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1
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0029819784
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Paneth cell defensins: Endogenous peptide components of intestinal host defense
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Ouellette AJ, Selsted ME. Paneth cell defensins: endogenous peptide components of intestinal host defense. FASEB J. 10:1996;1280-1289.
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(1996)
FASEB J
, vol.10
, pp. 1280-1289
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Ouellette, A.J.1
Selsted, M.E.2
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2
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0030832289
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Epithelial antibiotic induced in states of disease
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Stolzenberg ED, Anderson GM, Ackermann MR, Whitlock RH, Zasloff M. Epithelial antibiotic induced in states of disease. Proc Natl Acad Sci USA. 94:1997;8686-8690.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 8686-8690
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-
Stolzenberg, E.D.1
Anderson, G.M.2
Ackermann, M.R.3
Whitlock, R.H.4
Zasloff, M.5
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3
-
-
0030820726
-
A peptide antibiotic from human skin
-
of outstanding interest. The authors struck gold in shed psoriatic skin; they isolated a new human β-defensin that resembles the bovine epithelial defensins in its structure and inducibility by microbial and inflammatory stimuli.
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Harder J, Bartels J, Christophers E, Schroeder J-M. A peptide antibiotic from human skin. of outstanding interest Nature. 387:1997;861-862 The authors struck gold in shed psoriatic skin; they isolated a new human β-defensin that resembles the bovine epithelial defensins in its structure and inducibility by microbial and inflammatory stimuli.
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(1997)
Nature
, vol.387
, pp. 861-862
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Harder, J.1
Bartels, J.2
Christophers, E.3
Schroeder J-M4
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4
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0031046654
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Antimicrobial peptides of leukocytes
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Ganz T, Lehrer RI. Antimicrobial peptides of leukocytes. Curr Opin Hematol. 4:1997;53-58.
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(1997)
Curr Opin Hematol
, vol.4
, pp. 53-58
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Ganz, T.1
Lehrer, R.I.2
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5
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0030012702
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Antibiotic proteins of polymorphonuclear leukocytes
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Levy O. Antibiotic proteins of polymorphonuclear leukocytes. Eur J Haematol. 56:1996;263-277.
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(1996)
Eur J Haematol
, vol.56
, pp. 263-277
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Levy, O.1
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6
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0030029451
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Human enteric defensins. Gene structure and developmental expression
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Mallow EB, Harris A, Salzman N, Russell JP, DeBerardinis RJ, Ruchelli E, Bevins CL. Human enteric defensins. Gene structure and developmental expression. J Biol Chem. 271:1996;4038-4045.
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(1996)
J Biol Chem
, vol.271
, pp. 4038-4045
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-
Mallow, E.B.1
Harris, A.2
Salzman, N.3
Russell, J.P.4
Deberardinis, R.J.5
Ruchelli, E.6
Bevins, C.L.7
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7
-
-
10544223740
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Secretion of type II phospholipase A2 and cryptdin by rat small intestinal Paneth cells
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of special interest. This paper employs a model system consisting of exteriorized luminally perfused rat intestinal segment with preserved blood supply. The preparation was stimulated by an intravenous cholinergic agent or luminal lipopolysaccharide, and perfusate was assayed for secreted antimicrobial proteins. Among the nine antimicrobial molecules detected, a defensin, lysozyme and phospholipase A2 were identified. This paper is notable for connecting antimicrobial peptide release to physiological events in the small intestine.
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Qu XD, Lloyd KC, Walsh JH, Lehrer RI. Secretion of type II phospholipase A2 and cryptdin by rat small intestinal Paneth cells. of special interest Infect Immun. 64:1996;5161-5165 This paper employs a model system consisting of exteriorized luminally perfused rat intestinal segment with preserved blood supply. The preparation was stimulated by an intravenous cholinergic agent or luminal lipopolysaccharide, and perfusate was assayed for secreted antimicrobial proteins. Among the nine antimicrobial molecules detected, a defensin, lysozyme and phospholipase A2 were identified. This paper is notable for connecting antimicrobial peptide release to physiological events in the small intestine.
