conductance of human erythrocytes by calmodulin inhibitory drugs","volume":"133","author":"Lackington","year":"1981","journal-title":"FEBS (Fed. Eur. Biochem. Soc.) Lett."},{"key":"10.1016\/j.mvr.2020.104124_bb0305","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1038\/294667a0","article-title":"Physiological shear stresses enhance the Ca2+ permeability of human erythrocytes","volume":"294","author":"Larsen","year":"1981","journal-title":"Nature (Lond.)"},{"key":"10.1016\/j.mvr.2020.104124_bb0310","series-title":"Membrane Transport in Erythrocytes","first-page":"255","article-title":"Calcium related transient changes in membrane potential of red cells","volume":"vol. 14","author":"Lassen","year":"1980"},{"key":"10.1016\/j.mvr.2020.104124_bb0315","series-title":"Erythrocytes Physiology and Pathophysiology","first-page":"57","article-title":"Properties and membrane transport mechanisms of erythrocytes","author":"Lauf","year":"2012"},{"key":"10.1016\/j.mvr.2020.104124_bb0320","doi-asserted-by":"crossref","first-page":"977","DOI":"10.3389\/fphys.2017.00977","article-title":"On the mechanism of human red blood cell longevity: roles of calcium, the sodium pump, PIEZO1, and Gardos channels","volume":"8","author":"Lew","year":"2017","journal-title":"Front. Physiol."},{"key":"10.1016\/j.mvr.2020.104124_bb0325","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1097\/00004872-199816030-00007","article-title":"Activation by calcium of erythrocyte Na+\/H+ exchange in men","volume":"16","author":"Lijnen","year":"1998","journal-title":"J. Hypertens."},{"issue":"30","key":"10.1016\/j.mvr.2020.104124_bb0330","doi-asserted-by":"crossref","first-page":"13875","DOI":"10.1016\/S0021-9258(18)66951-0","article-title":"Protein kinase C phosphorylates a recently identified membrane skeleton-associated calmodulin-binding protein in human erythrocytes","volume":"261","author":"Ling","year":"1986","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.mvr.2020.104124_bb0335","doi-asserted-by":"crossref","first-page":"2209","DOI":"10.1016\/S0021-9258(18)69192-6","article-title":"Modulation of red cell band 4.1 function by cAMP-dependent kinase and protein kinase C phosphorylation","volume":"263","author":"Ling","year":"1988","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.mvr.2020.104124_bb0340","doi-asserted-by":"crossref","first-page":"C1123","DOI":"10.1152\/ajpcell.00031.2013","article-title":"N-methyl-D-aspartate receptors in human erythroid precursor cells and in circulating red blood cells contribute to the intracellular calcium regulation","volume":"305","author":"Makhro","year":"2013","journal-title":"Am. J. Physiol. Cell. Physiol."},{"key":"10.1016\/j.mvr.2020.104124_bb0345","doi-asserted-by":"crossref","first-page":"288","DOI":"10.3389\/fphys.2016.00288","article-title":"Red cell properties after different modes of blood transportation","volume":"7","author":"Makhro","year":"2016","journal-title":"Front. Physiol."},{"key":"10.1016\/j.mvr.2020.104124_bb0350","doi-asserted-by":"crossref","first-page":"5659","DOI":"10.1074\/jbc.270.10.5659","article-title":"Modulation of erythrocyte membrane mechanical function by b-spectrin phosphorylation and dephosphorylation","volume":"270","author":"Manno","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mvr.2020.104124_bb0355","doi-asserted-by":"crossref","first-page":"7581","DOI":"10.1074\/jbc.M410650200","article-title":"Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation","volume":"280","author":"Manno","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mvr.2020.104124_bb0360","doi-asserted-by":"crossref","first-page":"5282","DOI":"10.1073\/pnas.84.15.5282","article-title":"Protein kinase C activity and hexamethylenebisacetamide-induced erythroleukemia cell differentiation","volume":"84","author":"Melloni","year":"1987","journal-title":"Proc. Nati. Acad. Sci. U.S.A."