메뉴 건너뛰기




Volumn 48, Issue 4, 2013, Pages 708-715

Recombinant production of human ICAM-1 chimeras by single step on column refolding and purification

Author keywords

Adhesion molecules; LFA 1; On column refolding

Indexed keywords

ADHESION MOLECULES; COST-EFFECTIVE METHODS; EXTRACELLULAR DOMAINS; IMMOBILIZED METAL AFFINITY COLUMNS; INTERCELLULAR ADHESION MOLECULE-1; ISOTHERMAL TITRATION CALORIMETRY; LFA-1; ON-COLUMN REFOLDING;

EID: 84878015583     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2013.03.006     Document Type: Article
Times cited : (7)

References (62)
  • 1
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • T.A. Springer Adhesion receptors of the immune system Nature 346 1990 425 434
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.A.1
  • 2
    • 66949136652 scopus 로고    scopus 로고
    • ICAM-1 signaling in endothelial cells
    • C. Lawson, and S. Wolf ICAM-1 signaling in endothelial cells Pharmacol Rep 61 2009 22 32
    • (2009) Pharmacol Rep , vol.61 , pp. 22-32
    • Lawson, C.1    Wolf, S.2
  • 3
    • 79955545574 scopus 로고    scopus 로고
    • ICAM-1: Getting a grip on leukocyte adhesion
    • E.O. Long ICAM-1: getting a grip on leukocyte adhesion J Immunol 186 2011 5021 5023
    • (2011) J Immunol , vol.186 , pp. 5021-5023
    • Long, E.O.1
  • 4
    • 77956625541 scopus 로고    scopus 로고
    • Uncoating of human rhinoviruses
    • R. Fuchs, and D. Blaas Uncoating of human rhinoviruses Rev Med Virol 20 2010 281 297
    • (2010) Rev Med Virol , vol.20 , pp. 281-297
    • Fuchs, R.1    Blaas, D.2
  • 5
    • 0026542081 scopus 로고
    • The binding site on ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site
    • A.R. Berendt, A. McDowall, A.G. Craig, P.A. Bates, M.J. Sternberg, and K. Marsh The binding site on ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site Cell 68 1992 71 81
    • (1992) Cell , vol.68 , pp. 71-81
    • Berendt, A.R.1    McDowall, A.2    Craig, A.G.3    Bates, P.A.4    Sternberg, M.J.5    Marsh, K.6
  • 6
    • 0026580223 scopus 로고
    • Plasmodium falciparum-infected erythrocytes bind ICAM-1 at a site distinct from LFA-1, Mac-1, and human rhinovirus
    • C.F. Ockenhouse, R. Betageri, T.A. Springer, and D.E. Staunton Plasmodium falciparum-infected erythrocytes bind ICAM-1 at a site distinct from LFA-1, Mac-1, and human rhinovirus Cell 68 1992 63 69
    • (1992) Cell , vol.68 , pp. 63-69
    • Ockenhouse, C.F.1    Betageri, R.2    Springer, T.A.3    Staunton, D.E.4
  • 7
    • 84857444327 scopus 로고    scopus 로고
    • Functional analysis of Plasmodium vivax VIR proteins reveals different subcellular localizations and cytoadherence to the ICAM-1 endothelial receptor
    • M. Bernabeu, F.J. Lopez, M. Ferrer, L. Martin-Jaular, A. Razaname, and G. Corradin Functional analysis of Plasmodium vivax VIR proteins reveals different subcellular localizations and cytoadherence to the ICAM-1 endothelial receptor Cell Microbiol 14 2012 386 400
    • (2012) Cell Microbiol , vol.14 , pp. 386-400
    • Bernabeu, M.1    Lopez, F.J.2    Ferrer, M.3    Martin-Jaular, L.4    Razaname, A.5    Corradin, G.6
  • 8
    • 0025759969 scopus 로고
    • Binding of the integrin Mac-1 (CD11b/CD18) to the third immunoglobulin-like domain of ICAM-1 (CD54) and its regulation by glycosylation
    • M.S. Diamond, D.E. Staunton, S.D. Marlin, and T.A. Springer Binding of the integrin Mac-1 (CD11b/CD18) to the third immunoglobulin-like domain of ICAM-1 (CD54) and its regulation by glycosylation Cell 65 1991 961 971
    • (1991) Cell , vol.65 , pp. 961-971
    • Diamond, M.S.1    Staunton, D.E.2    Marlin, S.D.3    Springer, T.A.4
