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Volumn 9, Issue 3, 1997, Pages 319-323

Xid and Xid-like immunodeficiencies from a signaling point of view

Author keywords

[No Author keywords available]

Indexed keywords

LYMPHOCYTE RECEPTOR; PROTEIN KINASE C; PROTEIN TYROSINE KINASE;

EID: 0030740453     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(97)80076-3     Document Type: Article
Times cited : (21)

References (50)
  • 1
    • 0027959098 scopus 로고
    • Role of Bruton's tyrosine kinase in immunodeficiency
    • Tsukada S, Rawlings DJ, Witte ON. Role of Bruton's tyrosine kinase in immunodeficiency. Curr Opin Immunol. 6:1994;623-630.
    • (1994) Curr Opin Immunol , vol.6 , pp. 623-630
    • Tsukada, S.1    Rawlings, D.J.2    Witte, O.N.3
  • 3
    • 0028847329 scopus 로고
    • Defective B cell development and function in Btk-deficient mice
    • of outstanding interest. This study addresses the reason of much less severe immunodeficiency in xid mice as compared to XLA. In order to find whether the severity of Xid could be changed by additional alterations in Btk gene, the authors have generated Btk-deficient mice. Practically indistinguishable immunodeficiencies in Btk-deficient and xid mice suggest that severity of Xid is not dependent on the location of mutation. This study provides a comprehensive comparative analysis of the immune systems in xid and Btk-deficient mice.
    • Khan WN, Alt FW, Gerstein RM, Malynn BA, Larsson I, Rathbun G, Davidson L, Muller S, Kantor AB, Herzenberg LA, et al. Defective B cell development and function in Btk-deficient mice. of outstanding interest Immunity. 3:1995;283-299 This study addresses the reason of much less severe immunodeficiency in xid mice as compared to XLA. In order to find whether the severity of Xid could be changed by additional alterations in Btk gene, the authors have generated Btk-deficient mice. Practically indistinguishable immunodeficiencies in Btk-deficient and xid mice suggest that severity of Xid is not dependent on the location of mutation. This study provides a comprehensive comparative analysis of the immune systems in xid and Btk-deficient mice.
    • (1995) Immunity , vol.3 , pp. 283-299
    • Khan, W.N.1    Alt, F.W.2    Gerstein, R.M.3    Malynn, B.A.4    Larsson, I.5    Rathbun, G.6    Davidson, L.7    Muller, S.8    Kantor, A.B.9    Herzenberg, L.A.10
  • 4
    • 0028899718 scopus 로고
    • CD38 unresponsiveness of xid B cells implicates Bruton's tyrosine kinase (btk) as a regular of CD38 induced signal transduction
    • of special interest. Describes for the first time the alteration of CD38-mediated proliferation of xid B cells.
    • Santos-Argumedo L, Lund FE, Heath AW, Solvason N, Wu WW, Grimaldi JC, Parkhouse RM, Howard M. CD38 unresponsiveness of xid B cells implicates Bruton's tyrosine kinase (btk) as a regular of CD38 induced signal transduction. of special interest Int Immunol. 7:1995;163-170 Describes for the first time the alteration of CD38-mediated proliferation of xid B cells.
    • (1995) Int Immunol , vol.7 , pp. 163-170
    • Santos-Argumedo, L.1    Lund, F.E.2    Heath, A.W.3    Solvason, N.4    Wu, W.W.5    Grimaldi, J.C.6    Parkhouse, R.M.7    Howard, M.8
  • 5
    • 0028071612 scopus 로고
    • Murine B cell proliferation and protection from apoptosis with an antibody against a 105-kD molecule: Unresponsiveness of X-linked immunodeficient B cells
    • Miyake K, Yamashita Y, Hitoshi Y, Takatsu K, Kimoto M. Murine B cell proliferation and protection from apoptosis with an antibody against a 105-kD molecule: unresponsiveness of X-linked immunodeficient B cells. J Exp Med. 180:1994;1217-1224.
