메뉴 건너뛰기




Volumn 8, Issue 12, 2007, Pages 1269-1271

Bacterial cell walls, innate immunity and immunoadjuvants

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; BACTERIAL ENZYME; BACTERIAL POLYSACCHARIDE; BETA INTERFERON; CASPASE RECRUITMENT DOMAIN PROTEIN 15; CELL PROTEIN; CYTOKINE; FREUND ADJUVANT; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IMMUNOLOGICAL ADJUVANT; INTERLEUKIN 1BETA CONVERTING ENZYME; MITOGEN ACTIVATED PROTEIN KINASE; MURABUTIDE; MURAMYL TRIPEPTIDE; N ACETYLGLUCOSAMINE; PENICILLIN G; PEPTIDOGLYCAN POLYSACCHARIDE; TOLL LIKE RECEPTOR;

EID: 36248970136     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni1207-1269     Document Type: Article
Times cited : (21)

References (21)
  • 1
    • 33646165991 scopus 로고    scopus 로고
    • The tortuous journey of a biochemist to Immunoland and what he found there (prefatory chaprter)
    • Strominger, J.L. (2006). The tortuous journey of a biochemist to Immunoland and what he found there (prefatory chaprter). Annu. Rev. Inimunol. 24, 1-31 (2006).
    • (2006) Annu. Rev. Inimunol , vol.24 , pp. 1-31
    • Strominger, J.L.1
  • 2
    • 84873759632 scopus 로고
    • Uridine-5'-pyrophosphate derivatives. III. Amino acid-containing derivatives
    • Park, J.T. Uridine-5'-pyrophosphate derivatives. III. Amino acid-containing derivatives. J. Biol. Chem. 194, 897-904(1952).
    • (1952) J. Biol. Chem , vol.194 , pp. 897-904
    • Park, J.T.1
  • 3
    • 33646186467 scopus 로고
    • The amino acid sequence in the uridine nucleotide-peptide from Staphylococcus aureus
    • Strominger, J.L. The amino acid sequence in the uridine nucleotide-peptide from Staphylococcus aureus. C. R. Trav. Lab. Carlsberg 3l, 181-192 (1959).
    • (1959) C. R. Trav. Lab. Carlsberg , vol.3 l , pp. 181-192
    • Strominger, J.L.1
  • 4
    • 0002239231 scopus 로고
    • Mode of action of penicillin. Biochemical basis for the mechanism of action of penicillin and for its selective toxicity
    • Park, J.T. & Strominger, J.L. Mode of action of penicillin. Biochemical basis for the mechanism of action of penicillin and for its selective toxicity. Science 125, 99-101 (1957).
    • (1957) Science , vol.125 , pp. 99-101
    • Park, J.T.1    Strominger, J.L.2
  • 5
    • 33646169520 scopus 로고
    • Effects of penicillin on the biosynthesis of the cell walls of Escherichia coli and Staphylococcus aureus
    • Nathenson, S. & Strominger, J.L. Effects of penicillin on the biosynthesis of the cell walls of Escherichia coli and Staphylococcus aureus. J. Pharmacol. Exp. Therap. 131, 1-6 (1961).
    • (1961) J. Pharmacol. Exp. Therap , vol.131 , pp. 1-6
    • Nathenson, S.1    Strominger, J.L.2
  • 6
    • 0014371202 scopus 로고    scopus 로고
    • Strominger, J.L. Penicillin-sensitive enzymatic reactions in bacterial cell wall synthesis. in Harvey Lectures, Series 64 179-213 (Academic Press, New York, 1970).
    • Strominger, J.L. Penicillin-sensitive enzymatic reactions in bacterial cell wall synthesis. in Harvey Lectures, Series 64 179-213 (Academic Press, New York, 1970).
  • 7
    • 0013808622 scopus 로고
    • Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine
    • Tipper, D.J. & Strominger, J.L. Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc. Natl. Acad. Sci. USA 54, 1133-1141 (1965).
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 8
    • 0013887127 scopus 로고
    • Glycopeptide transpeptidase and D-alanine carboxypeptidase: Penicillin-sensitive enzymatic reactions
    • Izaki,K.,Matsuhashi,M.& Strominger J.L.Glycopeptide transpeptidase and D-alanine carboxypeptidase: Penicillin-sensitive enzymatic reactions. Proc. Natl. Acad. Sci. USA 55, 656-663 (1966).
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 656-663
    • Izaki, K.1    Matsuhashi, M.2    Strominger, J.L.3
  • 9
    • 0004865471 scopus 로고
    • On the structure at the cell wall of Staphylococcus aureus (Copenhagen)
    • Mandelstam, M.H. & Strominger, J.L. On the structure at the cell wall of Staphylococcus aureus (Copenhagen). Biochem. Res. Commun. 5, 466-476 (1961).
    • (1961) Biochem. Res. Commun , vol.5 , pp. 466-476
    • Mandelstam, M.H.1    Strominger, J.L.2
  • 10
    • 0014202386 scopus 로고
    • Mechanisms of enzymatic bacteriolysis