  • 9
    • 0027195088 scopus 로고
    • Functional studies of truncated soluble intercellular adhesion molecule 1 expressed in Escherichia coli
    • S. Martin, A. Martin, D.E. Staunton, and T.A. Springer Functional studies of truncated soluble intercellular adhesion molecule 1 expressed in Escherichia coli Antimicrob Agents Chemother 37 1993 1278 1284
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 1278-1284
    • Martin, S.1    Martin, A.2    Staunton, D.E.3    Springer, T.A.4
  • 10
    • 0025269047 scopus 로고
    • The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus
    • D.E. Staunton, M.L. Dustin, H.P. Erickson, and T.A. Springer The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus Cell 61 1990 243 254
    • (1990) Cell , vol.61 , pp. 243-254
    • Staunton, D.E.1    Dustin, M.L.2    Erickson, H.P.3    Springer, T.A.4
  • 11
    • 0028176012 scopus 로고
    • Involvement of the "i" domain of LFA-1 in selective binding to ligands ICAM-1 and ICAM-3
    • R.C. Landis, A. McDowall, C.L. Holness, A.J. Littler, D.L. Simmons, and N. Hogg Involvement of the "I" domain of LFA-1 in selective binding to ligands ICAM-1 and ICAM-3 J Cell Biol 126 1994 529 537
    • (1994) J Cell Biol , vol.126 , pp. 529-537
    • Landis, R.C.1    McDowall, A.2    Holness, C.L.3    Littler, A.J.4    Simmons, D.L.5    Hogg, N.6
  • 12
    • 0029059578 scopus 로고
    • A binding interface on the i domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1)
    • C. Huang, and T.A. Springer A binding interface on the I domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1) J Biol Chem 270 1995 19008 19016
    • (1995) J Biol Chem , vol.270 , pp. 19008-19016
    • Huang, C.1    Springer, T.A.2
  • 14
    • 0031017065 scopus 로고    scopus 로고
    • Molecular identification of a novel fibrinogen binding site on the first domain of ICAM-1 regulating leukocyte-endothelium bridging
    • A. Duperray, L.R. Languino, J. Plescia, A. McDowall, N. Hogg, and A.G. Craig Molecular identification of a novel fibrinogen binding site on the first domain of ICAM-1 regulating leukocyte-endothelium bridging J Biol Chem 272 1997 435 441
    • (1997) J Biol Chem , vol.272 , pp. 435-441
    • Duperray, A.1    Languino, L.R.2    Plescia, J.3    McDowall, A.4    Hogg, N.5    Craig, A.G.6
  • 15
    • 0028785507 scopus 로고
    • Intercellular adhesion molecule-1 dimerization and its consequences for adhesion mediated by lymphocyte function associated-1
    • J. Miller, R. Knorr, M. Ferrone, R. Houdei, C.P. Carron, and M.L. Dustin Intercellular adhesion molecule-1 dimerization and its consequences for adhesion mediated by lymphocyte function associated-1 J Exp Med 182 1995 1231 1241
    • (1995) J Exp Med , vol.182 , pp. 1231-1241
    • Miller, J.1    Knorr, R.2    Ferrone, M.3    Houdei, R.4    Carron, C.P.5    Dustin, M.L.6
  • 16
    • 0029013298 scopus 로고
    • The native structure of intercellular adhesion molecule-1 (ICAM-1) is a dimer. Correlation with binding to LFA-1
    • P.L. Reilly, J.R. Woska Jr., D.D. Jeanfavre, E. McNally, R. Rothlein, and B.J. Bormann The native structure of intercellular adhesion molecule-1 (ICAM-1) is a dimer. Correlation with binding to LFA-1 J Immunol 155 1995 529 532
    • (1995) J Immunol , vol.155 , pp. 529-532
    • Reilly, P.L.1    Woska, Jr.J.R.2    Jeanfavre, D.D.3    McNally, E.4    Rothlein, R.5    Bormann, B.J.6
  • 17
    • 0032516060 scopus 로고    scopus 로고
    • A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1
    • J.M. Casasnovas, T. Stehle, J.H. Liu, J.H. Wang, and T.A. Springer A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1 Proc Natl Acad Sci USA 95 1998 4134 4139