    • (1994) J Exp Med , vol.180 , pp. 1217-1224
    • Miyake, K.1    Yamashita, Y.2    Hitoshi, Y.3    Takatsu, K.4    Kimoto, M.5
  • 6
    • 0027329865 scopus 로고
    • IL-5 receptor positive B cells, but not eosinophils, are functionally and numerically influenced in mice carrying the X-linked immune defect
    • Hitoshi Y, Sonoda E, Kikuchi Y, Yonehara S, Nakauchi H, Takatsu H. IL-5 receptor positive B cells, but not eosinophils, are functionally and numerically influenced in mice carrying the X-linked immune defect. Int Immunol. 5:1993;1183-1190.
    • (1993) Int Immunol , vol.5 , pp. 1183-1190
    • Hitoshi, Y.1    Sonoda, E.2    Kikuchi, Y.3    Yonehara, S.4    Nakauchi, H.5    Takatsu, H.6
  • 7
    • 0025673971 scopus 로고
    • Interleukin 10, a novel B cell stimulatory factor: Unresponsiveness of X chromosome-linked immunodeficiency B cells
    • Go NF, Castle BE, Barret R, Kastelein R, Dang W, Mosmamm TR, Moore KW, Howard M. Interleukin 10, a novel B cell stimulatory factor: unresponsiveness of X chromosome-linked immunodeficiency B cells. J Exp Med. 172:1990;1625-1631.
    • (1990) J Exp Med , vol.172 , pp. 1625-1631
    • Go, N.F.1    Castle, B.E.2    Barret, R.3    Kastelein, R.4    Dang, W.5    Mosmamm, T.R.6    Moore, K.W.7    Howard, M.8
  • 8
    • 0030038840 scopus 로고    scopus 로고
    • Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases
    • of outstanding interest. Demonstrates the two-step mechanism of Btk tyrosine phosphorylation by Src-like kinases for the first time and reveals the exact position of phosphorylated tyrosines in Btk.
    • Rawlings DJ, Scharenberg AM, Park H, Wahl MI, Lin S, Kato RM, Fluckiger AC, Witte ON, Kinet JP. Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases. of outstanding interest Science. 271:1996;822-825 Demonstrates the two-step mechanism of Btk tyrosine phosphorylation by Src-like kinases for the first time and reveals the exact position of phosphorylated tyrosines in Btk.
    • (1996) Science , vol.271 , pp. 822-825
    • Rawlings, D.J.1    Scharenberg, A.M.2    Park, H.3    Wahl, M.I.4    Lin, S.5    Kato, R.M.6    Fluckiger, A.C.7    Witte, O.N.8    Kinet, J.P.9
  • 9
    • 0029976256 scopus 로고    scopus 로고
    • BTK base, mutation database for X-linked agammaglobulinemia (XLA)
    • of special interest. Very helpful compendium of Btk mutations.
    • Vihinen M, Iwata T, Kinnon C, Kwan SP, Ochs HD, Vorechovsky I, Smith CI. BTK base, mutation database for X-linked agammaglobulinemia (XLA). of special interest Nucleic Acids Res. 24:1996;160-165 Very helpful compendium of Btk mutations.
    • (1996) Nucleic Acids Res , vol.24 , pp. 160-165
    • Vihinen, M.1    Iwata, T.2    Kinnon, C.3    Kwan, S.P.4    Ochs, H.D.5    Vorechovsky, I.6    Smith, C.I.7
  • 10
    • 0030018304 scopus 로고    scopus 로고
    • A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-gamma 2
    • of special interest. This study demonstrates a diminished PLC-γ2 activation in Btk-deficient chicken lymphoma cells and suggests the cooperation between Btk and Syk in phosphorylation of PLC-γ2.
    • Takata M, Kurosaki T. A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-gamma 2. of special interest J Exp Med. 184:1996;31-40 This study demonstrates a diminished PLC-γ2 activation in Btk-deficient chicken lymphoma cells and suggests the cooperation between Btk and Syk in phosphorylation of PLC-γ2.
