메뉴 건너뛰기




Volumn 2014, Issue , 2014, Pages

Congenital defects in neutrophil dynamics

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 3 PHOSPHONOPROPIONIC ACID; LEUKOCYTE ELASTASE; ACTIN;

EID: 84929138345     PISSN: 23148861     EISSN: 23147156     Source Type: Journal    
DOI: 10.1155/2014/303782     Document Type: Review
Times cited : (26)

References (130)
  • 1
    • 77950611467 scopus 로고    scopus 로고
    • The French national registry of primary immunodeficiency diseases
    • CEREDIH: The French PID study group
    • CEREDIH: The French PID study group, "The French national registry of primary immunodeficiency diseases, " Clinical Immunology, vol. 135, no. 2, pp. 264-272, 2010.
    • (2010) Clinical Immunology , vol.135 , Issue.2 , pp. 264-272
  • 3
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • T. D. Pollard and G. G. Borisy, "Cellular motility driven by assembly and disassembly of actin filaments, " Cell, vol. 112, no. 4, pp. 453-465, 2003.
    • (2003) Cell , vol.112 , Issue.4 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 4
    • 0042698618 scopus 로고    scopus 로고
    • Two poles and a compass
    • R. Meili and R. A. Firtel, "Two poles and a compass, " Cell, vol. 114, no. 2, pp. 153-156, 2003.
    • (2003) Cell , vol.114 , Issue.2 , pp. 153-156
    • Meili, R.1    Firtel, R.A.2
  • 5
    • 80655128123 scopus 로고    scopus 로고
    • β-Actin specifically controls cell growth, migration, and the Gactin pool
    • T. M. Bunnell, B. J. Burbach, Y. Shimizu, and J. M. Ervasti, " β-Actin specifically controls cell growth, migration, and the Gactin pool, " Molecular Biology of the Cell, vol. 22, no. 21, pp. 4047-4058, 2011.
    • (2011) Molecular Biology of the Cell , vol.22 , Issue.21 , pp. 4047-4058
    • Bunnell, T.M.1    Burbach, B.J.2    Shimizu, Y.3    Ervasti, J.M.4
  • 6
    • 7144227259 scopus 로고    scopus 로고
    • Restricted β-galactosidase expression of a hygromycin-lacZ gene targeted to the β-actin locus and embryonic lethality of β-actin mutant mice
    • W. Shawlot, J. M. Deng, L. E. Fohn, and R. R. Behringer, "Restricted β-galactosidase expression of a hygromycin-lacZ gene targeted to the β-actin locus and embryonic lethality of β-actin mutant mice, " Transgenic Research, vol. 7, no. 2, pp. 95-103, 1998.
    • (1998) Transgenic Research , vol.7 , Issue.2 , pp. 95-103
    • Shawlot, W.1    Deng, J.M.2    Fohn, L.E.3    Behringer, R.R.4
  • 8
    • 33646873916 scopus 로고    scopus 로고
    • A mutation of β-actin that alters depolymerization dynamics is associated with autosomal dominant developmental malformations, deafness, and dystonia
    • V. Procaccio, G. Salazar, S. Ono, et al., "A mutation of β-actin that alters depolymerization dynamics is associated with autosomal dominant developmental malformations, deafness, and dystonia, "The American Journal ofHuman Genetics, vol. 78, no. 6, pp. 947-960, 2006.
    • (2006) The American Journal of Human Genetics , vol.78 , Issue.6 , pp. 947-960
    • Procaccio, V.1    Salazar, G.2    Ono, S.3
  • 9
    • 84859430859 scopus 로고    scopus 로고
    • De novo mutations in the actin genes ACTB and ACTG1 cause Baraitser-Winter syndrome
    • J. B. Rivière, B. W. van Bon, A. Hoischen, et al., "De novo mutations in the actin genes ACTB and ACTG1 cause Baraitser-Winter syndrome, " Nature Genetics, vol. 44, no. 4, pp. 440-444, 2012.
    • (2012) Nature Genetics , vol.44 , Issue.4 , pp. 440-444
    • Rivière, J.B.1    Van Bon, B.W.2    Hoischen, A.3
  • 10
    • 84892783735 scopus 로고    scopus 로고
    • Severe forms of Baraitser-Winter syndrome are caused by ACTB mutations rather than ACTG1 mutations
    • N. di Donato, A. Rump, R. Koenig, et al., "Severe forms of Baraitser-Winter syndrome are caused by ACTB mutations rather than ACTG1 mutations, " European Journal of Human Genetics, vol. 22, pp. 179-183, 2014.
    • (2014) European Journal of Human Genetics , vol.22 , pp. 179-183
    • Di Donato, N.1    Rump, A.2    Koenig, R.3
  • 11
    • 84881616487 scopus 로고    scopus 로고
    • Functional analysis of a de novo ACTB mutation in a patient with atypical Baraitser-Winter syndrome
    • J. J. Johnston, K. K. Wen, K. Keppler-Noreuil, et al., "Functional analysis of a de novo ACTB mutation in a patient with atypical Baraitser-Winter syndrome, " Human Mutation, vol. 34, no. 9, pp. 1242-1249, 2013.
    • (2013) Human Mutation , vol.34 , Issue.9 , pp. 1242-1249
    • Johnston, J.J.1    Wen, K.K.2    Keppler-Noreuil, K.3
  • 14
    • 33747149898 scopus 로고    scopus 로고
    • Impaired integrindependent function in Wiskott-Aldrich syndrome proteindeficientmurine and human neutrophils
    • H. Zhang, U. Y. Schaff, C. E. Green, et al., "Impaired integrindependent function in Wiskott-Aldrich syndrome proteindeficientmurine and human neutrophils, " Immunity, vol. 25, no. 2, pp. 285-295, 2006.
    • (2006) Immunity , vol.25 , Issue.2 , pp. 285-295
    • Zhang, H.1    Schaff, U.Y.2    Green, C.E.3
  • 15
    • 20044375773 scopus 로고    scopus 로고
    • WASPdeficiency leads to global defects of directed leukocyte migration in vitro and in vivo
    • S. B. Snapper, P. Meelu, D. Nguyenet al., "WASPdeficiency leads to global defects of directed leukocyte migration in vitro and in vivo, " Journal of Leukocyte Biology, vol. 77, no. 6, pp. 993-998, 2005.
    • (2005) Journal of Leukocyte Biology , vol.77 , Issue.6 , pp. 993-998
    • Snapper, S.B.1    Meelu, P.2    Nguyen, D.3
  • 16
    • 84868535997 scopus 로고    scopus 로고
    • Cdc42 regulates neutrophil migration via crosstalk between WASp, CD11b, and microtubules
    • S. Kumar, J. Xu, C. Perkins, et al., "Cdc42 regulates neutrophil migration via crosstalk between WASp, CD11b, and microtubules, " Blood, vol. 120, no. 17, pp. 3563-3574, 2012.
    • (2012) Blood , vol.120 , Issue.17 , pp. 3563-3574
    • Kumar, S.1    Xu, J.2    Perkins, C.3
  • 17
    • 0035093787 scopus 로고    scopus 로고
    • Constitutively activatingmutation in WASP causes X-linked severe congenital neutropenia
    • K. Devriendt, A. S. Kim, G. Mathijs, et al., "Constitutively activatingmutation inWASP causes X-linked severe congenital neutropenia, " Nature Genetics, vol. 27, no. 3, pp. 313-317, 2001.
    • (2001) Nature Genetics , vol.27 , Issue.3 , pp. 313-317
    • Devriendt, K.1    Kim, A.S.2    Mathijs, G.3
  • 18
    • 33749343053 scopus 로고    scopus 로고
    • Two novel activating mutations in the Wiskott-Aldrich syndrome protein result in congenital neutropenia
    • P. J. Ancliff, M. P. Blundell, G. O. Cory, et al., "Two novel activating mutations in the Wiskott-Aldrich syndrome protein result in congenital neutropenia, " Blood, vol. 108, no. 7, pp. 2182-2189, 2006.
