메뉴 건너뛰기




Volumn 87, Issue 8-9, 2008, Pages 591-599

Protons extruded by NHE1: Digestive or glue?

Author keywords

Adhesion; Integrin; Invasion; Matrix metalloproteinases; Migration; Na+ H+ exchange; NHE1

Indexed keywords

PROTEINASE; PROTON; SODIUM PROTON EXCHANGE PROTEIN 1;

EID: 49049086915     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2008.01.007     Document Type: Short Survey
Times cited : (82)

References (75)
  • 1
    • 0035858878 scopus 로고    scopus 로고
    • Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts
    • Beningo K.A., Dembo M., Kaverina I., Small J.V., and Wang Y.L. Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts. J. Cell Biol. 153 (2001) 881-888
    • (2001) J. Cell Biol. , vol.153 , pp. 881-888
    • Beningo, K.A.1    Dembo, M.2    Kaverina, I.3    Small, J.V.4    Wang, Y.L.5
  • 3
    • 3042692979 scopus 로고    scopus 로고
    • + exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion
    • + exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion. J. Biol. Chem. 279 (2004) 26991-27007
    • (2004) J. Biol. Chem. , vol.279 , pp. 26991-27007
    • Bourguignon, L.Y.1    Singleton, P.A.2    Diedrich, F.3    Stern, R.4    Gilad, E.5
  • 4
    • 0037904987 scopus 로고    scopus 로고
    • The integrin-actin connection, an eternal love affair
    • Brakebusch C., and Fassler R. The integrin-actin connection, an eternal love affair. EMBO J. 22 (2003) 2324-2333
    • (2003) EMBO J. , vol.22 , pp. 2324-2333
    • Brakebusch, C.1    Fassler, R.2
  • 5
    • 3543114271 scopus 로고    scopus 로고
    • Foot and mouth: podosomes, invadopodia and circular dorsal ruffles
    • Buccione R., Orth J.D., and McNiven M.A. Foot and mouth: podosomes, invadopodia and circular dorsal ruffles. Nat. Rev. Mol. Cell Biol. 5 (2004) 647-657
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 647-657
    • Buccione, R.1    Orth, J.D.2    McNiven, M.A.3
  • 8
  • 9
    • 33747508925 scopus 로고    scopus 로고
    • P-selectin mediates adhesion of leukocytes, platelets, and cancer cells in inflammation, thrombosis, and cancer growth and metastasis
    • Chen M., and Geng J.G. P-selectin mediates adhesion of leukocytes, platelets, and cancer cells in inflammation, thrombosis, and cancer growth and metastasis. Arch. Immunol. Ther. Exp. (Warsz.) 54 (2006) 75-84
    • (2006) Arch. Immunol. Ther. Exp. (Warsz.) , vol.54 , pp. 75-84
    • Chen, M.1    Geng, J.G.2
  • 10
    • 0037164808 scopus 로고    scopus 로고
    • Cell migration requires both ion translocation and cytoskeletal anchoring by the Na-H exchanger NHE1
    • Denker S.P., and Barber D.L. Cell migration requires both ion translocation and cytoskeletal anchoring by the Na-H exchanger NHE1. J. Cell Biol. 159 (2002) 1087-1096
    • (2002) J. Cell Biol. , vol.159 , pp. 1087-1096
    • Denker, S.P.1    Barber, D.L.2
  • 11
    • 0036532117 scopus 로고    scopus 로고
    • Ion transport proteins anchor and regulate the cytoskeleton
    • Denker S.P., and Barber D.L. Ion transport proteins anchor and regulate the cytoskeleton. Curr. Opin. Cell Biol. 14 (2002) 214-220
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 214-220
    • Denker, S.P.1    Barber, D.L.2
  • 12
    • 0344309120 scopus 로고    scopus 로고
    • The alpha2beta1 integrin inhibitor rhodocetin binds to the A-domain of the integrin alpha2 subunit proximal to the collagen-binding site
    • Eble J., and Tuckwell D.S. The alpha2beta1 integrin inhibitor rhodocetin binds to the A-domain of the integrin alpha2 subunit proximal to the collagen-binding site. Biochem. J. 376 (2003) 77-85
    • (2003) Biochem. J. , vol.376 , pp. 77-85
    • Eble, J.1    Tuckwell, D.S.2
  • 13
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M., and Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat. Rev. Cancer 2 (2002) 161-174