    • (1996) J Exp Med , vol.184 , pp. 31-40
    • Takata, M.1    Kurosaki, T.2
  • 11
    • 0030152357 scopus 로고    scopus 로고
    • Regulation of Btk function by a major autophosphorylation site within the SH3 domain
    • of outstanding interest. The gain-of-function mutant of Btk carries a point mutation in the PH domain that results in constitutive phosphorylation and increased membrane localization of the protein. Using this form of Btk the authors demonstrate the distinctive role of the phosphorylation of Y221 and Y551 residues (single-letter amino acid code) in Btk function.
    • Park H, Wahl MI, Afar DE, Turck CW, Rawlings DJ, Tam C, Scharenberg AM, Kinet JP, Witte ON. Regulation of Btk function by a major autophosphorylation site within the SH3 domain. of outstanding interest Immunity. 4:1996;515-525 The gain-of-function mutant of Btk carries a point mutation in the PH domain that results in constitutive phosphorylation and increased membrane localization of the protein. Using this form of Btk the authors demonstrate the distinctive role of the phosphorylation of Y221 and Y551 residues (single-letter amino acid code) in Btk function.
    • (1996) Immunity , vol.4 , pp. 515-525
    • Park, H.1    Wahl, M.I.2    Afar, D.E.3    Turck, C.W.4    Rawlings, D.J.5    Tam, C.6    Scharenberg, A.M.7    Kinet, J.P.8    Witte, O.N.9
  • 12
    • 0028999058 scopus 로고
    • Activation of Bruton's tyrosine kinase (BTK) by a point mutation in its pleckstrin homology (PH) domain
    • of outstanding interest. This study demonstrates that a single amino acid substitution in the PH domain of Btk (E41K) results in the constitutive activation of Btk. The mutated Btk becomes oncogenic for fibroblasts and induces the IL-5-independent growth of originally IL-5-dependent pro-B cells. Also suggests the direct correlation between membrane association and activation of Btk.
    • Li T, Tsukada S, Satterthwaite A, Havlik MH, Park H, Takatsu K, Witte ON. Activation of Bruton's tyrosine kinase (BTK) by a point mutation in its pleckstrin homology (PH) domain. of outstanding interest Immunity. 2:1995;451-460 This study demonstrates that a single amino acid substitution in the PH domain of Btk (E41K) results in the constitutive activation of Btk. The mutated Btk becomes oncogenic for fibroblasts and induces the IL-5-independent growth of originally IL-5-dependent pro-B cells. Also suggests the direct correlation between membrane association and activation of Btk.
    • (1995) Immunity , vol.2 , pp. 451-460
    • Li, T.1    Tsukada, S.2    Satterthwaite, A.3    Havlik, M.H.4    Park, H.5    Takatsu, K.6    Witte, O.N.7
  • 13
    • 0029124883 scopus 로고
    • Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian proto-oncogene c-cbl
    • cbl in the negative regulation of tyrosine kinase signaling.
    • cbl in the negative regulation of tyrosine kinase signaling.
    • (1995) Science , vol.269 , pp. 1102-1105
    • Yoon, C.H.1    Lee, J.2    Jongeward, G.D.3    Sternberg, P.W.4
  • 14
    • 0029098389 scopus 로고
    • The protein product of the c-cbl protooncogene is phosphorylated after B cell receptor stimulation and binds the SH3 domain of Bruton's tyrosine kinase
    • cbl interaction in vivo leaves the question about the physiological relevance of this interaction open.
    • cbl interaction in vivo leaves the question about the physiological relevance of this interaction open.