},{"issue":"3\u20134","key":"10.1016\/j.mvr.2020.104124_bb0365","first-page":"165","article-title":"Shear stress-induced improvement of red blood cell deformability","volume":"50","author":"Meram","year":"2013","journal-title":"Biorheology"},{"key":"10.1016\/j.mvr.2020.104124_bb0370","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1097\/00062752-199704020-00007","article-title":"Erythrocyte signal transduction pathways and their possible functions","volume":"4","author":"Minetti","year":"1997","journal-title":"Curr. Opin. Hematol."},{"key":"10.1016\/j.mvr.2020.104124_bb0375","first-page":"171","article-title":"Red blood cell deformability, membrane material properties and shape: regulation by transmembrane, skeletal and cytosolic proteins and lipids","volume":"30","author":"Mohandas","year":"1993","journal-title":"Semin. Hematol."},{"issue":"10","key":"10.1016\/j.mvr.2020.104124_bb0380","doi-asserted-by":"crossref","first-page":"3939","DOI":"10.1182\/blood-2008-07-161166","article-title":"Red cell membrane: past, present, and future","volume":"112","author":"Mohandas","year":"2008","journal-title":"Blood"},{"key":"10.1016\/j.mvr.2020.104124_bb0385","doi-asserted-by":"crossref","first-page":"45","DOI":"10.3233\/CH-2012-1575","article-title":"Role molecular signaling pathways in changes of red blood cell deformability","volume":"53","author":"Muravyov","year":"2013","journal-title":"Clin. Hemorheol. Microcirc."},{"issue":"1","key":"10.1016\/j.mvr.2020.104124_bb0390","doi-asserted-by":"crossref","first-page":"45","DOI":"10.3233\/JCB-15005","article-title":"Red blood cell microrheological changes and drug transport efficiency","volume":"1","author":"Muravyov","year":"2015","journal-title":"Journal of Cellular Biotechnology"},{"key":"10.1016\/j.mvr.2020.104124_bb0395","doi-asserted-by":"crossref","first-page":"223","DOI":"10.3233\/CH-2009-1212","article-title":"Extra- and intracellular signaling pathways under red blood cell aggregation and deformability changes","volume":"43","author":"Muravyov","year":"2009","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"10.1016\/j.mvr.2020.104124_bb0400","doi-asserted-by":"crossref","first-page":"337","DOI":"10.3233\/CH-2010-1317","article-title":"Crosstalk between adenylyl cyclase signaling pathway and Ca2+ regulatory mechanism under red blood cell microrheological changes","volume":"45","author":"Muravyov","year":"2010","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"10.1016\/j.mvr.2020.104124_bb0405","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1134\/S036211971202017X","article-title":"Role of protein kinases of human red cell membrane in deformability and aggregation changes","volume":"38","author":"Muravyov","year":"2012","journal-title":"Hum. Physiol."},{"key":"10.1016\/j.mvr.2020.104124_bb0410","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1182\/blood.V75.5.1192.1192","article-title":"Synergistic effects of oxidation and deformation on erythrocyte monovalent cation leak","volume":"75","author":"Ney","year":"1990","journal-title":"Blood"},{"issue":"5","key":"10.1016\/j.mvr.2020.104124_bb0425","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1159\/000138177","article-title":"Nitrendipine, nifedipine and verapamil inhibit the in vitro formation of irreversibly sickled cells","volume":"32","author":"Ohnishi","year":"1986","journal-title":"Pharmacology"},{"issue":"1","key":"10.1016\/j.mvr.2020.104124_bb0430","doi-asserted-by":"crossref","first-page":"39","DOI":"10.2170\/jjphysiol.54.39","article-title":"Verapamil prevents impairment in filterability of human erythrocytes exposed to oxidative stress","volume":"54","author":"Okamoto","year":"2004","journal-title":"The Japanese Journal of Physiology"},{"issue":"1\u20134","key":"10.1016\/j.mvr.2020.104124_bb0435","doi-asserted-by":"crossref","first-page":"363","DOI":"10.3233\/CH-2008-1101","article-title":"Modulation of