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 14
    • 0033803416 scopus 로고    scopus 로고
    • pH- and temperature-dependence of functional modulation in metalloproteinases. A. Comparison between neutrophil collagenase and gelatinases A and B
    • Fasciglione G.F., Marini S., D'Alessio S., Politi V., and Coletta M. pH- and temperature-dependence of functional modulation in metalloproteinases. A. Comparison between neutrophil collagenase and gelatinases A and B. Biophys. J. 79 (2000) 2138-2149
    • (2000) Biophys. J. , vol.79 , pp. 2138-2149
    • Fasciglione, G.F.1    Marini, S.2    D'Alessio, S.3    Politi, V.4    Coletta, M.5
  • 16
    • 0033952145 scopus 로고    scopus 로고
    • The biology of cell locomotion within three-dimensional extracellular matrix
    • Friedl P., and Brocker E.B. The biology of cell locomotion within three-dimensional extracellular matrix. Cell. Mol. Life Sci. 57 (2000) 41-64
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 41-64
    • Friedl, P.1    Brocker, E.B.2
  • 17
    • 0038049137 scopus 로고    scopus 로고
    • Tumour-cell invasion and migration: diversity and escape mechanisms
    • Friedl P., and Wolf K. Tumour-cell invasion and migration: diversity and escape mechanisms. Nat. Rev. Cancer 3 (2003) 362-374
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 18
    • 0032400495 scopus 로고    scopus 로고
    • Cell migration strategies in 3-D extracellular matrix: differences in morphology, cell matrix interactions, and integrin function
    • Friedl P., Zanker K.S., and Brocker E.B. Cell migration strategies in 3-D extracellular matrix: differences in morphology, cell matrix interactions, and integrin function. Microsc. Res. Tech. 43 (1998) 369-378
    • (1998) Microsc. Res. Tech. , vol.43 , pp. 369-378
    • Friedl, P.1    Zanker, K.S.2    Brocker, E.B.3
  • 22
    • 0025771650 scopus 로고
    • Are cancer cells acidic?
    • Griffiths J.R. Are cancer cells acidic?. Br. J. Cancer 64 (1991) 425-427
    • (1991) Br. J. Cancer , vol.64 , pp. 425-427
    • Griffiths, J.R.1
  • 24
    • 0029994483 scopus 로고    scopus 로고
    • Tumor oxygenation: a matter of supply and demand
    • Gulledge C.J., and Dewhirst M.W. Tumor oxygenation: a matter of supply and demand. Anticancer Res. 16 (1996) 741-749
    • (1996) Anticancer Res. , vol.16 , pp. 741-749
    • Gulledge, C.J.1    Dewhirst, M.W.2
  • 25
    • 0029974450 scopus 로고    scopus 로고
    • Cellular distribution and regulation of NHE-1 isoform of the NA-H exchanger in the avian osteoclast
    • Gupta A., Edwards J.C., and Hruska K.A. Cellular distribution and regulation of NHE-1 isoform of the NA-H exchanger in the avian osteoclast. Bone 18 (1996) 87-95
    • (1996) Bone , vol.18 , pp. 87-95
    • Gupta, A.1    Edwards, J.C.2    Hruska, K.A.3
  • 26
    • 33845414010 scopus 로고    scopus 로고
    • Cadherins in development: cell adhesion, sorting, and tissue morphogenesis
    • Halbleib J.M., and Nelson W.J. Cadherins in development: cell adhesion, sorting, and tissue morphogenesis. Genes Dev. 20 (2006) 3199-3214
    • (2006) Genes Dev. , vol.20 , pp. 3199-3214
    • Halbleib, J.M.1    Nelson, W.J.2
  • 28
    • 0036554644 scopus 로고    scopus 로고
    • Acid production in glycolysis-impaired tumors provides new insights into tumor metabolism
    • Helmlinger G., Sckell A., Dellian M., Forbes N.S., and Jain R.K. Acid production in glycolysis-impaired tumors provides new insights into tumor metabolism. Clin. Cancer Res. 8 (2002) 1284-1291
    • (2002) Clin. Cancer Res. , vol.8 , pp. 1284-1291
    • Helmlinger, G.1    Sckell, A.2    Dellian, M.3    Forbes, N.S.4    Jain, R.K.5
  • 29