    • (1995) J Exp Med , vol.182 , pp. 611-615
    • Cory, G.O.1    Lovering, R.C.2    Hinshelwood, S.3    MacCarthy-Morrogh, L.4    Levinsky, R.J.5    Kinnon, C.6
  • 15
    • 0029348814 scopus 로고
    • The Btk subfamily of cytolasmic tyrosine kinases: Structure, regulation and function
    • Rawlings D, Witte ON. The Btk subfamily of cytolasmic tyrosine kinases: structure, regulation and function. Semin Immunol. 7:1995;237-246.
    • (1995) Semin Immunol , vol.7 , pp. 237-246
    • Rawlings, D.1    Witte, O.N.2
  • 16
    • 0029834340 scopus 로고    scopus 로고
    • Identification of Itk/Tsk Src homology 3 domain ligands
    • of outstanding interest. Demonstrates binding of Itk to Wiscott-Aldrich syndrome protein and suggests the Wiscott-Aldrich syndrome protein-Btk interaction.
    • Bunnell SC, Henry PA, Kolluri R, Kirchhausen T, Rickles RJ, Berg LJ. Identification of Itk/Tsk Src homology 3 domain ligands. of outstanding interest J Biol Chem. 271:1996;25646-25656 Demonstrates binding of Itk to Wiscott-Aldrich syndrome protein and suggests the Wiscott-Aldrich syndrome protein-Btk interaction.
    • (1996) J Biol Chem , vol.271 , pp. 25646-25656
    • Bunnell, S.C.1    Henry, P.A.2    Kolluri, R.3    Kirchhausen, T.4    Rickles, R.J.5    Berg, L.J.6
  • 17
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss A, Littman. Signal transduction by lymphocyte antigen receptors. Cell. 76:1994;263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman2
  • 18
    • 0027980301 scopus 로고
    • Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interaction
    • Cheng G, Ye ZS, Baltimore D. Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interaction. Proc Natl Acad Sci USA. 91:1994;8152-8155.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8152-8155
    • Cheng, G.1    Ye, Z.S.2    Baltimore, D.3
  • 19
    • 0029786988 scopus 로고    scopus 로고
    • Knockouts of Src-family kinases: Stiff bones, wimpy T cells, and bad memories
    • of special interest. The most 'fresh' update on the phenotypes of mice deficient for various Src-like kinases.
    • Lowell CA, Soriano P. Knockouts of Src-family kinases: stiff bones, wimpy T cells, and bad memories. of special interest Gen Devel. 10:1996;1845-1857 The most 'fresh' update on the phenotypes of mice deficient for various Src-like kinases.
    • (1996) Gen Devel , vol.10 , pp. 1845-1857
    • Lowell, C.A.1    Soriano, P.2
  • 20
    • 0031066598 scopus 로고    scopus 로고
    • Molecular targets of CD45 in B cell antigen receptor signal transduction
    • of special interest. Demonstrates the reduction of Btk phosphorylation in CD45-deficient myeloma cells. Confirms an important role of Src-like kinases in Btk phosphorylation.
    • Pao LI, Bedzyk WD, Persin C, Cambier JC. Molecular targets of CD45 in B cell antigen receptor signal transduction. of special interest J Immunol. 158:1997;1116-1124 Demonstrates the reduction of Btk phosphorylation in CD45-deficient myeloma cells. Confirms an important role of Src-like kinases in Btk phosphorylation.
    • (1997) J Immunol , vol.158 , pp. 1116-1124
    • Pao, L.I.1    Bedzyk, W.D.2    Persin, C.3    Cambier, J.C.4
  • 21
    • 0029891789 scopus 로고    scopus 로고
    • Regulation of Btk by Src family tyrosine kinases
    • of special interest. Demonstrates the binding of purified SH3 domains of several Src-like kinases to the consensus region within the TH domain of Btk. Provides the structural basis for Btk activation by Src-like kinases.
    • Afar DE, Park H, Howell BW, Rawlings DJ, Cooper J, Witte ON. Regulation of Btk by Src family tyrosine kinases. of special interest Mol Cell Biol. 16:1996;3465-3471 Demonstrates the binding of purified SH3 domains of several Src-like kinases to the consensus region within the TH domain of Btk. Provides the structural basis for Btk activation by Src-like kinases.