-
(1996)
Infect Immun
, vol.64
, pp. 5161-5165
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Qu, X.D.1
Lloyd, K.C.2
Walsh, J.H.3
Lehrer, R.I.4
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8
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0029738094
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Positional specificity of defensin gene expression reveals Paneth cell heterogeneity in mouse small intestine
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Darmoul D, Ouellette AJ. Positional specificity of defensin gene expression reveals Paneth cell heterogeneity in mouse small intestine. Am J Physiol. 271:1996;G68-74.
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(1996)
Am J Physiol
, vol.271
, pp. 68-74
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Darmoul, D.1
Ouellette, A.J.2
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9
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0030739939
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Induction of epithelial chloride secretion by channel-forming cryptdins 2 and 3
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Lencer WI, Cheung G, Strohmeier GR, Currie MG, Oullette AJ, Selsted ME, Madara JL. Induction of epithelial chloride secretion by channel-forming cryptdins 2 and 3. Proc Natl Acad Sci USA. 94:1997;8585-8589.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 8585-8589
-
-
Lencer, W.I.1
Cheung, G.2
Strohmeier, G.R.3
Currie, M.G.4
Oullette, A.J.5
Selsted, M.E.6
Madara, J.L.7
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10
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0030914439
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Localization of human intestinal defensin 5 in Paneth cell granules
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Porter EM, Liu L, Oren A, Anton PA, Ganz T. Localization of human intestinal defensin 5 in Paneth cell granules. Infect Immunity. 65:1997;2389-2395.
-
(1997)
Infect Immunity
, vol.65
, pp. 2389-2395
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-
Porter, E.M.1
Liu, L.2
Oren, A.3
Anton, P.A.4
Ganz, T.5
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11
-
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0030913746
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Broad-spectrum antimicrobial activity of human intestinal defensin 5
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Porter EM, Van Dam E, Valore EV, Ganz T. Broad-spectrum antimicrobial activity of human intestinal defensin 5. Infect Immunity. 65:1997;2396-2401.
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(1997)
Infect Immunity
, vol.65
, pp. 2396-2401
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-
Porter, E.M.1
Van Dam, E.2
Valore, E.V.3
Ganz, T.4
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12
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0030463948
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Production of active bovine tracheal antimicrobial peptide in milk of transgenic mice
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Yarus S, Rosen JM, Cole AM, Diamond G. Production of active bovine tracheal antimicrobial peptide in milk of transgenic mice. Proc Natl Acad Sci USA. 93:1996;14118-14121.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 14118-14121
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Yarus, S.1
Rosen, J.M.2
Cole, A.M.3
Diamond, G.4
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13
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0029900207
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Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells
-
of outstanding interest. This paper, together with [14], explores the mechanism of transcriptional regulation of the bovine epithelial β-defensins by lipopolysaccharide (LPS) and TNF-α. The LPS receptor CD14 was found on epithelial cells and its blockade by monoclonal antibody inhibited the induction of TAP (transporter associated with antigen processing) mRNA by lipopolysaccharide. The responsiveness of the epithelial defensin genes to microbial and inflammatory stimuli constitutes strong support for its role in host defense.
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Diamond G, Russell JP, Bevins CL. Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells. of outstanding interest Proc Natl Acad Sci USA. 93:1996;5156-5160 This paper, together with [14], explores the mechanism of transcriptional regulation of the bovine epithelial β-defensins by lipopolysaccharide (LPS) and TNF-α. The LPS receptor CD14 was found on epithelial cells and its blockade by monoclonal antibody inhibited the induction of TAP (transporter associated with antigen processing) mRNA by lipopolysaccharide. The responsiveness of the epithelial defensin genes to microbial and inflammatory stimuli constitutes strong support for its role in host defense.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 5156-5160
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Diamond, G.1
Russell, J.P.2
Bevins, C.L.3
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14
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0029877550
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Coordinate induction of two antibiotic genes in tracheal epithelial cells exposed to the inflammatory mediators lipopolysaccharide and tumor necrosis factor alpha
-
of outstanding interest. This paper, together with [13], explores the mechanism of transcriptional regulation of the bovine epithelial β-defensins by lipopolysaccharide (LPS) and TNF-α. The LPS receptor CD14 was found on epithelial cells and its blockade by monoclonal antibody inhibited the induction of TAP (transporter associated with antigen processing) mRNA by lipopolysaccharide. The responsiveness of the epithelial defensin genes to microbial and inflammatory stimuli constitutes strong support for its role in host defense.