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 110 (2002) 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 30
    • 0035970008 scopus 로고    scopus 로고
    • Integrin-mediated mechanotransduction requires its dynamic interaction with specific extracellular matrix (ECM) ligands
    • Jalali S., del Pozo M.A., Chen K., Miao H., Li Y., Schwartz M.A., Shyy J.Y., and Chien S. Integrin-mediated mechanotransduction requires its dynamic interaction with specific extracellular matrix (ECM) ligands. Proc. Natl. Acad. Sci. USA 98 (2001) 1042-1046
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1042-1046
    • Jalali, S.1    del Pozo, M.A.2    Chen, K.3    Miao, H.4    Li, Y.5    Schwartz, M.A.6    Shyy, J.Y.7    Chien, S.8
  • 31
    • 33644950260 scopus 로고    scopus 로고
    • Podosome and sealing zone: specificity of the osteoclast model
    • Jurdic P., Saltel F., Chabadel A., and Destaing O. Podosome and sealing zone: specificity of the osteoclast model. Eur. J. Cell Biol. 85 (2006) 195-202
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 195-202
    • Jurdic, P.1    Saltel, F.2    Chabadel, A.3    Destaing, O.4
  • 32
    • 20144378365 scopus 로고    scopus 로고
    • Acidic extracellular pH induces matrix metalloproteinase-9 expression in mouse metastatic melanoma cells through the phospholipase D-mitogen-activated protein kinase signaling
    • Kato Y., Lambert C.A., Colige A.C., Mineur P., Noel A., Frankenne F., Foidart J.M., Baba M., Hata R., Miyazaki K., and Tsukuda M. Acidic extracellular pH induces matrix metalloproteinase-9 expression in mouse metastatic melanoma cells through the phospholipase D-mitogen-activated protein kinase signaling. J. Biol. Chem. 280 (2005) 10938-10944
    • (2005) J. Biol. Chem. , vol.280 , pp. 10938-10944
    • Kato, Y.1    Lambert, C.A.2    Colige, A.C.3    Mineur, P.4    Noel, A.5    Frankenne, F.6    Foidart, J.M.7    Baba, M.8    Hata, R.9    Miyazaki, K.10    Tsukuda, M.11
  • 33
    • 34249790593 scopus 로고    scopus 로고
    • Acidic extracellular pH increases calcium influx-triggered phospholipase D activity along with acidic sphingomyelinase activation to induce matrix metalloproteinase-9 expression in mouse metastatic melanoma
    • Kato Y., Ozawa S., Tsukuda M., Kubota E., Miyazaki K., St-Pierre Y., and Hata R.I. Acidic extracellular pH increases calcium influx-triggered phospholipase D activity along with acidic sphingomyelinase activation to induce matrix metalloproteinase-9 expression in mouse metastatic melanoma. FEBS J. 274 (2007) 3171-3183
    • (2007) FEBS J. , vol.274 , pp. 3171-3183
    • Kato, Y.1    Ozawa, S.2    Tsukuda, M.3    Kubota, E.4    Miyazaki, K.5    St-Pierre, Y.6    Hata, R.I.7
  • 35
    • 0034061827 scopus 로고    scopus 로고
    • Polarization of Na(+)/H(+) and Cl(-)/HCO (3)(-) exchangers in migrating renal epithelial cells
    • Klein M., Seeger P., Schuricht B., Alper S.L., and Schwab A. Polarization of Na(+)/H(+) and Cl(-)/HCO (3)(-) exchangers in migrating renal epithelial cells. J. Gen. Physiol. 115 (2000) 599-608
    • (2000) J. Gen. Physiol. , vol.115 , pp. 599-608
    • Klein, M.1    Seeger, P.2    Schuricht, B.3    Alper, S.L.4    Schwab, A.5
  • 36
  • 40
    • 0038433238 scopus 로고    scopus 로고
    • Podosomes: adhesion hot-spots of invasive cells
    • Linder S., and Aepfelbacher M. Podosomes: adhesion hot-spots of invasive cells. Trends Cell Biol. 13 (2003) 376-385
    • (2003) Trends Cell Biol. , vol.13 , pp. 376-385
    • Linder, S.1    Aepfelbacher, M.2
  • 41
    • 0032834211 scopus 로고    scopus 로고
    • Functional hierarchy of simultaneously expressed adhesion receptors: integrin alpha2beta1 but not CD44 mediates MV3 melanoma cell migration and matrix reorganization within three-dimensional hyaluronan-containing collagen matrices