    • (1996) Mol Cell Biol , vol.16 , pp. 3465-3471
    • Afar, D.E.1    Park, H.2    Howell, B.W.3    Rawlings, D.J.4    Cooper, J.5    Witte, O.N.6
  • 22
    • 0028060150 scopus 로고
    • Temporal differences in the activation of three classes of non transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement
    • Saouaf SJ, Mahajan S, Rowley RB, Kut SA, Fargnoli J, Burkhardt AL, Tsukada S, Witte ON, Bolen JB. Temporal differences in the activation of three classes of non transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement. Proc Natl Acad Sci USA. 91:1994;9524-9528.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9524-9528
    • Saouaf, S.J.1    Mahajan, S.2    Rowley, R.B.3    Kut, S.A.4    Fargnoli, J.5    Burkhardt, A.L.6    Tsukada, S.7    Witte, O.N.8    Bolen, J.B.9
  • 23
  • 25
    • 0028049537 scopus 로고
    • Tyrosine phosphorylation and activation of Bruton tyrosine kinase upon Fc epsilon RI cross-linking
    • Kawakami Y, Yao L, Miura T, Tsukada S, Witte ON, Kawakami T. Tyrosine phosphorylation and activation of Bruton tyrosine kinase upon Fc epsilon RI cross-linking. Mol Cell Biol. 14:1994;5108-5113.
    • (1994) Mol Cell Biol , vol.14 , pp. 5108-5113
    • Kawakami, Y.1    Yao, L.2    Miura, T.3    Tsukada, S.4    Witte, O.N.5    Kawakami, T.6
  • 26
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-biphosphate
    • Harlan JE, Hajduk PJ, Yoon HS, Fesik SW. Pleckstrin homology domains bind to phosphatidylinositol-4,5-biphosphate. Nature. 371:1994;168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 27
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • of outstanding interest. Suggests the role of the PH domain in membrane association of PH-domain-containing proteins.
    • Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. of outstanding interest Cell. 83:1995;1037-1046 Suggests the role of the PH domain in membrane association of PH-domain-containing proteins.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 28
    • 0029824848 scopus 로고    scopus 로고
    • Mutation in the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity
    • of special interest. Compares the binding of various phospholipids to the wild-type and mutated froms of the PH domain of Btk. Explains an increased membrane association of mutated Btk (E41K) by increased affinity of the mutated protein to phospholipids.
    • Fukuda M, Kojima T, Kabayama H, Mikoshiba K. Mutation in the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity. of special interest J Biol Chem. 271:1996;30303-30306 Compares the binding of various phospholipids to the wild-type and mutated froms of the PH domain of Btk. Explains an increased membrane association of mutated Btk (E41K) by increased affinity of the mutated protein to phospholipids.
    • (1996) J Biol Chem , vol.271 , pp. 30303-30306
    • Fukuda, M.1    Kojima, T.2    Kabayama, H.3    Mikoshiba, K.4
  • 29
    • 0028564915 scopus 로고
    • The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C
    • Yao L, Kawakami Y, Kawakami T. The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C. Proc Natl Acad Sci USA. 91:1994;9175-9179.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9175-9179
    • Yao, L.1    Kawakami, Y.2    Kawakami, T.3
  • 30
    • 0028173394 scopus 로고
    • Binding of beta gamma subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase
    • Tsukada S, Simon MI, Witte ON, Katz A. Binding of beta gamma subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase. Proc Natl Acad Sci USA. 91:1994;11256-11260.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11256-11260
    • Tsukada, S.1    Simon, M.I.2    Witte, O.N.3    Katz, A.4
  • 31
    • 0028896344 scopus 로고
    • Activation of Tsk and Btk tyrosine kinases by G protein beta gamma subunits
    • of special interest. Demonstrates the regulation of Btk activity by G proteins.