    • (2006) Blood , vol.108 , Issue.7 , pp. 2182-2189
    • Ancliff, P.J.1    Blundell, M.P.2    Cory, G.O.3
  • 19
    • 34548447079 scopus 로고    scopus 로고
    • Unregulated actin polymerization by WASp causes defects of mitosis and cytokinesis in X-linked neutropenia
    • D. A. Moulding, M. P. Blundell, D. G. Spiller, et al., "Unregulated actin polymerization by WASp causes defects of mitosis and cytokinesis in X-linked neutropenia, "The Journal of Experimental Medicine, vol. 204, no. 9, pp. 2213-2224, 2007.
    • (2007) The Journal of Experimental Medicine , vol.204 , Issue.9 , pp. 2213-2224
    • Moulding, D.A.1    Blundell, M.P.2    Spiller, D.G.3
  • 20
    • 57449089754 scopus 로고    scopus 로고
    • A large kindred with X-linked neutropenia with an I294T mutation of the Wiskott-Aldrich syndrome gene
    • K. Beel, M. M. Cotter, J. Blatny, et al., "A large kindred with X-linked neutropenia with an I294T mutation of the Wiskott-Aldrich syndrome gene, " British Journal of Haematology, vol. 144, no. 1, pp. 120-126, 2009.
    • (2009) British Journal of Haematology , vol.144 , Issue.1 , pp. 120-126
    • Beel, K.1    Cotter, M.M.2    Blatny, J.3
  • 21
    • 77955855361 scopus 로고    scopus 로고
    • A congenital activating mutant of WASp causes altered plasma membrane topography and adhesion under flow in lymphocytes
    • S. O. Burns, D. J. Killock, D. A. Moulding, et al., "A congenital activating mutant of WASp causes altered plasma membrane topography and adhesion under flow in lymphocytes, " Blood, vol. 115, no. 26, pp. 5355-5365, 2010.
    • (2010) Blood , vol.115 , Issue.26 , pp. 5355-5365
    • Burns, S.O.1    Killock, D.J.2    Moulding, D.A.3
  • 22
    • 77953497134 scopus 로고    scopus 로고
    • Activating WASPmutations associatedwithX-linkedneutropenia result in enhanced actin polymerization, altered cytoskeletal responses, and genomic instability in lymphocytes
    • L. S. Westerberg, P. Meelu, M. Baptista, et al., "Activating WASPmutations associatedwithX-linkedneutropenia result in enhanced actin polymerization, altered cytoskeletal responses, and genomic instability in lymphocytes, " Journal of Experimental Medicine, vol. 207, no. 6, pp. 1145-1152, 2010.
    • (2010) Journal of Experimental Medicine , vol.207 , Issue.6 , pp. 1145-1152
    • Westerberg, L.S.1    Meelu, P.2    Baptista, M.3
  • 23
    • 84868604959 scopus 로고    scopus 로고
    • Excess F-actin mechanically impedes mitosis leading to cytokinesis failure in X-linked neutropenia by exceeding Aurora B kinase error correction capacity
    • D. A. Moulding, E. Moeendarbary, L. Valon, J. Record, G. T. Charras, and A. J. Thrasher, "Excess F-actin mechanically impedes mitosis leading to cytokinesis failure in X-linked neutropenia by exceeding Aurora B kinase error correction capacity, " Blood, vol. 120, no. 18, pp. 3803-3811, 2012.
    • (2012) Blood , vol.120 , Issue.18 , pp. 3803-3811
    • Moulding, D.A.1    Moeendarbary, E.2    Valon, L.3    Record, J.4    Charras, G.T.5    Thrasher, A.J.6
  • 24
    • 84856116174 scopus 로고    scopus 로고
    • Membrane tension maintains cell polarity by confining signals to the leading edge during neutrophilmigration
    • A. R. Houk, A. Jilkine, C. O. Mejean, et al., "Membrane tension maintains cell polarity by confining signals to the leading edge during neutrophilmigration, " Cell, vol. 148, no. 1-2, pp. 175-188, 2012.
    • (2012) Cell , vol.148 , Issue.1-2 , pp. 175-188
    • Houk, A.R.1    Jilkine, A.2    Mejean, C.O.3
  • 25
    • 0033082165 scopus 로고    scopus 로고
    • Deficiency of the hematopoietic cell-specific Rho family GTPase Rac2 is characterized by abnormalities in neutrophil function and host defense
    • A. W. Roberts, C. Kim, L. Zhen, et al., "Deficiency of the hematopoietic cell-specific Rho family GTPase Rac2 is characterized by abnormalities in neutrophil function and host defense, " Immunity, vol. 10, no. 2, pp. 183-196, 1999.
    • (1999) Immunity , vol.10 , Issue.2 , pp. 183-196
    • Roberts, A.W.1    Kim, C.2    Zhen, L.3
  • 26
    • 84918832559 scopus 로고    scopus 로고
    • BAR domain proteins regulate Rho GTPase signaling
    • Article IDe28580
    • P. Aspenstrom, "BAR domain proteins regulate Rho GTPase signaling, " Small GTPases, vol. 5, Article IDe28580, 2014.
    • (2014) Small GTPases , vol.5
    • Aspenstrom, P.1
  • 27
    • 0037215397 scopus 로고    scopus 로고
    • Regulation of neutrophil function by Rac GTPases
    • M. C. Dinauer, "Regulation of neutrophil function by Rac GTPases, " Current Opinion in Hematology, vol. 10, no. 1, pp. 8-15, 2003.
    • (2003) Current Opinion in Hematology , vol.10 , Issue.1 , pp. 8-15
    • Dinauer, M.C.1
  • 29
    • 0034283717 scopus 로고    scopus 로고
    • Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency
    • D. A. Williams, W. Tao, F. Yang, et al., "Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency, " Blood, vol. 96, no. 5, pp. 1646-1654, 2000.
    • (2000) Blood , vol.96 , Issue.5 , pp. 1646-1654
    • Williams, D.A.1    Tao, W.2    Yang, F.3
  • 30
    • 79551486262 scopus 로고    scopus 로고
    • Human phagocyte defect caused by a Rac2mutation detected bymeans of neonatal screening for T-cell lymphopenia
    • D. Accetta, G. Syverson, B. Bonacci, et al., "Human phagocyte defect caused by a Rac2mutation detected bymeans of neonatal screening for T-cell lymphopenia, " The Journal of Allergy and Clinical Immunology, vol. 127, no. 2, pp. 535. e2-538. e2, 2011.
    • (2011) The Journal of Allergy and Clinical Immunology , vol.127 , Issue.2 , pp. 535e2-538e2
    • Accetta, D.1    Syverson, G.2    Bonacci, B.3
  • 32
    • 66349108700 scopus 로고    scopus 로고
    • Reactive oxygen species regulate a slingshot-cofilin activation pathway
    • J. S. Kim, T. Y. Huang, and G. M. Bokoch, "Reactive oxygen species regulate a slingshot-cofilin activation pathway, " Molecular Biology of the Cell, vol. 20, no. 11, pp. 2650-2660, 2009.
    • (2009) Molecular Biology of the Cell , vol.20 , Issue.11 , pp. 2650-2660
    • Kim, J.S.1    Huang, T.Y.2    Bokoch, G.M.3
  • 33
    • 65249141705 scopus 로고    scopus 로고
    • A common cofilin activity cycle in invasive tumor cells and inflammatory cells
    • J. van Rheenen, J. Condeelis, and M. Glogauer, "A common cofilin activity cycle in invasive tumor cells and inflammatory cells, " Journal of Cell Science, vol. 122, no. 3, pp. 305-311, 2009.
    • (2009) Journal of Cell Science , vol.122 , Issue.3 , pp. 305-311
    • Van Rheenen, J.1    Condeelis, J.2    Glogauer, M.3
  • 34
    • 0037341905 scopus 로고    scopus 로고
    • Redox-dependent downregulation of Rho by Rac
    • A. S. Nimnual, L. J. Taylor, and D. Bar-Sagi, "Redox-dependent downregulation of Rho by Rac, " Nature Cell Biology, vol. 5, no. 3, pp. 236-241, 2003.