    • Maaser K., Wolf K., Klein C.E., Niggemann B., Zanker K.S., Brocker E.B., and Friedl P. Functional hierarchy of simultaneously expressed adhesion receptors: integrin alpha2beta1 but not CD44 mediates MV3 melanoma cell migration and matrix reorganization within three-dimensional hyaluronan-containing collagen matrices. Mol. Biol. Cell 10 (1999) 3067-3079
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3067-3079
    • Maaser, K.1    Wolf, K.2    Klein, C.E.3    Niggemann, B.4    Zanker, K.S.5    Brocker, E.B.6    Friedl, P.7
  • 42
    • 15144352303 scopus 로고    scopus 로고
    • The effect of two actin depolymerizing factors (ADF/cofilins) on actin filament turnover: pH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin
    • Maciver S.K., Pope B.J., Whytock S., and Weeds A.G. The effect of two actin depolymerizing factors (ADF/cofilins) on actin filament turnover: pH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin. Eur. J. Biochem. 256 (1998) 388-397
    • (1998) Eur. J. Biochem. , vol.256 , pp. 388-397
    • Maciver, S.K.1    Pope, B.J.2    Whytock, S.3    Weeds, A.G.4
  • 43
    • 0037379779 scopus 로고    scopus 로고
    • Clinical, cellular, and molecular aspects of cancer invasion
    • Mareel M., and Leroy A. Clinical, cellular, and molecular aspects of cancer invasion. Physiol. Rev. 83 (2003) 337-376
    • (2003) Physiol. Rev. , vol.83 , pp. 337-376
    • Mareel, M.1    Leroy, A.2
  • 45
    • 2442664415 scopus 로고    scopus 로고
    • The role of dynamin in the assembly and function of podosomes and invadopodia
    • McNiven M.A., Baldassarre M., and Buccione R. The role of dynamin in the assembly and function of podosomes and invadopodia. Front. Biosci. 9 (2004) 1944-1953
    • (2004) Front. Biosci. , vol.9 , pp. 1944-1953
    • McNiven, M.A.1    Baldassarre, M.2    Buccione, R.3
  • 46
    • 34250683573 scopus 로고    scopus 로고
    • Beyond ion translocation: structural functions of the sodium-hydrogen exchanger isoform-1
    • Meima M.E., Mackley J.R., and Barber D.L. Beyond ion translocation: structural functions of the sodium-hydrogen exchanger isoform-1. Curr. Opin. Nephrol. Hypertens. 16 (2007) 365-372
    • (2007) Curr. Opin. Nephrol. Hypertens. , vol.16 , pp. 365-372
    • Meima, M.E.1    Mackley, J.R.2    Barber, D.L.3
  • 47
    • 0030049170 scopus 로고    scopus 로고
    • Actin-based cell motility and cell locomotion
    • Mitchison T.J., and Cramer L.P. Actin-based cell motility and cell locomotion. Cell 84 (1996) 371-379
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 48
    • 33749017931 scopus 로고    scopus 로고
    • Cystine cathepsins: multifunctional enzymes in cancer
    • Mohamed M.M., and Sloane B.F. Cystine cathepsins: multifunctional enzymes in cancer. Nat. Rev. Cancer 6 (2006) 764-775
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 49
    • 1242272754 scopus 로고    scopus 로고
    • Diversity of the mammalian sodium/proton exchanger SLC9 gene family
    • Orlowski J., and Grinstein S. Diversity of the mammalian sodium/proton exchanger SLC9 gene family. Pflugers Arch. Eur. J. Physiol. 447 (2004) 549-565
    • (2004) Pflugers Arch. Eur. J. Physiol. , vol.447 , pp. 549-565
    • Orlowski, J.1    Grinstein, S.2
  • 51
    • 0028817908 scopus 로고
    • Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper G.E., McNamee H.P., Dike L.E., Bojanowski K., and Ingber D.E. Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol. Biol. Cell 6 (1995) 1349-1365
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1349-1365
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 52
    • 9144231428 scopus 로고    scopus 로고
    • Expression profile of genes regulated by activity of the Na-H exchanger NHE1