    • Langhans-Rajasekaran SA, Wan Y, Huang XY. Activation of Tsk and Btk tyrosine kinases by G protein beta gamma subunits. of special interest Proc Natl Acad Sci USA. 92:1995;8601-8605 Demonstrates the regulation of Btk activity by G proteins.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8601-8605
    • Langhans-Rajasekaran, S.A.1    Wan, Y.2    Huang, X.Y.3
  • 33
    • 0029165836 scopus 로고
    • Activation and interaction with protein kinase C of a cytoplasmic tyrosine kinase, Itk/Tsk/Emt, on FcεeRI cross-linking on mast cells
    • of special interest. Provides further support for the role of PKC in the regulation of Btk-like kinases.
    • Kawakami Y, Yao L, Gibson S, Mills GB, Kawakami T. Activation and interaction with protein kinase C of a cytoplasmic tyrosine kinase, Itk/Tsk/Emt, on FcεeRI cross-linking on mast cells. of special interest J Immunol. 155:1995;3556-3562 Provides further support for the role of PKC in the regulation of Btk-like kinases.
    • (1995) J Immunol , vol.155 , pp. 3556-3562
    • Kawakami, Y.1    Yao, L.2    Gibson, S.3    Mills, G.B.4    Kawakami, T.5
  • 34
    • 0030273388 scopus 로고    scopus 로고
    • Protein kinase Cμ (PKCμ) associates with the B cell antigen receptor complex and regulates lymphocyte signalling
    • of special interest. Demonstrates the association of PKCμ with BCR and suggests potentially important role of this protein in BCR signaling.
    • Sidorenko SP, Law C-L, Klaus SJ, Chandran KA, Takata M, Kurosaki T, Clark EA. Protein kinase Cμ (PKCμ) associates with the B cell antigen receptor complex and regulates lymphocyte signalling. of special interest Immunity. 5:1996;353-363 Demonstrates the association of PKCμ with BCR and suggests potentially important role of this protein in BCR signaling.
    • (1996) Immunity , vol.5 , pp. 353-363
    • Sidorenko, S.P.1    Law, C.-L.2    Klaus, S.J.3    Chandran, K.A.4    Takata, M.5    Kurosaki, T.6    Clark, E.A.7
  • 36
    • 0030586680 scopus 로고    scopus 로고
    • Signaling through CD38 augments B cell antigen receptor (BCR) responses and is dependent on BCR expression
    • of special interest. Demonstrates the involvement of BCR-associated signaling molecules in CD38-mediated signaling.
    • Lund FE, Yu N, Kim KM, Reth M, Howard MC. Signaling through CD38 augments B cell antigen receptor (BCR) responses and is dependent on BCR expression. of special interest J Immunol. 157:1996;1455-1467 Demonstrates the involvement of BCR-associated signaling molecules in CD38-mediated signaling.
    • (1996) J Immunol , vol.157 , pp. 1455-1467
    • Lund, F.E.1    Yu, N.2    Kim, K.M.3    Reth, M.4    Howard, M.C.5
  • 37
    • 0028949390 scopus 로고
    • RP105, a novel B cell surface molecule implicated in B cell activation, is a member of the leucine-rich repeat protein family
    • of special interest. Describes the structure of RP105 protein. Very important study in view of the regulatory role of RP105 in IgM-mediated apoptosis of mature B cells.
    • Miyake K, Yamashita Y, Ogata M, Sudo T, Kimoto M. RP105, a novel B cell surface molecule implicated in B cell activation, is a member of the leucine-rich repeat protein family. of special interest J Immunol. 154:1995;3333-3340 Describes the structure of RP105 protein. Very important study in view of the regulatory role of RP105 in IgM-mediated apoptosis of mature B cells.
    • (1995) J Immunol , vol.154 , pp. 3333-3340
    • Miyake, K.1    Yamashita, Y.2    Ogata, M.3    Sudo, T.4    Kimoto, M.5
  • 40
    • 0029064680 scopus 로고
    • Impairment of T-cell-dependent B-cell responses and B-1 cell development in CD19-deficient mice
    • of outstanding interest. See annotation [41].