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Russell JP, Diamond G, Tarver AP, Scanlin TF, Bevins CL. Coordinate induction of two antibiotic genes in tracheal epithelial cells exposed to the inflammatory mediators lipopolysaccharide and tumor necrosis factor alpha. of outstanding interest Infect Immun. 64:1996;1565-1568 This paper, together with [13], explores the mechanism of transcriptional regulation of the bovine epithelial β-defensins by lipopolysaccharide (LPS) and TNF-α. The LPS receptor CD14 was found on epithelial cells and its blockade by monoclonal antibody inhibited the induction of TAP (transporter associated with antigen processing) mRNA by lipopolysaccharide. The responsiveness of the epithelial defensin genes to microbial and inflammatory stimuli constitutes strong support for its role in host defense.
-
(1996)
Infect Immun
, vol.64
, pp. 1565-1568
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Russell, J.P.1
Diamond, G.2
Tarver, A.P.3
Scanlin, T.F.4
Bevins, C.L.5
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15
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0030569343
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Widespread expression of beta-defensin HBD-1 in human secretory glands and epithelial cells
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Zhao CQ, Wang I, Lehrer RI. Widespread expression of beta-defensin HBD-1 in human secretory glands and epithelial cells. FEBS Lett. 396:1996;319-322.
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(1996)
FEBS Lett
, vol.396
, pp. 319-322
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-
Zhao, C.Q.1
Wang, I.2
Lehrer, R.I.3
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16
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0031213832
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The human β-defensin-1 and α-defensins are encoded by adjacent genes: Two peptide families with differing disulfide topology share a common ancestry
-
of special interest. The genomic and mRNA sequences of the two defensin families were so divergent that their ancestral connection was in serious doubt. The common ancestry of the two families is now firmly established by the adjacent location of the genes encoding α- and β-defensins in humans.
-
Liu L, Zhao C, Heng HHQ, Ganz T. The human β-defensin-1 and α-defensins are encoded by adjacent genes: two peptide families with differing disulfide topology share a common ancestry. of special interest Genomics. 43:1997;316-320 The genomic and mRNA sequences of the two defensin families were so divergent that their ancestral connection was in serious doubt. The common ancestry of the two families is now firmly established by the adjacent location of the genes encoding α- and β-defensins in humans.
-
(1997)
Genomics
, vol.43
, pp. 316-320
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-
Liu, L.1
Zhao, C.2
Heng, H.H.Q.3
Ganz, T.4
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17
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0029870085
-
Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid
-
of outstanding interest. This pioneering study presents evidence that respiratory epithelia generate soluble and stable antimicrobial activity that is inhibited by the abnormally high salinity of the secretions in CF patients. The reported properties of the active substance(s) were reminiscent of salt-inhibited cationic peptides such as defensins.
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Smith JJ, Travis SM, Greenberg EP, Welsh MJ. Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid. of outstanding interest Cell. 85:1996;229-236 This pioneering study presents evidence that respiratory epithelia generate soluble and stable antimicrobial activity that is inhibited by the abnormally high salinity of the secretions in CF patients. The reported properties of the active substance(s) were reminiscent of salt-inhibited cationic peptides such as defensins.
-
(1996)
Cell
, vol.85
, pp. 229-236
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Smith, J.J.1
Travis, S.M.2
Greenberg, E.P.3
Welsh, M.J.4
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18
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0030949875
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Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
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of special interest. A technically complex series of studies in human respiratory epithelia implanted into nude mice points to HBD-1 as a critically important component of the antimicrobial activity that is inactivated in cystic fibrosis.
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Goldman M, Anderson G, Stolzenberg ED, Kari UP, Zasloff M, Wilson JM. Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. of special interest Cell. 88:1997;553-560 A technically complex series of studies in human respiratory epithelia implanted into nude mice points to HBD-1 as a critically important component of the antimicrobial activity that is inactivated in cystic fibrosis.