    • Putney L.K., and Barber D.L. Expression profile of genes regulated by activity of the Na-H exchanger NHE1. BMC Genomics 5 (2004) 46
    • (2004) BMC Genomics , vol.5 , pp. 46
    • Putney, L.K.1    Barber, D.L.2
  • 53
    • 0034058373 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase is involved in the tumor-specific activation of human breast cancer cell Na(+)/H(+) exchange, motility, and invasion induced by serum deprivation
    • Reshkin S.J., Bellizzi A., Albarani V., Guerra L., Tommasino M., Paradiso A., and Casavola V. Phosphoinositide 3-kinase is involved in the tumor-specific activation of human breast cancer cell Na(+)/H(+) exchange, motility, and invasion induced by serum deprivation. J. Biol. Chem. 275 (2000) 5361-5369
    • (2000) J. Biol. Chem. , vol.275 , pp. 5361-5369
    • Reshkin, S.J.1    Bellizzi, A.2    Albarani, V.3    Guerra, L.4    Tommasino, M.5    Paradiso, A.6    Casavola, V.7
  • 55
    • 0028618307 scopus 로고
    • Pericellular pH affects distribution and secretion of cathepsin-B in malignant cells
    • Rozhin J., Sameni M., Ziegler G., and Sloane B.F. Pericellular pH affects distribution and secretion of cathepsin-B in malignant cells. Cancer Res. 54 (1994) 6517-6525
    • (1994) Cancer Res. , vol.54 , pp. 6517-6525
    • Rozhin, J.1    Sameni, M.2    Ziegler, G.3    Sloane, B.F.4
  • 56
    • 17144379334 scopus 로고    scopus 로고
    • Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption
    • Saadoun S., Papadopoulos M.C., Hara-Chikuma M., and Verkman A.S. Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption. Nature 434 (2005) 786-792
    • (2005) Nature , vol.434 , pp. 786-792
    • Saadoun, S.1    Papadopoulos, M.C.2    Hara-Chikuma, M.3    Verkman, A.S.4
  • 58
    • 33644945032 scopus 로고    scopus 로고
    • Podosomes as smart regulators of cellular adhesion
    • Spinardi L., and Marchisio P.C. Podosomes as smart regulators of cellular adhesion. Eur. J. Cell Biol. 85 (2006) 191-194
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 191-194
    • Spinardi, L.1    Marchisio, P.C.2
  • 59
    • 33847240145 scopus 로고    scopus 로고
    • Intracellular pH sensors: design principles and functional significance
    • Srivastava J., Barber D.L., and Jacobson M.P. Intracellular pH sensors: design principles and functional significance. Physiology (Bethesda) 22 (2007) 30-39
    • (2007) Physiology (Bethesda) , vol.22 , pp. 30-39
    • Srivastava, J.1    Barber, D.L.2    Jacobson, M.P.3
  • 60
    • 33744832157 scopus 로고    scopus 로고
    • Role of the Na/H exchanger NHE1 in cell migration
    • Stock C., and Schwab A. Role of the Na/H exchanger NHE1 in cell migration. Acta Physiol. (Oxford) 187 (2006) 149-157
    • (2006) Acta Physiol. (Oxford) , vol.187 , pp. 149-157
    • Stock, C.1    Schwab, A.2
  • 63
    • 36649014657 scopus 로고    scopus 로고
    • pH dependence of melanoma cell migration: protons extruded by NHE1 dominate protons of the bulk solution
    • Stuwe L., Muller M., Fabian A., Waning J., Mally S., Noel J., Schwab A., and Stock C. pH dependence of melanoma cell migration: protons extruded by NHE1 dominate protons of the bulk solution. J. Physiol. 585 (2007) 351-360
    • (2007) J. Physiol. , vol.585 , pp. 351-360
    • Stuwe, L.1    Muller, M.2    Fabian, A.3    Waning, J.4    Mally, S.5    Noel, J.6    Schwab, A.7    Stock, C.8
  • 64
    • 0035870263 scopus 로고    scopus 로고
    • An intracellular form of cathepsin B contributes to invasiveness in cancer
    • Szpaderska A.M., and Frankfater A. An intracellular form of cathepsin B contributes to invasiveness in cancer. Cancer Res. 61 (2001) 3493-3500
    • (2001) Cancer Res. , vol.61 , pp. 3493-3500
    • Szpaderska, A.M.1    Frankfater, A.2
  • 65
    • 0024379967 scopus 로고