    • Rickert RC, Rajewsky K, Roes J. Impairment of T-cell-dependent B-cell responses and B-1 cell development in CD19-deficient mice. of outstanding interest Nature. 376:1995;352-355 See annotation [41].
    • (1995) Nature , vol.376 , pp. 352-355
    • Rickert, R.C.1    Rajewsky, K.2    Roes, J.3
  • 41
    • 15844412034 scopus 로고    scopus 로고
    • Disruption of the Cr2 locus results in a reduction in B-1a cells and in an impaired B cell response to T-dependnet antigen
    • of outstanding interest. This paper, along with [40], demonstrates an essential role of CD19/CD21 complex in the development or maintenance of B-1 cells. Reveals the difference in CD19 contribution for the T-cell-dependent and -independent B cell responses.
    • Ahearn JM, Fisher MB, Croix D, Goerg S, Ma M, Xia J, Zhou X, Howard RG, Rothstein TL, Carroll MC. Disruption of the Cr2 locus results in a reduction in B-1a cells and in an impaired B cell response to T-dependnet antigen. of outstanding interest Immunity. 4:1996;251-262 This paper, along with [40], demonstrates an essential role of CD19/CD21 complex in the development or maintenance of B-1 cells. Reveals the difference in CD19 contribution for the T-cell-dependent and -independent B cell responses.
    • (1996) Immunity , vol.4 , pp. 251-262
    • Ahearn, J.M.1    Fisher, M.B.2    Croix, D.3    Goerg, S.4    Ma, M.5    Xia, J.6    Zhou, X.7    Howard, R.G.8    Rothstein, T.L.9    Carroll, M.C.10
  • 42
    • 0028915948 scopus 로고
    • Defective signalling through the T- And B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene
    • of special interest. See annotation [43].
    • Zhang R, Alt FW, Davidson L, Orkin SH, Swat W. Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene. of special interest Nature. 374:1995;470-473 See annotation [43].
    • (1995) Nature , vol.374 , pp. 470-473
    • Zhang, R.1    Alt, F.W.2    Davidson, L.3    Orkin, S.H.4    Swat, W.5
  • 43
    • 0028956337 scopus 로고
    • Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav
    • of special interest. This paper, along with [42], demonstrates the critical role of Vav in antigen-receptor-mediated proliferation of B and T cells.
    • Tarakhovsky A, Turner M, Schaal S, Mee PJ, Duddy LP, Rajewsky K, Tybulewicz VLJ. Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav. of special interest Nature. 374:1995;467-470 This paper, along with [42], demonstrates the critical role of Vav in antigen-receptor-mediated proliferation of B and T cells.
    • (1995) Nature , vol.374 , pp. 467-470
    • Tarakhovsky, A.1    Turner, M.2    Schaal, S.3    Mee, P.J.4    Duddy, L.P.5    Rajewsky, K.6    Tybulewicz, V.L.J.7
  • 44
    • 0028958669 scopus 로고
    • The CD19/CR2/TAPA-1 complex of B lymphocytes: Linking natural to acquired immunity
    • Fearon DT, Carter RH. The CD19/CR2/TAPA-1 complex of B lymphocytes: linking natural to acquired immunity. Annu Rev Immunol. 13:1995;127-150.
    • (1995) Annu Rev Immunol , vol.13 , pp. 127-150
    • Fearon, D.T.1    Carter, R.H.2
  • 45
    • 0030176019 scopus 로고    scopus 로고
    • Activation of B lymphocytes: Integrating signals from CD19, CD22 and FcγRIIb1
    • Doody GM, Dempsey PW, Fearon DT. Activation of B lymphocytes: integrating signals from CD19, CD22 and FcγRIIb1. Curr Opin Immunol. 8:1996;378-382.