    • (2003) Nature Cell Biology , vol.5 , Issue.3 , pp. 236-241
    • Nimnual, A.S.1    Taylor, L.J.2    Bar-Sagi, D.3
  • 35
    • 0037149510 scopus 로고    scopus 로고
    • Killing activity of neutrophils is mediated through activation of proteases by K+ flux
    • E. P. Reeves, H. Lu, H. L. Jacobs, et al., "Killing activity of neutrophils is mediated through activation of proteases by K+ flux, " Nature, vol. 416, no. 6878, pp. 291-297, 2002.
    • (2002) Nature , vol.416 , Issue.6878 , pp. 291-297
    • Reeves, E.P.1    Lu, H.2    Jacobs, H.L.3
  • 36
  • 37
    • 0024232831 scopus 로고
    • Neutrophil actin dysfunction is a genetic disorder associated with partial impairment of neutrophil actin assembly in three family members
    • F. S. Southwick, G. A. Dabiri, and T. P. Stossel, "Neutrophil actin dysfunction is a genetic disorder associated with partial impairment of neutrophil actin assembly in three family members, " The Journal of Clinical Investigation, vol. 82, no. 5, pp. 1525-1531, 1988.
    • (1988) The Journal of Clinical Investigation , vol.82 , Issue.5 , pp. 1525-1531
    • Southwick, F.S.1    Dabiri, G.A.2    Stossel, T.P.3
  • 38
    • 0024381133 scopus 로고
    • The relationship between CR3 deficiency and neutrophil actin assembly
    • F. S. Southwick, T. H. Howard, T. Holbrook, D. C. Anderson, T. P. Stossel, and M. A. Arnaout, "The relationship between CR3 deficiency and neutrophil actin assembly, " Blood, vol. 73, no. 7, pp. 1973-1979, 1989.
    • (1989) Blood , vol.73 , Issue.7 , pp. 1973-1979
    • Southwick, F.S.1    Howard, T.H.2    Holbrook, T.3    Anderson, D.C.4    Stossel, T.P.5    Arnaout, M.A.6
  • 39
    • 0025992199 scopus 로고
    • An inherited defect of neutrophil motility and microfilamentous cytoskeleton associated with abnormalities in 47-Kd and 89-Kd proteins
    • T. D. Coates, J. C. Torkildson, M. Torres, J. A. Church, and T. H. Howard, "An inherited defect of neutrophil motility and microfilamentous cytoskeleton associated with abnormalities in 47-Kd and 89-Kd proteins, " Blood, vol. 78, no. 5, pp. 1338-1346, 1991.
    • (1991) Blood , vol.78 , Issue.5 , pp. 1338-1346
    • Coates, T.D.1    Torkildson, J.C.2    Torres, M.3    Church, J.A.4    Howard, T.H.5
  • 40
    • 0028125674 scopus 로고
    • The 47-kD protein increased in neutrophil actin dysfunction with 47-and 89-kD protein abnormalities is lymphocyte-specific protein
    • T. Howard, Y. Li, M. Torres, A. Guerrero, and T. Coates, "The 47-kD protein increased in neutrophil actin dysfunction with 47-and 89-kD protein abnormalities is lymphocyte-specific protein, " Blood, vol. 83, no. 1, pp. 231-241, 1994.
    • (1994) Blood , vol.83 , Issue.1 , pp. 231-241
    • Howard, T.1    Li, Y.2    Torres, M.3    Guerrero, A.4    Coates, T.5
  • 41
    • 0029084606 scopus 로고
    • The actin-binding protein, lymphocyte-specific protein 1, is expressed in human leukocytes and humanmyeloid and lymphoid cell lines
    • Y. Li, A. Guerrero, and T. H. Howard, "The actin-binding protein, lymphocyte-specific protein 1, is expressed in human leukocytes and humanmyeloid and lymphoid cell lines, " Journal of Immunology, vol. 155, no. 7, pp. 3563-3569, 1995.
    • (1995) Journal of Immunology , vol.155 , Issue.7 , pp. 3563-3569
    • Li, Y.1    Guerrero, A.2    Howard, T.H.3
  • 42
    • 0031864869 scopus 로고    scopus 로고
    • Lymphocytespecific protein 1 expression in eukaryotic cells reproduces the morphologic and motile abnormality of NAD 47/89 neutrophils
    • T. H. Howard, J. Hartwig, and C. Cunningham, "Lymphocytespecific protein 1 expression in eukaryotic cells reproduces the morphologic and motile abnormality of NAD 47/89 neutrophils, " Blood, vol. 91, no. 12, pp. 4786-4795, 1998.
    • (1998) Blood , vol.91 , Issue.12 , pp. 4786-4795
    • Howard, T.H.1    Hartwig, J.2    Cunningham, C.3
  • 43
    • 0034284331 scopus 로고    scopus 로고
    • LSP1modulates leukocyte populations in resting and inflamed peritoneum
    • J. Jongstra-Bilen, V. L. Misener, C. Wang, et al., "LSP1modulates leukocyte populations in resting and inflamed peritoneum, " Blood, vol. 96, no. 5, pp. 1827-1835, 2000.
    • (2000) Blood , vol.96 , Issue.5 , pp. 1827-1835
    • Jongstra-Bilen, J.1    Misener, V.L.2    Wang, C.3
  • 45
    • 33846309701 scopus 로고    scopus 로고
    • Integrins and the actin cytoskeleton
    • I. Delon and N. H. Brown, "Integrins and the actin cytoskeleton, " Current Opinion in Cell Biology, vol. 19, no. 1, pp. 43-50, 2007.
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.1 , pp. 43-50
    • Delon, I.1    Brown, N.H.2
  • 47
    • 21844450244 scopus 로고    scopus 로고
    • Intracellular signalling controlling integrin activation in lymphocytes
    • T. Kinashi, "Intracellular signalling controlling integrin activation in lymphocytes, " Nature Reviews Immunology, vol. 5, no. 7, pp. 546-559, 2005.
    • (2005) Nature Reviews Immunology , vol.5 , Issue.7 , pp. 546-559
    • Kinashi, T.1
  • 48
    • 84889889065 scopus 로고    scopus 로고
    • Pathogenic mechanisms and clinical implications of congenital neutropenia syndromes
    • F. Hauck and C. Klein, "Pathogenic mechanisms and clinical implications of congenital neutropenia syndromes, " Current Opinion in Allergy and Clinical Immunology, vol. 13, pp. 596-606, 2013.
    • (2013) Current Opinion in Allergy and Clinical Immunology , vol.13 , pp. 596-606
    • Hauck, F.1    Klein, C.2
  • 49
    • 33845904894 scopus 로고    scopus 로고
    • HAX1 deficiency causes autosomal recessive severe congenital neutropenia (Kostmann disease)
    • C. Klein, M. Grudzien, G. Appaswamy, et al., "HAX1 deficiency causes autosomal recessive severe congenital neutropenia (Kostmann disease), " Nature Genetics, vol. 39, no. 1, pp. 86-92, 2007.
    • (2007) Nature Genetics , vol.39 , Issue.1 , pp. 86-92
    • Klein, C.1    Grudzien, M.2    Appaswamy, G.3
  • 50
    • 0031569110 scopus 로고    scopus 로고
    • HAX-1, a novel intracellular protein, localized on Mitochondria, directly associates with HS1, a substrate of Src family Tyrosine kinases
    • Y. Suzuki, C. Demoliere, D. Kitamura, H. Takeshita, U. Deuschle, and T. Watanabe, "HAX-1, a novel intracellular protein, localized on Mitochondria, directly associates with HS1, a substrate of Src family Tyrosine kinases, " Journal of Immunology, vol. 158, no. 6, pp. 2736-2744, 1997.
    • (1997) Journal of Immunology , vol.158 , Issue.6 , pp. 2736-2744
    • Suzuki, Y.1    Demoliere, C.2    Kitamura, D.3    Takeshita, H.4    Deuschle, U.5    Watanabe, T.6
  • 51
    • 9644259048 scopus 로고    scopus 로고
    • Regulation of HAX-1 anti-apoptotic protein by Omi/HtrA2 protease during cell death
    • L. Cilenti, M. M. Soundarapandian, G. A. Kyriazis, et al., "Regulation of HAX-1 anti-apoptotic protein by Omi/HtrA2 protease during cell death, "The Journal of Biological Chemistry, vol. 279, no. 48, pp. 50295-50301, 2004.