    • Acid pH in tumors and its potential for therapeutic exploitation
    • Tannock I.F., and Rotin D. Acid pH in tumors and its potential for therapeutic exploitation. Cancer Res. 49 (1989) 4373-4384
    • (1989) Cancer Res. , vol.49 , pp. 4373-4384
    • Tannock, I.F.1    Rotin, D.2
  • 66
    • 0030872194 scopus 로고    scopus 로고
    • Release of the aspartyl protease cathepsin D is associated with and facilitates human breast cancer cell invasion
    • Tedone T., Correale M., Barbarossa G., Casavola V., Paradiso A., and Reshkin S.J. Release of the aspartyl protease cathepsin D is associated with and facilitates human breast cancer cell invasion. FASEB J. 11 (1997) 785-792
    • (1997) FASEB J. , vol.11 , pp. 785-792
    • Tedone, T.1    Correale, M.2    Barbarossa, G.3    Casavola, V.4    Paradiso, A.5    Reshkin, S.J.6
  • 68
    • 0034053775 scopus 로고    scopus 로고
    • Intracellular pH regulation in a nonmalignant and a derived malignant human breast cell line
    • Wahl M.L., Pooler P.M., Briand P., Leeper D.B., and Owen C.S. Intracellular pH regulation in a nonmalignant and a derived malignant human breast cell line. J. Cell. Physiol. 183 (2000) 373-380
    • (2000) J. Cell. Physiol. , vol.183 , pp. 373-380
    • Wahl, M.L.1    Pooler, P.M.2    Briand, P.3    Leeper, D.B.4    Owen, C.S.5
  • 69
    • 0031439129 scopus 로고    scopus 로고
    • Neural cell adhesion molecules of the immunoglobulin superfamily: role in axon growth and guidance
    • Walsh F.S., and Doherty P. Neural cell adhesion molecules of the immunoglobulin superfamily: role in axon growth and guidance. Annu. Rev. Cell Dev. Biol. 13 (1997) 425-456
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 425-456
    • Walsh, F.S.1    Doherty, P.2
  • 70
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly, disassembly and turnover in migrating cells - over and over and over again
    • Webb D.J., Parsons J.T., and Horwitz A.F. Adhesion assembly, disassembly and turnover in migrating cells - over and over and over again. Nat. Cell Biol. 4 (2002) E97-E100
    • (2002) Nat. Cell Biol. , vol.4
    • Webb, D.J.1    Parsons, J.T.2    Horwitz, A.F.3
  • 72
    • 34547569807 scopus 로고    scopus 로고
    • Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • Wolf K., Wu Y.I., Geiger J., Tam E., Overall C., Stack M.S., and Friedl P. Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat. Cell Biol. 9 (2007) 893-904
    • (2007) Nat. Cell Biol. , vol.9 , pp. 893-904
    • Wolf, K.1    Wu, Y.I.2    Geiger, J.3    Tam, E.4    Overall, C.5    Stack, M.S.6    Friedl, P.7
  • 73
    • 0030013044 scopus 로고    scopus 로고
    • The chronic administration of drugs that inhibit the regulation of intracellular pH: in vitro and anti-tumour effects
    • Yamagata M., and Tannock I.F. The chronic administration of drugs that inhibit the regulation of intracellular pH: in vitro and anti-tumour effects. Br. J. Cancer 73 (1996) 1328-1334
    • (1996) Br. J. Cancer , vol.73 , pp. 1328-1334
    • Yamagata, M.1    Tannock, I.F.2
  • 74
    • 0023707565 scopus 로고
    • The distribution of podosomes in osteoclasts cultured on bone laminae: effect of retinol
    • Zambonin-Zallone A., Teti A., Carano A., and Marchisio P.C. The distribution of podosomes in osteoclasts cultured on bone laminae: effect of retinol. J. Bone Miner. Res. 3 (1988) 517-523
    • (1988) J. Bone Miner. Res. , vol.3 , pp. 517-523
    • Zambonin-Zallone, A.1    Teti, A.2    Carano, A.3    Marchisio, P.C.4
  • 75
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir E., and Geiger B. Molecular complexity and dynamics of cell-matrix adhesions. J. Cell Sci. 114 (2001) 3583-3590
    • (2001) J. Cell Sci. , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.