-
(1997)
Cell
, vol.88
, pp. 553-560
-
-
Goldman, M.1
Anderson, G.2
Stolzenberg, E.D.3
Kari, U.P.4
Zasloff, M.5
Wilson, J.M.6
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19
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0030942221
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Purification and characterization of defensins from cystic fibrosis sputum
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of special interest. The potentially complex role of defensins in the pathogenesis of CF is pointed out by the very high concentrations of neutrophil defensins in CF sputum. Whereas epithelial defensins may be protective in early disease, neutrophil defensins could contribute to tissue injury in advanced disease.
-
Soong LB, Ganz T, Ellison A, Caughey GH. Purification and characterization of defensins from cystic fibrosis sputum. of special interest Inflamm Res. 46:1997;98-102 The potentially complex role of defensins in the pathogenesis of CF is pointed out by the very high concentrations of neutrophil defensins in CF sputum. Whereas epithelial defensins may be protective in early disease, neutrophil defensins could contribute to tissue injury in advanced disease.
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(1997)
Inflamm Res
, vol.46
, pp. 98-102
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-
Soong, L.B.1
Ganz, T.2
Ellison, A.3
Caughey, G.H.4
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20
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0030038197
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Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils
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Chertov O, Michiel DF, Xu L, Wang JM, Tani K, Murphy WJ, Longo DL, Taub DD, Oppenheim JJ. Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils. J Biol Chem. 271:1996;2935-2940.
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(1996)
J Biol Chem
, vol.271
, pp. 2935-2940
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-
Chertov, O.1
Michiel, D.F.2
Xu, L.3
Wang, J.M.4
Tani, K.5
Murphy, W.J.6
Longo, D.L.7
Taub, D.D.8
Oppenheim, J.J.9
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21
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0029892845
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Defensin modulates tissue-type plasminogen activator and plasminogen binding to fibrin and endothelial cells
-
of special interest. This paper, together with [22], explores the idea that defensins are among the inflammatory molecules that may initiate or accelerate atherosclerosis and, by inhibiting fibrinolysis, promote its thrombotic complications.
-
Higazi AAR, Ganz T, Kariko K, Cines DB. Defensin modulates tissue-type plasminogen activator and plasminogen binding to fibrin and endothelial cells. of special interest J Biol Chem. 271:1996;17650-17655 This paper, together with [22], explores the idea that defensins are among the inflammatory molecules that may initiate or accelerate atherosclerosis and, by inhibiting fibrinolysis, promote its thrombotic complications.
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(1996)
J Biol Chem
, vol.271
, pp. 17650-17655
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-
Higazi, A.A.R.1
Ganz, T.2
Kariko, K.3
Cines, D.B.4
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22
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0031052346
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Immunohistochemical localization of defensin in human coronary vessels
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of special interest. This paper, together with [21], explores the idea that defensins are among the inflammatory molecules that may initiate or accelerate atherosclerosis and, by inhibiting fibrinolysis, promote its thrombotic complications.
-
Barnathan ES, Raghunath PN, Tomaszewski JE, Ganz T, Cines DB, Higazi AA. Immunohistochemical localization of defensin in human coronary vessels. of special interest Am J Pathol. 150:1997;1009-1020 This paper, together with [21], explores the idea that defensins are among the inflammatory molecules that may initiate or accelerate atherosclerosis and, by inhibiting fibrinolysis, promote its thrombotic complications.
-
(1997)
Am J Pathol
, vol.150
, pp. 1009-1020
-
-
Barnathan, E.S.1
Raghunath, P.N.2
Tomaszewski, J.E.3
Ganz, T.4
Cines, D.B.5
Higazi, A.A.6
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23
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15844422471
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The isolation and characterization of a novel corticostatin/defensin-like peptide from the kidney
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Bateman A, MacLeod RJ, Lembessis P, Hu J, Esch F, Solomon S. The isolation and characterization of a novel corticostatin/defensin-like peptide from the kidney. J Biol Chem. 271:1996;10654-10659.
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(1996)
J Biol Chem
, vol.271
, pp. 10654-10659
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Bateman, A.1
MacLeod, R.J.2
Lembessis, P.3
Hu, J.4
Esch, F.5
Solomon, S.6
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24
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0030057777
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Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides
-
of special interest. The first structural study of bovine cathelicidin precursors revealed structural similarity to the cystatin domains of thiol protease inhibitors but only very weak inhibitory activity towards the thiol protease cathepsin L. The function of the ~100 amino acid cathelin domain in cathelicidins remains unknown.