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.48 , pp. 50295-50301
    • Cilenti, L.1    Soundarapandian, M.M.2    Kyriazis, G.A.3
  • 52
    • 0036140439 scopus 로고    scopus 로고
    • K15 protein of Kaposi's sarcoma-associated herpesvirus is latently expressed and binds to HAX-1, a protein with antiapoptotic function
    • T. V. Sharp, H. W. Wang, A. Koumi, et al., "K15 protein of Kaposi's sarcoma-associated herpesvirus is latently expressed and binds to HAX-1, a protein with antiapoptotic function, " Journal of Virology, vol. 76, no. 2, pp. 802-816, 2002.
    • (2002) Journal of Virology , vol.76 , Issue.2 , pp. 802-816
    • Sharp, T.V.1    Wang, H.W.2    Koumi, A.3
  • 54
    • 34347230941 scopus 로고    scopus 로고
    • HS1-associated protein X-1 regulates carcinoma cell migration and invasion via clathrin-mediated endocytosis of integrin αvβ6
    • A. G. Ramsay, M. D. Keppler, M. Jazayeri, et al., "HS1-associated protein X-1 regulates carcinoma cell migration and invasion via clathrin-mediated endocytosis of integrin αvβ6, " Cancer Research, vol. 67, no. 11, pp. 5275-5284, 2007.
    • (2007) Cancer Research , vol.67 , Issue.11 , pp. 5275-5284
    • Ramsay, A.G.1    Keppler, M.D.2    Jazayeri, M.3
  • 55
    • 10344234244 scopus 로고    scopus 로고
    • G13 stimulates cell migration through cortactin-interacting protein Hax-1
    • V. Radhika, D. Onesime, J. H. Ha, and N. Dhanasekaran, "G13 stimulates cell migration through cortactin-interacting protein Hax-1, "The Journal of Biological Chemistry, vol. 279, no. 47, pp. 49406-49413, 2004.
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 49406-49413
    • Radhika, V.1    Onesime, D.2    Ha, J.H.3    Dhanasekaran, N.4
  • 56
    • 79956197089 scopus 로고    scopus 로고
    • Hax1 regulates neutrophil adhesion and motility through RhoA
    • P. J. Cavnar, E. Berthier, D. J. Beebe, and A. Huttenlocher, "Hax1 regulates neutrophil adhesion and motility through RhoA, " Journal of Cell Biology, vol. 193, no. 3, pp. 465-473, 2011.
    • (2011) Journal of Cell Biology , vol.193 , Issue.3 , pp. 465-473
    • Cavnar, P.J.1    Berthier, E.2    Beebe, D.J.3    Huttenlocher, A.4
  • 57
    • 0037656291 scopus 로고    scopus 로고
    • Mutations in the chemokine receptor gene CXCR4 are associated with WHIM syndrome, a combined immunodeficiency disease
    • P. A. Hernandez, R. J. Gorlin, J. N. Lukens, et al., "Mutations in the chemokine receptor gene CXCR4 are associated with WHIM syndrome, a combined immunodeficiency disease, " Nature Genetics, vol. 34, no. 1, pp. 70-74, 2003.
    • (2003) Nature Genetics , vol.34 , Issue.1 , pp. 70-74
    • Hernandez, P.A.1    Gorlin, R.J.2    Lukens, J.N.3
  • 58
    • 0142188265 scopus 로고    scopus 로고
    • Chemokines acting via CXCR2 and CXCR4 control the release of neutrophils from the bone marrow and their return following senescence
    • C. Martin, P. C. E. Burdon, G. Bridger, J. Gutierrez-Ramos, T. J. Williams, and S. M. Rankin, "Chemokines acting via CXCR2 and CXCR4 control the release of neutrophils from the bone marrow and their return following senescence, " Immunity, vol. 19, no. 4, pp. 583-593, 2003.
    • (2003) Immunity , vol.19 , Issue.4 , pp. 583-593
    • Martin, C.1    Burdon, P.C.E.2    Bridger, G.3    Gutierrez-Ramos, J.4    Williams, T.J.5    Rankin, S.M.6
  • 59
    • 3142593911 scopus 로고    scopus 로고
    • Role of the CXCR4/SDF-1 chemokine axis in circulating neutrophil homeostasis
    • B. T. Suratt, J. M. Petty, S. K. Young, et al., "Role of the CXCR4/SDF-1 chemokine axis in circulating neutrophil homeostasis, " Blood, vol. 104, no. 2, pp. 565-571, 2004.
    • (2004) Blood , vol.104 , Issue.2 , pp. 565-571
    • Suratt, B.T.1    Petty, J.M.2    Young, S.K.3
  • 60
    • 58149112207 scopus 로고    scopus 로고
    • WHIM syndrome: Congenital immune deficiency disease
    • T. Kawai and H. L. Malech, "WHIM syndrome: congenital immune deficiency disease, " Current Opinion in Hematology, vol. 16, no. 1, pp. 20-26, 2009.
    • (2009) Current Opinion in Hematology , vol.16 , Issue.1 , pp. 20-26
    • Kawai, T.1    Malech, H.L.2
  • 61
    • 20144372356 scopus 로고    scopus 로고
    • WHIM syndromes with different genetic anomalies are accounted for by impaired CXCR4 desensitization to CXCL12
    • K. Balabanian, B. Lagane, J. L. Pablos, et al., "WHIM syndromes with different genetic anomalies are accounted for by impaired CXCR4 desensitization to CXCL12, " Blood, vol. 105, no. 6, pp. 2449-2457, 2005.
    • (2005) Blood , vol.105 , Issue.6 , pp. 2449-2457
    • Balabanian, K.1    Lagane, B.2    Pablos, J.L.3
  • 62
    • 33846106798 scopus 로고    scopus 로고
    • WHIM syndrome myelokathexis reproduced in the NOD/SCID mouse xenotransplant model engrafted with healthy human stem cells transduced with C-terminus-truncatedCXCR4
    • T. Kawai, U. Choi, L. Cardwell, et al., "WHIM syndrome myelokathexis reproduced in the NOD/SCID mouse xenotransplant model engrafted with healthy human stem cells transduced with C-terminus-truncatedCXCR4, " Blood, vol. 109, no. 1, pp. 78-84, 2007.
    • (2007) Blood , vol.109 , Issue.1 , pp. 78-84
    • Kawai, T.1    Choi, U.2    Cardwell, L.3
  • 63
    • 77957933530 scopus 로고    scopus 로고
    • Live imaging of neutrophil motility in a zebrafish model ofWHIM syndrome
    • K. B. Walters, J. M. Green, J. C. Surfus, S. K. Yoo, and A. Huttenlocher, "Live imaging of neutrophil motility in a zebrafish model ofWHIM syndrome, " Blood, vol. 116, no. 15, pp. 2803-2811, 2010.
    • (2010) Blood , vol.116 , Issue.15 , pp. 2803-2811
    • Walters, K.B.1    Green, J.M.2    Surfus, J.C.3    Yoo, S.K.4    Huttenlocher, A.5
  • 64
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic polymorphonuclear leukocyte
    • N. Borregaard and J. B. Cowland, "Granules of the human neutrophilic polymorphonuclear leukocyte, " Blood, vol. 89, no. 10, pp. 3503-3521, 1997.
    • (1997) Blood , vol.89 , Issue.10 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 65
    • 58049135823 scopus 로고    scopus 로고
    • Roles of F-BAR/PCH proteins in the regulation of membrane dynamics and actin reorganization
    • P. Aspenstrom, "Roles of F-BAR/PCH proteins in the regulation of membrane dynamics and actin reorganization, " International Review of Cell and Molecular Biology, vol. 272, pp. 1-31, 2008.
    • (2008) International Review of Cell and Molecular Biology , vol.272 , pp. 1-31
    • Aspenstrom, P.1
  • 66
    • 0029680639 scopus 로고    scopus 로고
    • TwoGTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorderWiskott-Aldrich syndrome
    • P. Aspenstrom, U. Lindberg, and A. Hall, "TwoGTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorderWiskott-Aldrich syndrome, " Current Biology, vol. 6, no. 1, pp. 70-75, 1996.