erythrocyte deformability by PKC activity","volume":"39","author":"Oliveira","year":"2008","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"10.1016\/j.mvr.2020.104124_bb0440","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/0005-2736(82)90416-3","article-title":"Reduced erythrocyte deformability associated with calcium accumulation","volume":"691","author":"O\u2019Rear","year":"1982","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.mvr.2020.104124_bb0445","doi-asserted-by":"crossref","first-page":"16021","DOI":"10.1016\/S0021-9258(17)36360-3","article-title":"Protein kinase C in the human erythrocyte","volume":"260","author":"Palfrey","year":"1985","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.mvr.2020.104124_bb0450","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1042\/BJ20081557","article-title":"Oxidized and poorly glycosylated band 3 is selectively phosphorylated by Syk kinase to form large membrane clusters in normal and G6PD-deficient red blood cells","volume":"418","author":"Pantaleo","year":"2009","journal-title":"Biochem. J."},{"key":"10.1016\/j.mvr.2020.104124_bb0460","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1074\/mcp.M700458-MCP200","article-title":"Deep coverage mouse red blood cell proteome. A first comparison with the human red blood cell","volume":"7","author":"Pasini","year":"2008","journal-title":"Molecular & Cellular Proteomics"},{"key":"10.1016\/j.mvr.2020.104124_bb0465","doi-asserted-by":"crossref","first-page":"3676","DOI":"10.1016\/S0021-9258(19)83676-1","article-title":"Interaction between Protein 4.1 and Band 3. An alternative binding site for the element of the membrane skeleton","volume":"260","author":"Pasternack","year":"1985","journal-title":"Biol. Chem."},{"key":"10.1016\/j.mvr.2020.104124_bb0470","doi-asserted-by":"crossref","first-page":"3604","DOI":"10.1073\/pnas.84.11.3604","article-title":"Phosphorylation and proteolytic modification of specific cytoskeletal proteins in human neutrophils stimulated by phorbol 12-myristate 13-acetate Proc","volume":"84","author":"Pontremoli","year":"1987","journal-title":"Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.mvr.2020.104124_bb0475","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1146\/annurev.fluid.37.042604.133933","article-title":"Microcirculation and hemorheology","volume":"37","author":"Popel","year":"2005","journal-title":"Ann. Rev. Fluid Mech."},{"issue":"2\u20133","key":"10.1016\/j.mvr.2020.104124_bb0480","first-page":"159","article-title":"Deformability analysis of sickle blood using ektacytometry","volume":"51","author":"Rabai","year":"2014","journal-title":"Biorheology."},{"key":"10.1016\/j.mvr.2020.104124_bb0485","doi-asserted-by":"crossref","first-page":"6771","DOI":"10.1038\/s41598-019-43200-y","article-title":"Impact of surface-area-to-volume ratio, internal viscosity and membrane viscoelasticity on red blood cell deformability measured in isotonic condition","volume":"9","author":"Renoux","year":"2019","journal-title":"Sci. Rep."},{"issue":"1\u20134","key":"10.1016\/j.mvr.2020.104124_bb0490","doi-asserted-by":"crossref","first-page":"315","DOI":"10.3233\/CH-2011-1482","article-title":"Lipid A decreases human erythrocytes deformability by increasing intracellular Ca2+: effects of verapamil, staurosporine and the rho-kinase inhibitor Y-27632","volume":"49","author":"Ruef","year":"2011","journal-title":"Clin. Hemorheol. Microcirc."},{"issue":"6","key":"10.1016\/j.mvr.2020.104124_bb0495","doi-asserted-by":"crossref","first-page":"411","DOI":"10.3109\/00365519409085463","article-title":"Effect of acute smoking on red blood cell deformability in healthy young and elderly non-smokers, and effect of verapamil on age- and acute smoking-induced change in red blood cell deformability","volume":"54","author":"Salbas","year":"1994","journal-title":"Scand. J. Clin. Lab. Invest."