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4134-4139
    • Casasnovas, J.M.1    Stehle, T.2    Liu, J.H.3    Wang, J.H.4    Springer, T.A.5
  • 18
    • 0035811057 scopus 로고    scopus 로고
    • Dimerization and the effectiveness of ICAM-1 in mediating LFA-1-dependent adhesion
    • C.D. Jun, M. Shimaoka, C.V. Carman, J. Takagi, and T.A. Springer Dimerization and the effectiveness of ICAM-1 in mediating LFA-1-dependent adhesion Proc Natl Acad Sci USA 98 2001 6830 6835
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6830-6835
    • Jun, C.D.1    Shimaoka, M.2    Carman, C.V.3    Takagi, J.4    Springer, T.A.5
  • 19
    • 0031738502 scopus 로고    scopus 로고
    • Soluble forms of intercellular adhesion molecule-1 inhibit insulitis and onset of autoimmune diabetes
    • S. Martin, E. Heidenthal, B. Schulte, H. Rothe, and H. Kolb Soluble forms of intercellular adhesion molecule-1 inhibit insulitis and onset of autoimmune diabetes Diabetologia 41 1998 1298 1303
    • (1998) Diabetologia , vol.41 , pp. 1298-1303
    • Martin, S.1    Heidenthal, E.2    Schulte, B.3    Rothe, H.4    Kolb, H.5
  • 20
    • 78649455687 scopus 로고    scopus 로고
    • Intermediate monomer-dimer equilibrium structure of native ICAM-1: Implication for enhanced cell adhesion
    • H.M. Oh, M.S. Kwon, H.J. Kim, B.H. Jeon, H.R. Kim, and H.O. Choi Intermediate monomer-dimer equilibrium structure of native ICAM-1: implication for enhanced cell adhesion Exp Cell Res 317 2011 163 172
    • (2011) Exp Cell Res , vol.317 , pp. 163-172
    • Oh, H.M.1    Kwon, M.S.2    Kim, H.J.3    Jeon, B.H.4    Kim, H.R.5    Choi, H.O.6
  • 21
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • T.A. Springer Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm Cell 76 1994 301 314
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 22
    • 33645162400 scopus 로고    scopus 로고
    • Lymphocyte transcellular migration occurs through recruitment of endothelial ICAM-1 to caveola- and F-actin-rich domains
    • J. Millan, L. Hewlett, M. Glyn, D. Toomre, P. Clark, and A.J. Ridley Lymphocyte transcellular migration occurs through recruitment of endothelial ICAM-1 to caveola- and F-actin-rich domains Nat Cell Biol 8 2006 113 123
    • (2006) Nat Cell Biol , vol.8 , pp. 113-123
    • Millan, J.1    Hewlett, L.2    Glyn, M.3    Toomre, D.4    Clark, P.5    Ridley, A.J.6
  • 23
    • 84857688656 scopus 로고    scopus 로고
    • Integrin inside-out signaling and the immunological synapse
    • T.A. Springer, and M.L. Dustin Integrin inside-out signaling and the immunological synapse Curr Opin Cell Biol 24 2012 107 115
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 107-115
    • Springer, T.A.1    Dustin, M.L.2
  • 24
    • 54049114757 scopus 로고    scopus 로고
    • ICAM-1: Role in inflammation and in the regulation of vascular permeability
    • P.G. Frank, and M.P. Lisanti ICAM-1: role in inflammation and in the regulation of vascular permeability Am J Physiol Heart Circ Physiol 295 2008 H926 H927
    • (2008) Am J Physiol Heart Circ Physiol , vol.295
    • Frank, P.G.1    Lisanti, M.P.2
  • 25
    • 33847216148 scopus 로고    scopus 로고
    • Endothelial cell adhesion molecules and cancer progression
    • H. Kobayashi, K.C. Boelte, and P.C. Lin Endothelial cell adhesion molecules and cancer progression Curr Med Chem 14 2007 377 386
    • (2007) Curr Med Chem , vol.14 , pp. 377-386
    • Kobayashi, H.1    Boelte, K.C.2    Lin, P.C.3
  • 27
    • 0027930709 scopus 로고
    • Enhanced metastatic ability of TNF-alpha-treated malignant melanoma cells is reduced by intercellular adhesion molecule-1 (ICAM-1, CD54) antisense oligonucleotides