    • (1996) Current Biology , vol.6 , Issue.1 , pp. 70-75
    • Aspenstrom, P.1    Lindberg, U.2    Hall, A.3
  • 67
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between NWASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • R. Rohatgi, L. Ma, H. Miki, et al., "The interaction between NWASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly, " Cell, vol. 97, no. 2, pp. 221-231, 1999.
    • (1999) Cell , vol.97 , Issue.2 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3
  • 68
    • 3042793578 scopus 로고    scopus 로고
    • Linking albinism and immunity: The secrets of secretory lysosomes
    • J. Stinchcombe, G. Bossi, and G. M. Giffiths, "Linking albinism and immunity: the secrets of secretory lysosomes, " Science, vol. 305, no. 5680, pp. 55-59, 2004.
    • (2004) Science , vol.305 , Issue.5680 , pp. 55-59
    • Stinchcombe, J.1    Bossi, G.2    Giffiths, G.M.3
  • 71
    • 0015184560 scopus 로고
    • Defective granulocyte chemotaxis in the Chediak-Higashi syndrome
    • R. A. Clark and H. R. Kimball, "Defective granulocyte chemotaxis in the Chediak-Higashi syndrome, " Journal of Clinical Investigation, vol. 50, no. 12, pp. 2645-2652, 1971.
    • (1971) Journal of Clinical Investigation , vol.50 , Issue.12 , pp. 2645-2652
    • Clark, R.A.1    Kimball, H.R.2
  • 72
    • 0015310380 scopus 로고
    • Abnormal bactericidal, metabolic, and lysosomal functions of Chediak-Higashi Syndrome leukocytes
    • R. K. Root, A. S. Rosenthal, and D. J. Balestra, "Abnormal bactericidal, metabolic, and lysosomal functions of Chediak-Higashi Syndrome leukocytes, "The Journal of Clinical Investigation, vol. 51, no. 3, pp. 649-665, 1972.
    • (1972) The Journal of Clinical Investigation , vol.51 , Issue.3 , pp. 649-665
    • Root, R.K.1    Rosenthal, A.S.2    Balestra, D.J.3
  • 73
    • 0023812897 scopus 로고
    • Microbicidal/cytotoxic proteins of neutrophils are deficient in two disorders: Chediak-Higashi syndrome and "specific" granule deficiency
    • T. Ganz, J. A. Metcalf, J. I. Gallin, L. A. Boxer, and R. I. Lehrer, "Microbicidal/cytotoxic proteins of neutrophils are deficient in two disorders: Chediak-Higashi syndrome and "specific" granule deficiency, " Journal of Clinical Investigation, vol. 82, no. 2, pp. 552-556, 1988.
    • (1988) Journal of Clinical Investigation , vol.82 , Issue.2 , pp. 552-556
    • Ganz, T.1    Metcalf, J.A.2    Gallin, J.I.3    Boxer, L.A.4    Lehrer, R.I.5
  • 74
    • 0031745886 scopus 로고    scopus 로고
    • Giant granules of neutrophils in Chediak-Higashi syndrome are derived from azurophil granules but not from specific and gelatinase granules
    • L. Kjeldsen, J. Calafat, and N. Borregaard, "Giant granules of neutrophils in Chediak-Higashi syndrome are derived from azurophil granules but not from specific and gelatinase granules, " Journal of Leukocyte Biology, vol. 64, no. 1, pp. 72-77, 1998.
    • (1998) Journal of Leukocyte Biology , vol.64 , Issue.1 , pp. 72-77
    • Kjeldsen, L.1    Calafat, J.2    Borregaard, N.3
  • 75
    • 15844397403 scopus 로고    scopus 로고
    • Identification of the homologous beige and Chediak-Higashi syndrome genes
    • M. D. F. S. Barbosa, Q. A. Nguyen, V. T. Tchernev, et al., "Identification of the homologous beige and Chediak-Higashi syndrome genes, " Nature, vol. 382, no. 6588, pp. 262-265, 1996.
    • (1996) Nature , vol.382 , Issue.6588 , pp. 262-265
    • Barbosa, M.D.F.S.1    Nguyen, Q.A.2    Tchernev, V.T.3
  • 77
    • 0344002689 scopus 로고    scopus 로고
    • Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome
    • G. Menasche, E. Pastural, J. Feldmann, et al., "Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome, " Nature Genetics, vol. 25, no. 2, pp. 173-176, 2000.
    • (2000) Nature Genetics , vol.25 , Issue.2 , pp. 173-176
    • Menasche, G.1    Pastural, E.2    Feldmann, J.3
  • 78
    • 77951709524 scopus 로고    scopus 로고
    • Rab27a and Rab27b regulate neutrophil azurophilic granule exocytosis and NADPH oxidase activity by independent mechanisms
    • J. L. Johnson, A. A. Brzezinska, T. Tolmachova, et al., "Rab27a and Rab27b regulate neutrophil azurophilic granule exocytosis and NADPH oxidase activity by independent mechanisms, " Traffic, vol. 11, no. 4, pp. 533-547, 2010.
    • (2010) Traffic , vol.11 , Issue.4 , pp. 533-547
    • Johnson, J.L.1    Brzezinska, A.A.2    Tolmachova, T.3
  • 79
    • 84863083748 scopus 로고    scopus 로고
    • Rab27a-mediated protease release regulates neutrophil recruitment by allowing uropod detachment
    • R. K. Singh, W. Liao, D. Tracey-White, et al., "Rab27a-mediated protease release regulates neutrophil recruitment by allowing uropod detachment, " Journal of Cell Science, vol. 125, no. 7, pp. 1652-1656, 2012.
    • (2012) Journal of Cell Science , vol.125 , Issue.7 , pp. 1652-1656
    • Singh, R.K.1    Liao, W.2    Tracey-White, D.3
  • 80
    • 33847754590 scopus 로고    scopus 로고
    • Rab27a is a key component of the secretory machinery of azurophilic granules in granulocytes
    • D. B. Munafo, J. L. Johnson, B. A. Ellis, S. Rutschmann, B. Beutler, and S. D. Catz, "Rab27a is a key component of the secretory machinery of azurophilic granules in granulocytes, " The Biochemical Journal, vol. 402, no. 2, pp. 229-239, 2007.
    • (2007) The Biochemical Journal , vol.402 , Issue.2 , pp. 229-239
    • Munafo, D.B.1    Johnson, J.L.2    Ellis, B.A.3    Rutschmann, S.4    Beutler, B.5    Catz, S.D.6
  • 81
    • 33846109356 scopus 로고    scopus 로고
    • A novel human primary immunodeficiency syndrome caused by deficiency of the endosomal adaptor protein p14
    • G. Bohn, A. Allroth, G. Brandes, et al., "A novel human primary immunodeficiency syndrome caused by deficiency of the endosomal adaptor protein p14, " Nature Medicine, vol. 13, no. 1, pp. 38-45, 2007.
    • (2007) Nature Medicine , vol.13 , Issue.1 , pp. 38-45
    • Bohn, G.1    Allroth, A.2    Brandes, G.3
  • 82
    • 0032757863 scopus 로고    scopus 로고
    • Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis
    • M. Horwitz, K. F. Benson, R. E. Person, A. G. Aprikyan, and D. C. Dale, "Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis, " Nature Genetics, vol. 23, no. 4, pp. 433-436, 1999.
    • (1999) Nature Genetics , vol.23 , Issue.4 , pp. 433-436
    • Horwitz, M.1    Benson, K.F.2    Person, R.E.3    Aprikyan, A.G.4    Dale, D.C.5
  • 83
    • 33847395071 scopus 로고    scopus 로고
    • Neutrophil elastase in cyclic and severe congenital neutropenia
    • M. S. Horwitz, Z. Duan, B. Korkmaz, H. Lee, M. E. Mealiffe, and S. J. Salipante, "Neutrophil elastase in cyclic and severe congenital neutropenia, " Blood, vol. 109, no. 5, pp. 1817-1824, 2007.