},{"issue":"3","key":"10.1016\/j.mvr.2020.104124_bb0500","first-page":"183","article-title":"Modulation of erythrocyte hemorheological properties by band 3 phosphorylation and dephosphorylation","volume":"36","author":"Saldanha","year":"2007","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"10.1016\/j.mvr.2020.104124_bb0505","doi-asserted-by":"crossref","first-page":"8026","DOI":"10.1073\/pnas.0803225105","article-title":"Protein 4.1R-dependent multiprotein complex: new insights into the structural organization of the red blood cell membrane","volume":"105","author":"Salomao","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"12","key":"10.1016\/j.mvr.2020.104124_bb0510","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0028169","article-title":"Glycosylation of erythrocyte spectrin and its modification in visceral leishmaniasis","volume":"6","author":"Samanta","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.mvr.2020.104124_bb0515","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/0014-5793(80)80024-X","article-title":"Effects of several inhibitors on the K + efflux induced by activation of the Ca2+-dependent channel and by valinomycin in the human red cell","volume":"110","author":"Sanchez","year":"1980","journal-title":"FEBS (Fed. Eur. Biochem. Soc.) Lett."},{"issue":"20","key":"10.1016\/j.mvr.2020.104124_bb0520","doi-asserted-by":"crossref","first-page":"14359","DOI":"10.1074\/jbc.274.20.14359","article-title":"Evidence for a calpeptin-sensitive protein-tyrosine phosphatase upstream of the small GTPase rho","volume":"274","author":"Schoenwaelder","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.mvr.2020.104124_bb0525","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1182\/blood.V64.2.564.564","article-title":"Impaired erythrocyte calcium homeostasis in beta-thalassemia","volume":"64","author":"Shalev","year":"1984","journal-title":"Blood"},{"key":"10.1016\/j.mvr.2020.104124_bb0530","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/0005-2736(85)90447-X","article-title":"Cell age-dependent changes in deformability and calcium accumulation of human erythrocytes","volume":"814","author":"Shiga","year":"1985","journal-title":"Biochim. Biophys. Acta"},{"issue":"5\u20136","key":"10.1016\/j.mvr.2020.104124_bb0535","first-page":"237","article-title":"Prediction of the level and duration of shear stress exposure that induces subhemolytic damage to erythrocytes","volume":"53","author":"Simmonds","year":"2016","journal-title":"Biorheology."},{"issue":"6","key":"10.1016\/j.mvr.2020.104124_bb0540","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1111\/j.1365-2125.1985.tb02707.x","article-title":"Effects of verapamil on calcium-induced rigidity and on filterability of red blood cells from healthy volunteers and patients with progressive systemic sclerosis","volume":"19","author":"Sowemimo-Coker","year":"1985","journal-title":"Br. J. Clin. Pharmacol."},{"key":"10.1016\/j.mvr.2020.104124_bb0545","doi-asserted-by":"crossref","first-page":"1759","DOI":"10.1111\/j.1742-4658.2006.05193.x","article-title":"Binding and activation of nitric oxide synthase isozymes by calmodulin EF hand pairs","volume":"273","author":"Spratt","year":"2006","journal-title":"FEBS J."},{"issue":"13","key":"10.1016\/j.mvr.2020.104124_bb0550","doi-asserted-by":"crossref","first-page":"3400","DOI":"10.1016\/j.jbiomech.2014.07.022","article-title":"Alteration Young\u2019s moduli by protein 4.1 phosphorylation play a potential role in the deformability development of vertebrate erythrocytes","volume":"47","author":"Tang","year":"2014","journal-title":"J. Biomech."},{"issue":"4","key":"10.1016\/j.mvr.2020.104124_bb9045","doi-asserted-by":"crossref","first-page":"155","DOI":"10.3109\/09687689709048178","article-title":"The structure and function of band 3 (AE1): recent developments (review)","volume":"14","author":"Tanner","year":"1997","journal-title":"Mol. Membr. Biol."