    • M.E. Miele, C.F. Bennett, B.E. Miller, and D.R. Welch Enhanced metastatic ability of TNF-alpha-treated malignant melanoma cells is reduced by intercellular adhesion molecule-1 (ICAM-1, CD54) antisense oligonucleotides Exp Cell Res 214 1994 231 241
    • (1994) Exp Cell Res , vol.214 , pp. 231-241
    • Miele, M.E.1    Bennett, C.F.2    Miller, B.E.3    Welch, D.R.4
  • 28
    • 84876363986 scopus 로고    scopus 로고
    • PSGL-1/selectin and ICAM-1/CD18 interactions are involved in macrophage-induced drug resistance in myeloma
    • Y. Zheng, J. Yang, J. Qian, P. Qiu, S. Hanabuchi, and Y. Lu PSGL-1/selectin and ICAM-1/CD18 interactions are involved in macrophage-induced drug resistance in myeloma Leukemia 189 2012 786 792
    • (2012) Leukemia , vol.189 , pp. 786-792
    • Zheng, Y.1    Yang, J.2    Qian, J.3    Qiu, P.4    Hanabuchi, S.5    Lu, Y.6
  • 29
    • 0026348189 scopus 로고
    • ICAM-1-dependent pathway is critically involved in the pathogenesis of adjuvant arthritis in rats
    • Y. Iigo, T. Takashi, T. Tamatani, M. Miyasaka, T. Higashida, and H. Yagita ICAM-1-dependent pathway is critically involved in the pathogenesis of adjuvant arthritis in rats J Immunol 147 1991 4167 4171
    • (1991) J Immunol , vol.147 , pp. 4167-4171
    • Iigo, Y.1    Takashi, T.2    Tamatani, T.3    Miyasaka, M.4    Higashida, T.5    Yagita, H.6
  • 30
    • 36048979880 scopus 로고    scopus 로고
    • Vascular adhesion molecules in atherosclerosis
    • E. Galkina, and K. Ley Vascular adhesion molecules in atherosclerosis Arterioscler Thromb Vasc Biol 27 2007 2292 2301
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 2292-2301
    • Galkina, E.1    Ley, K.2
  • 31
    • 54349115416 scopus 로고    scopus 로고
    • Lymphocyte homing and its role in the pathogenesis of IBD
    • B. Eksteen, E. Liaskou, and D.H. Adams Lymphocyte homing and its role in the pathogenesis of IBD Inflamm Bowel Dis 14 2008 1298 1312
    • (2008) Inflamm Bowel Dis , vol.14 , pp. 1298-1312
    • Eksteen, B.1    Liaskou, E.2    Adams, D.H.3
  • 32
    • 84861318436 scopus 로고    scopus 로고
    • Targeting leukocyte migration and adhesion in Crohn's disease and ulcerative colitis
    • S. Thomas, and D.C. Baumgart Targeting leukocyte migration and adhesion in Crohn's disease and ulcerative colitis Inflammopharmacology 20 2012 1 18
    • (2012) Inflammopharmacology , vol.20 , pp. 1-18
    • Thomas, S.1    Baumgart, D.C.2
  • 33
    • 4944227529 scopus 로고    scopus 로고
    • Inhibition of ICAM-1 gene expression, monocyte adhesion and cancer cell invasion by targeting IKK complex: Molecular and functional study of novel alpha-methylene-gamma-butyrolactone derivatives
    • W.C. Huang, S.T. Chan, T.L. Yang, C.C. Tzeng, and C.C. Chen Inhibition of ICAM-1 gene expression, monocyte adhesion and cancer cell invasion by targeting IKK complex: molecular and functional study of novel alpha-methylene-gamma- butyrolactone derivatives Carcinogenesis 25 2004 1925 1934
    • (2004) Carcinogenesis , vol.25 , pp. 1925-1934
    • Huang, W.C.1    Chan, S.T.2    Yang, T.L.3    Tzeng, C.C.4    Chen, C.C.5
  • 34
    • 4844223386 scopus 로고    scopus 로고
    • Therapeutic antagonists and the conformational regulation of the beta2 integrins
    • M. Shimaoka, and T.A. Springer Therapeutic antagonists and the conformational regulation of the beta2 integrins Curr Top Med Chem 4 2004 1485 1495
    • (2004) Curr Top Med Chem , vol.4 , pp. 1485-1495
    • Shimaoka, M.1    Springer, T.A.2
  • 35
    • 0038404760 scopus 로고    scopus 로고