    • (2007) Blood , vol.109 , Issue.5 , pp. 1817-1824
    • Horwitz, M.S.1    Duan, Z.2    Korkmaz, B.3    Lee, H.4    Mealiffe, M.E.5    Salipante, S.J.6
  • 84
    • 0034307655 scopus 로고    scopus 로고
    • Mutations in the gene encoding neutrophil elastase in congenital and cyclic neutropenia
    • D. C. Dale, R. E. Person, A. A. Bolyard, et al., "Mutations in the gene encoding neutrophil elastase in congenital and cyclic neutropenia, " Blood, vol. 96, no. 7, pp. 2317-2322, 2000.
    • (2000) Blood , vol.96 , Issue.7 , pp. 2317-2322
    • Dale, D.C.1    Person, R.E.2    Bolyard, A.A.3
  • 85
    • 84893061901 scopus 로고    scopus 로고
    • Neutropeniaassociated ELANE mutations disrupting translation initiation produce novel neutrophil elastase isoforms
    • T. Tidwell, J. Wechsler, R. C. Nayak, et al., "Neutropeniaassociated ELANE mutations disrupting translation initiation produce novel neutrophil elastase isoforms, " Blood, vol. 123, pp. 562-569, 2014.
    • (2014) Blood , vol.123 , pp. 562-569
    • Tidwell, T.1    Wechsler, J.2    Nayak, R.C.3
  • 86
    • 36549023532 scopus 로고    scopus 로고
    • Severe congenital neutropenia and the unfolded protein response
    • J. Xia and D. C. Link, "Severe congenital neutropenia and the unfolded protein response, " Current Opinion in Hematology, vol. 15, no. 1, pp. 1-7, 2008.
    • (2008) Current Opinion in Hematology , vol.15 , Issue.1 , pp. 1-7
    • Xia, J.1    Link, D.C.2
  • 87
    • 0034177476 scopus 로고    scopus 로고
    • A new variant of Hermansky-Pudlak syndrome due to mutations in a gene responsible for vesicle formation
    • V. Shotelersuk, E. C. DellAngelica, L. Hartnell, J. S. Bonifacino, and W. A. Gahl, "A new variant of Hermansky-Pudlak syndrome due to mutations in a gene responsible for vesicle formation, " The American Journal of Medicine, vol. 108, no. 5, pp. 423-427, 2000.
    • (2000) The American Journal of Medicine , vol.108 , Issue.5 , pp. 423-427
    • Shotelersuk, V.1    DellAngelica, E.C.2    Hartnell, L.3    Bonifacino, J.S.4    Gahl, W.A.5
  • 88
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor
    • E. C. DellAngelica, V. Shotelersuk, R. C. Aguilar, W. A. Gahl, and J. S. Bonifacino, "Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor, " Molecular Cell, vol. 3, no. 1, pp. 11-21, 1999.
    • (1999) Molecular Cell , vol.3 , Issue.1 , pp. 11-21
    • DellAngelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 89
    • 0041353534 scopus 로고    scopus 로고
    • Mutations associatedwith neutropenia in dogs and humans disrupt intracellular transport of neutrophil elastase
    • K. F. Benson, F. Li, R. E. Personet al., "Mutations associatedwith neutropenia in dogs and humans disrupt intracellular transport of neutrophil elastase, " Nature Genetics, vol. 35, no. 1, pp. 90-96, 2003.
    • (2003) Nature Genetics , vol.35 , Issue.1 , pp. 90-96
    • Benson, K.F.1    Li, F.2    Person, R.E.3
  • 90
    • 33745490496 scopus 로고    scopus 로고
    • Mutations in neutrophil elastase causing congenital neutropenia lead to cytoplasmic protein accumulation and induction of the unfolded protein response
    • I. Kollner, B. Sodeik, S. Schreek, et al., "Mutations in neutrophil elastase causing congenital neutropenia lead to cytoplasmic protein accumulation and induction of the unfolded protein response, " Blood, vol. 108, no. 2, pp. 493-500, 2006.
    • (2006) Blood , vol.108 , Issue.2 , pp. 493-500
    • Kollner, I.1    Sodeik, B.2    Schreek, S.3
  • 91
    • 39649098272 scopus 로고    scopus 로고
    • Mutations of the ELA2 gene found in patientswith severe congenital neutropenia induce the unfolded protein response and cellular apoptosis
    • D. S. Grenda, M. Murakami, J. Ghatak, et al., "Mutations of the ELA2 gene found in patientswith severe congenital neutropenia induce the unfolded protein response and cellular apoptosis, " Blood, vol. 110, no. 13, pp. 4179-4187, 2007.
    • (2007) Blood , vol.110 , Issue.13 , pp. 4179-4187
    • Grenda, D.S.1    Murakami, M.2    Ghatak, J.3
  • 92
    • 0038757823 scopus 로고    scopus 로고
    • Mutations in protooncogene GFI1 cause human neutropenia and target ELA2
    • R. E. Person, F. Li, Z. Duan, et al., "Mutations in protooncogene GFI1 cause human neutropenia and target ELA2, " Nature Genetics, vol. 34, no. 3, pp. 308-312, 2003.
    • (2003) Nature Genetics , vol.34 , Issue.3 , pp. 308-312
    • Person, R.E.1    Li, F.2    Duan, Z.3
  • 93
    • 20144366550 scopus 로고    scopus 로고
    • Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease
    • S. Zuchner, M. Noureddine, M. Kennerson, et al., "Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease, " Nature Genetics, vol. 37, no. 3, pp. 289-294, 2005.
    • (2005) Nature Genetics , vol.37 , Issue.3 , pp. 289-294
    • Zuchner, S.1    Noureddine, M.2    Kennerson, M.3
  • 94
    • 0015831045 scopus 로고
    • A new syndrome with hypotonia, obesity, mental deficiency, and facial, oral, ocular, and limb anomalies
    • M. M. Cohen, B. D. Hall, D. W. Smith, C. B. Graham, and K. J. Lampert, "A new syndrome with hypotonia, obesity, mental deficiency, and facial, oral, ocular, and limb anomalies, " The Journal of Pediatrics, vol. 83, pp. 280-284, 1973.
    • (1973) The Journal of Pediatrics , vol.83 , pp. 280-284
    • Cohen, M.M.1    Hall, B.D.2    Smith, D.W.3    Graham, C.B.4    Lampert, K.J.5
  • 96
    • 0031732790 scopus 로고    scopus 로고
    • Increased neutrophil adhesive capability in Cohen syndrome, an autosomal recessive disorder associated with granulocytopenia
    • O. Olivieri, S. Lombardi, C. Russo, and R. Corrocher, "Increased neutrophil adhesive capability in Cohen syndrome, an autosomal recessive disorder associated with granulocytopenia, " Haematologica, vol. 83, no. 9, pp. 778-782, 1998.
    • (1998) Haematologica , vol.83 , Issue.9 , pp. 778-782
    • Olivieri, O.1    Lombardi, S.2    Russo, C.3    Corrocher, R.4
  • 97
    • 0038353767 scopus 로고    scopus 로고
    • Cohen syndrome is caused by mutations in a novel gene, COH1, encoding a transmembrane protein with a presumed role in vesicle-mediated sorting and intracellular protein transport
    • J. Kolehmainen, G. C. M. Black, A. Saarinen, et al., "Cohen syndrome is caused by mutations in a novel gene, COH1, encoding a transmembrane protein with a presumed role in vesicle-mediated sorting and intracellular protein transport, " The American Journal of Human Genetics, vol. 72, no. 6, pp. 1359-1369, 2003.
    • (2003) The American Journal of Human Genetics , vol.72 , Issue.6 , pp. 1359-1369
    • Kolehmainen, J.1    Black, G.C.M.2    Saarinen, A.3
  • 98
    • 84879753994 scopus 로고    scopus 로고
    • A congenital neutrophil defect syndrome associated with mutations in VPS45
    • T. Vilboux, A. Lev, M. C. V. Malicdan, et al., "A congenital neutrophil defect syndrome associated with mutations in VPS45, " The New England Journal of Medicine, vol. 369, no. 1, pp. 54-65, 2013.