    • (1996) Curr Opin Immunol , vol.8 , pp. 378-382
    • Doody, G.M.1    Dempsey, P.W.2    Fearon, D.T.3
  • 46
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of rac-1 GDP/GTP exchange by vav protooncogene product
    • of outstanding interest. Resolves the long lasting problem about the substrate specificity of the Dbl-like domain of Vav. Demonstrates the role of Vav in the regulation of GDP/GTP exchange in the small G protein Rac in a very elegant way.
    • Crespo P, Schuebel KE, Ostrom AA, Gutkind JS, Bustelo X. Phosphotyrosine-dependent activation of rac-1 GDP/GTP exchange by vav protooncogene product. of outstanding interest Nature. 385:1997;169-172 Resolves the long lasting problem about the substrate specificity of the Dbl-like domain of Vav. Demonstrates the role of Vav in the regulation of GDP/GTP exchange in the small G protein Rac in a very elegant way.
    • (1997) Nature , vol.385 , pp. 169-172
    • Crespo, P.1    Schuebel, K.E.2    Ostrom, A.A.3    Gutkind, J.S.4    Bustelo, X.5
  • 47
    • 0028597993 scopus 로고
    • Signalling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors
    • Weng W-K, Jarvis L, LeBien TW. Signalling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors. J Biol Chem. 269:1994;32514-32521.
    • (1994) J Biol Chem , vol.269 , pp. 32514-32521
    • Weng, W.-K.1    Jarvis, L.2    Lebien, T.W.3
  • 48
    • 0028183406 scopus 로고
    • X-linked agammaglobulinemia: New approaches to old questions based on the identification of the defective gene
    • Conley ME, Parolini O, Rohrer J, Campana D. X-linked agammaglobulinemia: new approaches to old questions based on the identification of the defective gene. Immunol Rev. 138:1994;5-21.
    • (1994) Immunol Rev , vol.138 , pp. 5-21
    • Conley, M.E.1    Parolini, O.2    Rohrer, J.3    Campana, D.4
  • 49
    • 0029085548 scopus 로고
    • The spectrum of mutations in Btk that cause X-linked agammaglobulinemia
    • of special interest. A comprehensive compendium of mutations within the Btk locus.
    • Conley ME, Rohrer J. The spectrum of mutations in Btk that cause X-linked agammaglobulinemia. of special interest Clin Immunol Immunopathol. 76:1995;S192-S197 A comprehensive compendium of mutations within the Btk locus.
    • (1995) Clin Immunol Immunopathol , vol.76
    • Conley, M.E.1    Rohrer, J.2
  • 50
    • 8944246315 scopus 로고    scopus 로고
    • (S)-13-[(dimethylamino)methyl]-10,11,14,15-tetrahydro-4,9:16,21- dimetheno-1H, 13H-dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecene-1,3(2H)-dione (LY333531) and related analogues: Isozyme selective inhibitors of protein kinase C beta
    • of special interest. Describes the structure and properties of a selective inhibitor of PKCβ.
    • Jirousek MR, Gillig JR, Gonzalez CM, Heath WF, McDonald J, Neel DA, Rito CJ, Singh U, Stramm LE, Melikian-Badalian A, et al. (S)-13-[(dimethylamino)methyl]-10,11,14,15-tetrahydro-4,9:16,21-dimetheno-1H, 13H-dibenzo[e,k]pyrrolo[3,4-h][1,4,13]oxadiazacyclohexadecene-1,3(2H)-dione (LY333531) and related analogues: isozyme selective inhibitors of protein kinase C beta. of special interest J Med Chem. 39:1996;2664-2671 Describes the structure and properties of a selective inhibitor of PKCβ.
    • (1996) J Med Chem , vol.39 , pp. 2664-2671
    • Jirousek, M.R.1    Gillig, J.R.2    Gonzalez, C.M.3    Heath, W.F.4    McDonald, J.5    Neel, D.A.6    Rito, C.J.7    Singh, U.8    Stramm, L.E.9    Melikian-Badalian, A.10


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