    • Targeting ICAM-1/LFA-1 interaction for controlling autoimmune diseases: Designing peptide and small molecule inhibitors
    • M.E. Anderson, and T.J. Siahaan Targeting ICAM-1/LFA-1 interaction for controlling autoimmune diseases: designing peptide and small molecule inhibitors Peptides 24 2003 487 501
    • (2003) Peptides , vol.24 , pp. 487-501
    • Anderson, M.E.1    Siahaan, T.J.2
  • 36
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • J. Porath, J. Carlsson, I. Olsson, and G. Belfrage Metal chelate affinity chromatography, a new approach to protein fractionation Nature 258 1975 598 599
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 37
    • 0025202555 scopus 로고
    • Protein interactions with immobilized transition metal ions: Quantitative evaluations of variations in affinity and binding capacity
    • T.W. Hutchens, and T.T. Yip Protein interactions with immobilized transition metal ions: quantitative evaluations of variations in affinity and binding capacity Anal Biochem 191 1990 160 168
    • (1990) Anal Biochem , vol.191 , pp. 160-168
    • Hutchens, T.W.1    Yip, T.T.2
  • 38
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • H. Lilie, E. Schwarz, and R. Rudolph Advances in refolding of proteins produced in E. coli Curr Opin Biotechnol 9 1998 497 501
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 39
    • 0028348944 scopus 로고
    • Protein refolding at high concentrations using detergent/phospholipid mixtures
    • G. Zardeneta, and P.M. Horowitz Protein refolding at high concentrations using detergent/phospholipid mixtures Anal Biochem 218 1994 392 398
    • (1994) Anal Biochem , vol.218 , pp. 392-398
    • Zardeneta, G.1    Horowitz, P.M.2
  • 40
    • 0036922141 scopus 로고    scopus 로고
    • Chromatographic methods for the isolation of, and refolding of proteins from, Escherichia coli inclusion bodies
    • Z. Gu, M. Weidenhaupt, N. Ivanova, M. Pavlov, B. Xu, and Z.G. Su Chromatographic methods for the isolation of, and refolding of proteins from, Escherichia coli inclusion bodies Protein Expr Purif 25 2002 174 179
    • (2002) Protein Expr Purif , vol.25 , pp. 174-179
    • Gu, Z.1    Weidenhaupt, M.2    Ivanova, N.3    Pavlov, M.4    Xu, B.5    Su, Z.G.6
  • 41
    • 0023181996 scopus 로고
    • Refolding of denatured thioredoxin observed by size-exclusion chromatography
    • W. Shalongo, R. Ledger, M.V. Jagannadham, and E. Stellwagen Refolding of denatured thioredoxin observed by size-exclusion chromatography Biochemistry 26 1987 3135 3141
    • (1987) Biochemistry , vol.26 , pp. 3135-3141
    • Shalongo, W.1    Ledger, R.2    Jagannadham, M.V.3    Stellwagen, E.4
  • 42
    • 0033962914 scopus 로고    scopus 로고
    • Refolding and purification of a urokinase plasminogen activator fragment by chromatography
    • E.M. Fahey, J.B. Chaudhuri, and P. Binding Refolding and purification of a urokinase plasminogen activator fragment by chromatography J Chromatogr B Biomed Sci Appl 737 2000 225 235
    • (2000) J Chromatogr B Biomed Sci Appl , vol.737 , pp. 225-235
    • Fahey, E.M.1    Chaudhuri, J.B.2    Binding, P.3
  • 44
    • 4544387635 scopus 로고    scopus 로고
    • Refolding and purification of interferon-gamma in industry by hydrophobic interaction chromatography
    • X. Geng, Q. Bai, Y. Zhang, X. Li, and D. Wu Refolding and purification of interferon-gamma in industry by hydrophobic interaction chromatography J Biotechnol 113 2004 137 149
    • (2004) J Biotechnol , vol.113 , pp. 137-149
    • Geng, X.1    Bai, Q.2    Zhang, Y.3    Li, X.4    Wu, D.5
  • 45
  • 46
    • 0034705827 scopus 로고    scopus 로고