    • (2013) The New England Journal of Medicine , vol.369 , Issue.1 , pp. 54-65
    • Vilboux, T.1    Lev, A.2    Malicdan, M.C.V.3
  • 99
    • 84882432632 scopus 로고    scopus 로고
    • The Thr224Asn mutation in the VPS45 gene is associated with the congenital neutropenia and primary myelofibrosis of infancy
    • P. Stepensky, A. Saada, M. Cowan, et al., "The Thr224Asn mutation in the VPS45 gene is associated with the congenital neutropenia and primary myelofibrosis of infancy., " Blood, vol. 121, no. 25, pp. 5078-5087, 2013.
    • (2013) Blood , vol.121 , Issue.25 , pp. 5078-5087
    • Stepensky, P.1    Saada, A.2    Cowan, M.3
  • 100
    • 58249089770 scopus 로고    scopus 로고
    • A syndrome with congenital neutropenia and mutations in G6PC3
    • K. Boztug, G. Appaswamy, A. Ashikov, et al., "A syndrome with congenital neutropenia and mutations in G6PC3, " The New England Journal of Medicine, vol. 360, no. 1, pp. 32-43, 2009.
    • (2009) The New England Journal of Medicine , vol.360 , Issue.1 , pp. 32-43
    • Boztug, K.1    Appaswamy, G.2    Ashikov, A.3
  • 101
    • 0031448837 scopus 로고    scopus 로고
    • Sequence of a putative glucose 6-phosphate translocase, mutated in glycogen storage disease type Ib
    • I. Gerin, M. Veiga-da-Cunha, Y. Achouri, J. F. Collet, and E. van Schaftingen, "Sequence of a putative glucose 6-phosphate translocase, mutated in glycogen storage disease type Ib, " The FEBS Letters, vol. 419, no. 2-3, pp. 235-238, 1997.
    • (1997) The FEBS Letters , vol.419 , Issue.2-3 , pp. 235-238
    • Gerin, I.1    Veiga-Da-Cunha, M.2    Achouri, Y.3    Collet, J.F.4    Van Schaftingen, E.5
  • 102
    • 0018198963 scopus 로고
    • Anewvarient of glycogen storage disease Type i probably due to a defect in the glucose-6-phosphate transport system
    • K. Narisawa, Y. Igarashi, H. Otomo, and K. Tada, "Anewvarient of glycogen storage disease Type I probably due to a defect in the glucose-6-phosphate transport system, " Biochemical and Biophysical Research Communications, vol. 83, no. 4, pp. 1360-1364, 1978.
    • (1978) Biochemical and Biophysical Research Communications , vol.83 , Issue.4 , pp. 1360-1364
    • Narisawa, K.1    Igarashi, Y.2    Otomo, H.3    Tada, K.4
  • 103
    • 33847420515 scopus 로고    scopus 로고
    • Impaired neutrophil activity and increased susceptibility to bacterial infection in mice lacking glucose-6-phosphatase-β
    • Y. Y. Cheung, S. Y. Kim, W. H. Yiu, et al., "Impaired neutrophil activity and increased susceptibility to bacterial infection in mice lacking glucose-6-phosphatase-β, " The Journal of Clinical Investigation, vol. 117, no. 3, pp. 784-793, 2007.
    • (2007) The Journal of Clinical Investigation , vol.117 , Issue.3 , pp. 784-793
    • Cheung, Y.Y.1    Kim, S.Y.2    Yiu, W.H.3
  • 104
    • 84900400413 scopus 로고    scopus 로고
    • Molecular mechanisms of neutrophil dysfunction in glycogen storage disease type Ib
    • H. S. Jun, D. A. Weinstein, Y. M. Lee, B. C. Mansfield, and J. Y. Chou, "Molecular mechanisms of neutrophil dysfunction in glycogen storage disease type Ib, " Blood, vol. 123, pp. 2843-2853, 2014.
    • (2014) Blood , vol.123 , pp. 2843-2853
    • Jun, H.S.1    Weinstein, D.A.2    Lee, Y.M.3    Mansfield, B.C.4    Chou, J.Y.5
  • 105
    • 0032709548 scopus 로고    scopus 로고
    • Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis
    • C. Toomes, J. James, A. J. Wood, et al., "Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis, " Nature Genetics, vol. 23, no. 4, pp. 421-424, 1999.
    • (1999) Nature Genetics , vol.23 , Issue.4 , pp. 421-424
    • Toomes, C.1    James, J.2    Wood, A.J.3
  • 106
    • 0033455594 scopus 로고    scopus 로고
    • Mutations of the cathepsin C gene are responsible for Papillon-Lefevre syndrome
    • T. C. Hart, P. S. Hart, D. W. Bowden, et al., "Mutations of the cathepsin C gene are responsible for Papillon-Lefevre syndrome, " Journal of Medical Genetics, vol. 36, no. 12, pp. 881-887, 1999.
    • (1999) Journal of Medical Genetics , vol.36 , Issue.12 , pp. 881-887
    • Hart, T.C.1    Hart, P.S.2    Bowden, D.W.3
  • 107
    • 0030897071 scopus 로고    scopus 로고
    • Human dipeptidylpeptidase I: Gene characterization, localization, and expression
    • N. V. Rao, G. V. Rao, and J. R. Hoidal, "Human dipeptidylpeptidase I: gene characterization, localization, and expression, " The Journal of Biological Chemistry, vol. 272, no. 15, pp. 10260-10265, 1997.
    • (1997) The Journal of Biological Chemistry , vol.272 , Issue.15 , pp. 10260-10265
    • Rao, N.V.1    Rao, G.V.2    Hoidal, J.R.3
  • 108
    • 0027518670 scopus 로고
    • Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase i
    • M. J. McGuire, P. E. Lipsky, and D. L. Thiele, "Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I, " Journal of Biological Chemistry, vol. 268, no. 4, pp. 2458-2467, 1993.
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.4 , pp. 2458-2467
    • McGuire, M.J.1    Lipsky, P.E.2    Thiele, D.L.3
  • 109
    • 0036168150 scopus 로고    scopus 로고
    • Dipeptidyl peptidase i activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis
    • A. M. Adkison, S. Z. Raptis, D. G. Kelley, and C. T. N. Pham, "Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis, "The Journal of Clinical Investigation, vol. 109, no. 3, pp. 363-371, 2002.
    • (2002) The Journal of Clinical Investigation , vol.109 , Issue.3 , pp. 363-371
    • Adkison, A.M.1    Raptis, S.Z.2    Kelley, D.G.3    Pham, C.T.N.4
  • 110
    • 0018330757 scopus 로고
    • The Papillon-Lefevre syndrome: Keratosis palmoplantaris with periodontopathy. Report of a case and review of the cases in the literature
    • E. Haneke, "The Papillon-Lefevre syndrome: keratosis palmoplantaris with periodontopathy. Report of a case and review of the cases in the literature, " Human Genetics, vol. 51, no. 1, pp. 1-35, 1979.
    • (1979) Human Genetics , vol.51 , Issue.1 , pp. 1-35
    • Haneke, E.1
  • 111
    • 0030160661 scopus 로고    scopus 로고
    • Papillon-Lefèvre syndrome: Analysis of neutrophil chemotaxis
    • E. Firatli, B. Tuzun, and A. Efeoglu, "Papillon-Lefèvre syndrome: analysis of neutrophil chemotaxis, " Journal of Periodontology, vol. 67, no. 6, pp. 617-620, 1996.
    • (1996) Journal of Periodontology , vol.67 , Issue.6 , pp. 617-620
    • Firatli, E.1    Tuzun, B.2    Efeoglu, A.3
  • 112
    • 0036214084 scopus 로고    scopus 로고
    • Shwachman-Diamond syndrome
    • O. P. Smith, "Shwachman-Diamond syndrome, " Seminars in Hematology, vol. 39, no. 2, pp. 95-102, 2002.