},{"issue":"6","key":"10.1016\/j.mvr.2020.104124_bb0555","doi-asserted-by":"crossref","first-page":"2563","DOI":"10.1016\/S0021-9258(19)85929-X","article-title":"Purification and characterization of a membrane-bound protein kinase from human erythrocytes","volume":"255","author":"Tao","year":"1980","journal-title":"The Journal of Biological Chemistry, Vol."},{"key":"10.1016\/j.mvr.2020.104124_bb0560","series-title":"Red Cell Membrane Transport in Health and Disease","first-page":"373","article-title":"Calcium homeostasis in normal and abnormal human red cells","author":"Tiffert","year":"2003"},{"issue":"5","key":"10.1016\/j.mvr.2020.104124_bb0565","doi-asserted-by":"crossref","DOI":"10.1063\/1.4895755","article-title":"Biomechanical properties of red blood cells in health and disease towards microfluidics","volume":"8","author":"Tomaiuolo","year":"2014","journal-title":"Biomicrofluidics"},{"key":"10.1016\/j.mvr.2020.104124_bb0575","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.niox.2011.03.003","article-title":"Shear stress activation of nitric oxide synthase and increased nitric oxide levels in human red blood cells","volume":"24","author":"Ulker","year":"2011","journal-title":"Nitric Oxide"},{"key":"10.1016\/j.mvr.2020.104124_bb0580","doi-asserted-by":"crossref","first-page":"45","DOI":"10.3233\/CH-151944","article-title":"Correlation between blood rheological properties and red blood cell indices (MCH, MCV, MCHC) in healthy women","volume":"62","author":"von Tempelhoff","year":"2016","journal-title":"Clin. Hemorheol. Microcirc."},{"issue":"14","key":"10.1016\/j.mvr.2020.104124_bb0585","doi-asserted-by":"crossref","first-page":"9078","DOI":"10.1016\/S0021-9258(18)31554-0","article-title":"Protein kinase C phosphorylates the carboxyl terminus of the plasma membrane Ca(2+)-ATPase from human erythrocytes","volume":"266","author":"Wang","year":"1991","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.mvr.2020.104124_bb0590","first-page":"141","article-title":"Calpain-1 knockout reveals broad effects on erythrocyte deformability and physiology. Biochem. J","volume":"448","author":"Wieschhaus","year":"2012","journal-title":"November 15"},{"key":"10.1016\/j.mvr.2020.104124_bb0595","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/S0014-5793(97)00263-9","article-title":"Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation\/reduction of band 3-associated phosphotyrosine phosphatase","volume":"406","author":"Zipser","year":"1997","journal-title":"FEBS Lett."},{"key":"10.1016\/j.mvr.2020.104124_bb0600","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1042\/bj20020359","article-title":"Ca2+ promotes erythrocyte band 3 tyrosine phosphorylation via dissociation of phosphotyrosine phosphatase from band 3","volume":"368","author":"Zipser","year":"2002","journal-title":"Biochem. J."}],"container-title":["Microvascular Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0026286220301849?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0026286220301849?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,21]],"date-time":"2025-09-21T05:58:20Z","timestamp":1758434300000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0026286220301849"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,5]]},"references-count":112,"alternative-id":["S0026286220301849"],"URL":"https:\/\/doi.org\/10.1016\/j.mvr.2020.104124","relation":{},"ISSN":["0026-2862"],"issn-type":[{"type":"print","value":"0026-2862"}],"subject":[],"published":{"date-parts":[[2021,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Calcium\/protein kinase C signaling mechanisms in shear-induced mechanical responses of red blood cells","name":"articletitle","label":"Article Title"},{"value":"Microvascular Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.mvr.2020.104124","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"104124"}}