    • Model process for separation based on unfolding and refolding of chymotrypsin inhibitor 2 in thermoseparating polymer two-phase systems
    • H. Umakoshi, J. Persson, M. Kroon, H.O. Johansson, D.E. Otzen, and R. Kuboi Model process for separation based on unfolding and refolding of chymotrypsin inhibitor 2 in thermoseparating polymer two-phase systems J Chromatogr B Biomed Sci Appl 743 2000 13 19
    • (2000) J Chromatogr B Biomed Sci Appl , vol.743 , pp. 13-19
    • Umakoshi, H.1    Persson, J.2    Kroon, M.3    Johansson, H.O.4    Otzen, D.E.5    Kuboi, R.6
  • 47
    • 26444467667 scopus 로고    scopus 로고
    • On-column protein refolding for crystallization
    • N. Oganesyan, S.H. Kim, and R. Kim On-column protein refolding for crystallization J Struct Funct Genomics 6 2005 177 182
    • (2005) J Struct Funct Genomics , vol.6 , pp. 177-182
    • Oganesyan, N.1    Kim, S.H.2    Kim, R.3
  • 48
    • 0032584765 scopus 로고    scopus 로고
    • Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography
    • H. Rogl, K. Kosemund, W. Kuhlbrandt, and I. Collinson Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography FEBS Lett 432 1998 21 26
    • (1998) FEBS Lett , vol.432 , pp. 21-26
    • Rogl, H.1    Kosemund, K.2    Kuhlbrandt, W.3    Collinson, I.4
  • 49
    • 0031810858 scopus 로고    scopus 로고
    • Three-step purification of lipopolysaccharide-free, polyhistidine-tagged recombinant antigens of Mycobacterium tuberculosis
    • R. Colangeli, A. Heijbel, A.M. Williams, C. Manca, J. Chan, and K. Lyashchenko Three-step purification of lipopolysaccharide-free, polyhistidine-tagged recombinant antigens of Mycobacterium tuberculosis J Chromatogr B Biomed Sci Appl 714 1998 223 235
    • (1998) J Chromatogr B Biomed Sci Appl , vol.714 , pp. 223-235
    • Colangeli, R.1    Heijbel, A.2    Williams, A.M.3    Manca, C.4    Chan, J.5    Lyashchenko, K.6
  • 51
    • 0033789773 scopus 로고    scopus 로고
    • Linear and cyclic LFA-1 and ICAM-1 peptides inhibit T cell adhesion and function
    • S.A. Tibbetts, S.D. Jois, T.J. Siahaan, S.H. Benedict, and M.A. Chan Linear and cyclic LFA-1 and ICAM-1 peptides inhibit T cell adhesion and function Peptides 21 2000 1161 1167
    • (2000) Peptides , vol.21 , pp. 1161-1167
    • Tibbetts, S.A.1    Jois, S.D.2    Siahaan, T.J.3    Benedict, S.H.4    Chan, M.A.5
  • 52
    • 0032533487 scopus 로고    scopus 로고
    • The same natural ligand is involved in allorecognition of multiple HLA-B27 subtypes by a single T cell clone: Role of peptide and the MHC molecule in alloreactivity
    • A. Paradela, M. Garcia-Peydro, J. Vazquez, D. Rognan, and J.A. Lopez de Castro The same natural ligand is involved in allorecognition of multiple HLA-B27 subtypes by a single T cell clone: role of peptide and the MHC molecule in alloreactivity J Immunol 161 1998 5481 5490
    • (1998) J Immunol , vol.161 , pp. 5481-5490
    • Paradela, A.1    Garcia-Peydro, M.2    Vazquez, J.3    Rognan, D.4    Lopez De Castro, J.A.5
  • 53
    • 0022453692 scopus 로고
    • A human intercellular adhesion molecule (ICAM-1) distinct from LFA-1
    • R. Rothlein, M.L. Dustin, S.D. Marlin, and T.A. Springer A human intercellular adhesion molecule (ICAM-1) distinct from LFA-1 J Immunol 137 1986 1270 1274
    • (1986) J Immunol , vol.137 , pp. 1270-1274
    • Rothlein, R.1    Dustin, M.L.2    Marlin, S.D.3    Springer, T.A.4
  • 54
    • 84965822602 scopus 로고
    • Feasibility of drug screening with panels of human tumor cell lines using a microculture tetrazolium assay
    • M.C. Alley, D.A. Scudiero, A. Monks, M.L. Hursey, M.J. Czerwinski, and D.L. Fine Feasibility of drug screening with panels of human tumor cell lines using a microculture tetrazolium assay Cancer Res 48 1988 589 601