    • (2002) Seminars in Hematology , vol.39 , Issue.2 , pp. 95-102
    • Smith, O.P.1
  • 114
    • 62949240235 scopus 로고    scopus 로고
    • Shwachman-diamond syndrome neutrophils have altered chemoattractant-induced Factin polymerization and polarization characteristics
    • C. Orelio and T. W. Kuijpers, "Shwachman-diamond syndrome neutrophils have altered chemoattractant-induced Factin polymerization and polarization characteristics, " Haematologica, vol. 94, no. 3, pp. 409-413, 2009.
    • (2009) Haematologica , vol.94 , Issue.3 , pp. 409-413
    • Orelio, C.1    Kuijpers, T.W.2
  • 115
    • 0037229094 scopus 로고    scopus 로고
    • Mutations in SBDS are associated with Shwachman-Diamond syndrome
    • G. R. B. Boocock, J. A. Morrison, M. Popovic, et al., "Mutations in SBDS are associated with Shwachman-Diamond syndrome, " Nature Genetics, vol. 33, no. 1, pp. 97-101, 2003.
    • (2003) Nature Genetics , vol.33 , Issue.1 , pp. 97-101
    • Boocock, G.R.B.1    Morrison, J.A.2    Popovic, M.3
  • 116
    • 79952495602 scopus 로고    scopus 로고
    • Infections and immunodeficiency in Down syndrome
    • G. Ram and J. Chinen, "Infections and immunodeficiency in Down syndrome, " Clinical and Experimental Immunology, vol. 164, no. 1, pp. 9-16, 2011.
    • (2011) Clinical and Experimental Immunology , vol.164 , Issue.1 , pp. 9-16
    • Ram, G.1    Chinen, J.2
  • 117
    • 0027270192 scopus 로고
    • Nonspecific immunity in Down syndrome: A study of chemotaxis, phagocytosis, oxidative metabolism, and cell surface marker expression of polymorphonuclear cells
    • E. Novo, M. I. Garcia, and J. Lavergne, "Nonspecific immunity in Down syndrome: a study of chemotaxis, phagocytosis, oxidative metabolism, and cell surface marker expression of polymorphonuclear cells, " The American Journal of Medical Genetics, vol. 46, no. 4, pp. 384-391, 1993.
    • (1993) The American Journal of Medical Genetics , vol.46 , Issue.4 , pp. 384-391
    • Novo, E.1    Garcia, M.I.2    Lavergne, J.3
  • 118
    • 77956025424 scopus 로고    scopus 로고
    • In vivo labeling with 2H2O reveals a human neutrophil lifespan of 5. 4 days
    • J. Pillay, I. den Braber, N. Vrisekoop, et al., "In vivo labeling with 2H2O reveals a human neutrophil lifespan of 5. 4 days, " Blood, vol. 116, no. 4, pp. 625-627, 2010.
    • (2010) Blood , vol.116 , Issue.4 , pp. 625-627
    • Pillay, J.1    Den Braber, I.2    Vrisekoop, N.3
  • 119
    • 54049148978 scopus 로고    scopus 로고
    • Homeostatic regulation of blood neutrophil counts
    • S. von Vietinghoff and K. Ley, "Homeostatic regulation of blood neutrophil counts, " The Journal of Immunology, vol. 181, no. 8, pp. 5183-5188, 2008.
    • (2008) The Journal of Immunology , vol.181 , Issue.8 , pp. 5183-5188
    • Von Vietinghoff, S.1    Ley, K.2
  • 120
    • 44649094127 scopus 로고    scopus 로고
    • Migration across the sinusoidal endothelium regulates neutrophil mobilization in response to ELR + CXC chemokines
    • P. C. E. Burdon, C. Martin, and S. M. Rankin, "Migration across the sinusoidal endothelium regulates neutrophil mobilization in response to ELR + CXC chemokines, " British Journal of Haematology, vol. 142, no. 1, pp. 100-108, 2008.
    • (2008) British Journal of Haematology , vol.142 , Issue.1 , pp. 100-108
    • Burdon, P.C.E.1    Martin, C.2    Rankin, S.M.3
  • 121
    • 0037085788 scopus 로고    scopus 로고
    • Mechanical properties of rat bone marrow and circulating neutrophils and their responses to inflammatory mediators
    • H. Saito, J. Lai, R. Rogers, and C. M. Doerschuk, "Mechanical properties of rat bone marrow and circulating neutrophils and their responses to inflammatory mediators, " Blood, vol. 99, no. 6, pp. 2207-2213, 2002.
    • (2002) Blood , vol.99 , Issue.6 , pp. 2207-2213
    • Saito, H.1    Lai, J.2    Rogers, R.3    Doerschuk, C.M.4
  • 122
    • 0025299155 scopus 로고
    • Identification of surface proteins mediating adherence of CD11/CD18-deficient lymphoblastoid cells to cultured human endothelium
    • B. R. Schwartz, E. A. Wayner, T. M. Carlos, H. D. Ochs, and J. M. Harlan, "Identification of surface proteins mediating adherence of CD11/CD18-deficient lymphoblastoid cells to cultured human endothelium, " Journal of Clinical Investigation, vol. 85, no. 6, pp. 2019-2022, 1990.
    • (1990) Journal of Clinical Investigation , vol.85 , Issue.6 , pp. 2019-2022
    • Schwartz, B.R.1    Wayner, E.A.2    Carlos, T.M.3    Ochs, H.D.4    Harlan, J.M.5
  • 124
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • A. Belaaouaj, R. Mccarthy, M. Baumann, et al., "Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis, " Nature Medicine, vol. 4, no. 5, pp. 615-618, 1998.
    • (1998) Nature Medicine , vol.4 , Issue.5 , pp. 615-618
    • Belaaouaj, A.1    Mccarthy, R.2    Baumann, M.3
  • 125
    • 84942880384 scopus 로고    scopus 로고
    • The Jackson Laboratory MPD: Jaxpheno4, Mouse Phenome Database web site, The Jackson Laboratory, Bar Harbor, Me, USA
    • TheJacksonLaboratory, "Hematological survey of 11 inbred strains of mice, " MPD: Jaxpheno4, Mouse Phenome Database web site, The Jackson Laboratory, Bar Harbor, Me, USA, 2014, http://www.phenome.jax.org/.
    • (2014) Hematological Survey of 11 Inbred Strains of Mice
  • 127
    • 1842370351 scopus 로고    scopus 로고
    • Retroviral-mediated gene transfer of gp91phox into bone marrow cells rescues defect in host defense against Aspergillus fumigatus in murine X-linked chronic granulomatous disease
    • H. Bjorgvinsd?ttir, C. Ding, N. Pech, M. A. Gifford, L. L. Li, and M. C. Dinauer, "Retroviral-mediated gene transfer of gp91phox into bone marrow cells rescues defect in host defense against Aspergillus fumigatus in murine X-linked chronic granulomatous disease, " Blood, vol. 89, no. 1, pp. 41-48, 1997.
    • (1997) Blood , vol.89 , Issue.1 , pp. 41-48
    • Bjorgvinsdttir, H.1    Ding, C.2    Pech, N.3    Gifford, M.A.4    Li, L.L.5    Dinauer, M.C.6
  • 128
    • 0030940510 scopus 로고    scopus 로고
    • Enhanced host defense after gene transfer in the murine p47(phox)-deficient model of chronic granulomatous disease
    • M. Mardiney III, S. H. Jackson, S. K. Spratt, F. Li, S. M. Holland, and H. L. Malech, "Enhanced host defense after gene transfer in the murine p47(phox)-deficient model of chronic granulomatous disease, " Blood, vol. 89, no. 7, pp. 2268-2275, 1997.
    • (1997) Blood , vol.89 , Issue.7 , pp. 2268-2275
    • Mardiney, M.1    Jackson, S.H.2    Spratt, S.K.3    Li, F.4    Holland, S.M.5    Malech, H.L.6
  • 129
    • 84879883823 scopus 로고    scopus 로고
    • Gene therapy for PIDs: Progress, pitfalls and prospects
    • S. Mukherjee and A. J. Thrasher, "Gene therapy for PIDs: progress, pitfalls and prospects, " Gene, vol. 525, no. 2, pp. 174-181, 2013.
    • (2013) Gene , vol.525 , Issue.2 , pp. 174-181
    • Mukherjee, S.1    Thrasher, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.