    • Strominger, J.L. & Ghuysen, J,-M. Mechanisms of enzymatic bacteriolysis. Science 156, 213-221 (1967).
    • (1967) Science , vol.156 , pp. 213-221
    • Strominger, J.L.1    Ghuysen, J.-M.2
  • 11
    • 33646189358 scopus 로고
    • Chemical basis for an immunological specificity of a strain of Staphylococcus aureus
    • Juergens, W.G., Sanderson, A.R. & Strominger, J.L. Chemical basis for an immunological specificity of a strain of Staphylococcus aureus. J. Exp. Ued. 117, 925-935 (1963).
    • (1963) J. Exp. Ued , vol.117 , pp. 925-935
    • Juergens, W.G.1    Sanderson, A.R.2    Strominger, J.L.3
  • 12
    • 0019771196 scopus 로고
    • Muramyl peptides. Chemical structure, biological activity and mechanism of action
    • Adam, A., Petit, j.F., Lefrancier, P. & Lederer, E. Muramyl peptides. Chemical structure, biological activity and mechanism of action. Mol Cell. Biochem. 41, 27-47 (1981).
    • (1981) Mol Cell. Biochem , vol.41 , pp. 27-47
    • Adam, A.1    Petit, J.F.2    Lefrancier, P.3    Lederer, E.4
  • 13
    • 33646204548 scopus 로고
    • Accumulation of a uridine nucleotide in Staphylococcus aureus as the consequence of lysine deprivation
    • Strominger, J.L. & Threnn, R.H. Accumulation of a uridine nucleotide in Staphylococcus aureus as the consequence of lysine deprivation. Biochim. Biophys. Acta 38, 83-92 (1959).
    • (1959) Biochim. Biophys. Acta , vol.38 , pp. 83-92
    • Strominger, J.L.1    Threnn, R.H.2
  • 14
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira, S., Uematsu, S. & Takeuchi, O. Pathogen recognition and innate immunity. Cell 124,. 783-801 (2006).
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 15
    • 36249005596 scopus 로고    scopus 로고
    • NLR proteins: Integral members of innate immunity and mediators of inflammatory diseases
    • published online 17 September
    • Wilmanski, J.M., Petnicki-Ocwieja, T. & Kobayashi, K. NLR proteins: integral members of innate immunity and mediators of inflammatory diseases. J. Leukoc. Biol. published online 17 September (2007).
    • (2007) J. Leukoc. Biol
    • Wilmanski, J.M.1    Petnicki-Ocwieja, T.2    Kobayashi, K.3
  • 16
    • 3442893287 scopus 로고    scopus 로고
    • Mini-review: The role of peptidoglycan recognition in innate immunity
    • Girardin, S.E. &,Philpott, D.J. Mini-review: The role of peptidoglycan recognition in innate immunity. Eur. J. Immunal. 34, 1777-1782 (2004).
    • (2004) Eur. J. Immunal , vol.34 , pp. 1777-1782
    • Girardin, S.E.1    Philpott, D.J.2
  • 17
    • 0001420011 scopus 로고
    • Thymidine diphosphate 4-acetamido-4,6-dideoxyhexoses. L. Enzymatic synthesis by strains of Escherichia colli
    • Matsuhashi, M. & Strominger, J.L. Thymidine diphosphate 4-acetamido-4,6-dideoxyhexoses. L. Enzymatic synthesis by strains of Escherichia colli. J. Biol.Chem. 239, 2454-2463 (1964).
    • (1964) J. Biol.Chem , vol.239 , pp. 2454-2463
    • Matsuhashi, M.1    Strominger, J.L.2
  • 18
    • 34250876388 scopus 로고    scopus 로고
    • Fitzgerald, K.A. & Golenbock, D.T. Immunology. The shape of things to come. Science 316, 1574-1576 (2007).
    • Fitzgerald, K.A. & Golenbock, D.T. Immunology. The shape of things to come. Science 316, 1574-1576 (2007).
  • 19
    • 34250854079 scopus 로고    scopus 로고
    • The vaccine adjuvant monophosphoryl lipid A as a TRIF-biased agonist of TLR4
    • Mata-Haro, V. et al. The vaccine adjuvant monophosphoryl lipid A as a TRIF-biased agonist of TLR4. Science 316, 1628-1632 (2007).
    • (2007) Science , vol.316 , pp. 1628-1632
    • Mata-Haro, V.1
  • 20
    • 34250813748 scopus 로고    scopus 로고
    • Crystal structures of human MD-2 and its corpplex with antiendotoxic lipid IVa
    • Ohto, U., Fukase, K., Miyake, K. & Satow, Y. Crystal structures of human MD-2 and its corpplex with antiendotoxic lipid IVa. Science 316 1632-1634 (2007).
    • (2007) Science , vol.316 , pp. 1632-1634
    • Ohto, U.1    Fukase, K.2    Miyake, K.3    Satow, Y.4
  • 21
    • 2542448243 scopus 로고    scopus 로고
    • CD1: Antigen presentation and T cell function
    • Brigl, M. & Brenner, M.B. CD1: Antigen presentation and T cell function. Annu. Rev. Immunol. 22,817-890 (2004)
    • (2004) Annu. Rev. Immunol , vol.22 , pp. 817-890
    • Brigl, M.1    Brenner, M.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.