    • (1988) Cancer Res , vol.48 , pp. 589-601
    • Alley, M.C.1    Scudiero, D.A.2    Monks, A.3    Hursey, M.L.4    Czerwinski, M.J.5    Fine, D.L.6
  • 55
    • 79961094856 scopus 로고    scopus 로고
    • Phenotypic and functional evaluation of CD3 + CD4 - CD8- T cells in human CD8 immunodeficiency
    • I. Bernardo, E. Mancebo, I. Aguilo, A. Anel, L.M. Allende, and J.M. Guerra-Vales Phenotypic and functional evaluation of CD3 + CD4 - CD8- T cells in human CD8 immunodeficiency Haematologica 96 2011 1195 1203
    • (2011) Haematologica , vol.96 , pp. 1195-1203
    • Bernardo, I.1    Mancebo, E.2    Aguilo, I.3    Anel, A.4    Allende, L.M.5    Guerra-Vales, J.M.6
  • 57
    • 0037297123 scopus 로고    scopus 로고
    • One-step purification and refolding of recombinant photoprotein aequorin by immobilized metal-ion affinity chromatography
    • K. Glynou, P.C. Ioannou, and T.K. Christopoulos One-step purification and refolding of recombinant photoprotein aequorin by immobilized metal-ion affinity chromatography Protein Expr Purif 27 2003 384 390
    • (2003) Protein Expr Purif , vol.27 , pp. 384-390
    • Glynou, K.1    Ioannou, P.C.2    Christopoulos, T.K.3
  • 58
    • 0024296564 scopus 로고
    • Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families
    • D.E. Staunton, S.D. Marlin, C. Stratowa, M.L. Dustin, and T.A. Springer Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families Cell 52 1988 925 933
    • (1988) Cell , vol.52 , pp. 925-933
    • Staunton, D.E.1    Marlin, S.D.2    Stratowa, C.3    Dustin, M.L.4    Springer, T.A.5
  • 59
    • 0032531998 scopus 로고    scopus 로고
    • Affinity and kinetic analysis of the molecular interaction of ICAM-1 and leukocyte function-associated antigen-1
    • Y. Tominaga, Y. Kita, A. Satoh, S. Asai, K. Kato, and K. Ishikawa Affinity and kinetic analysis of the molecular interaction of ICAM-1 and leukocyte function-associated antigen-1 J Immunol 161 1998 4016 4022
    • (1998) J Immunol , vol.161 , pp. 4016-4022
    • Tominaga, Y.1    Kita, Y.2    Satoh, A.3    Asai, S.4    Kato, K.5    Ishikawa, K.6
  • 60
    • 78751641702 scopus 로고    scopus 로고
    • The latest developments in synthetic peptides with immunoregulatory activities
    • C.L. Zhou, R. Lu, G. Lin, and Z. Yao The latest developments in synthetic peptides with immunoregulatory activities Peptides 32 2011 408 414
    • (2011) Peptides , vol.32 , pp. 408-414
    • Zhou, C.L.1    Lu, R.2    Lin, G.3    Yao, Z.4
  • 61
    • 68249149660 scopus 로고    scopus 로고
    • Integrin-dependent organization and bidirectional vesicular traffic at cytotoxic immune synapses
    • D. Liu, Y.T. Bryceson, T. Meckel, G. Vasiliver-Shamis, M.L. Dustin, and E.O. Long Integrin-dependent organization and bidirectional vesicular traffic at cytotoxic immune synapses Immunity 31 2009 99 109
    • (2009) Immunity , vol.31 , pp. 99-109
    • Liu, D.1    Bryceson, Y.T.2    Meckel, T.3    Vasiliver-Shamis, G.4    Dustin, M.L.5    Long, E.O.6
  • 62
    • 25844464180 scopus 로고    scopus 로고
    • Cytolytic granule polarization and degranulation controlled by different receptors in resting NK cells
    • Y.T. Bryceson, M.E. March, D.F. Barber, H.G. Ljunggren, and E.O. Long Cytolytic granule polarization and degranulation controlled by different receptors in resting NK cells J Exp Med 202 2005 1001 1012
    • (2005) J Exp Med , vol.202 , pp. 1001-1012
    • Bryceson, Y.T.1    March, M.E.2    Barber, D.F.3    Ljunggren, H.G.4    Long, E.O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.