-
Storici P, Tossi A, Lenarcic B, Romeo D. Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides. of special interest Eur J Biochem. 238:1996;769-776 The first structural study of bovine cathelicidin precursors revealed structural similarity to the cystatin domains of thiol protease inhibitors but only very weak inhibitory activity towards the thiol protease cathepsin L. The function of the ~100 amino acid cathelin domain in cathelicidins remains unknown.
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(1996)
Eur J Biochem
, vol.238
, pp. 769-776
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Storici, P.1
Tossi, A.2
Lenarcic, B.3
Romeo, D.4
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25
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0031028188
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Porcine polymorphonuclear leukocytes generate extracellular microbicidal activity by elastase-mediated activation of secreted proprotegrins
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of special interest. Most cathelicidins contain neutrophil elastase consensus cleavage sites. This paper documents that very small amounts of neutrophil elastase are sufficient to cleave and activate secreted cathelicidin precursors to active microbicidal peptides.
-
Panyutich A, Shi J, Boutz PL, Zhao C, Ganz T. Porcine polymorphonuclear leukocytes generate extracellular microbicidal activity by elastase-mediated activation of secreted proprotegrins. of special interest Infect Immun. 65:1997;978-985 Most cathelicidins contain neutrophil elastase consensus cleavage sites. This paper documents that very small amounts of neutrophil elastase are sufficient to cleave and activate secreted cathelicidin precursors to active microbicidal peptides.
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(1997)
Infect Immun
, vol.65
, pp. 978-985
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Panyutich, A.1
Shi, J.2
Boutz, P.L.3
Zhao, C.4
Ganz, T.5
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26
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0029893253
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The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
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Gudmundsson GH, Agerberth B, Odeberg J, Bergman T, Olsson B, Salcedo R. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur J Biochem. 238:1996;325-332.
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(1996)
Eur J Biochem
, vol.238
, pp. 325-332
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Gudmundsson, G.H.1
Agerberth, B.2
Odeberg, J.3
Bergman, T.4
Olsson, B.5
Salcedo, R.6
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27
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0030956070
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The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders
-
of outstanding interest. This is the first well-documented instance of the induction of cathelicidin genes by inflammatory stimuli in epithelia. It now appears that the synthesis of many vertebrate antimicrobial peptides, like that of their insect counterparts, is induced by microbial infection or the consequent cytokine release.
-
Frohm M, Agerberth B, Ahangari G, Stahle-Backdahl M, Liden S, Wigzell H, Gudmundsson GH. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. of outstanding interest J Biol Chem. 272:1997;15258-15263 This is the first well-documented instance of the induction of cathelicidin genes by inflammatory stimuli in epithelia. It now appears that the synthesis of many vertebrate antimicrobial peptides, like that of their insect counterparts, is induced by microbial infection or the consequent cytokine release.
-
(1997)
J Biol Chem
, vol.272
, pp. 15258-15263
-
-
Frohm, M.1
Agerberth, B.2
Ahangari, G.3
Stahle-Backdahl, M.4
Liden, S.5
Wigzell, H.6
Gudmundsson, G.H.7
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28
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0029664907
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PR-39, a proline-rich antibacterial peptide that inhibits phagocyte NADPH oxidase activity by binding to Src homology 3 domains of p47 phox
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Shi J, Ross CR, Leto TL, Blecha F. PR-39, a proline-rich antibacterial peptide that inhibits phagocyte NADPH oxidase activity by binding to Src homology 3 domains of p47 phox. Proc Natl Acad Sci USA. 93:1996;6014-6018.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 6014-6018
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Shi, J.1
Ross, C.R.2
Leto, T.L.3
Blecha, F.4
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29
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9444225012
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Mode of action of the antimicrobial peptide indolicidin
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Falla TJ, Karunaratne DN, Hancock REW. Mode of action of the antimicrobial peptide indolicidin. J Biol Chem. 271:1996;19298-19303.
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(1996)
J Biol Chem
, vol.271
, pp. 19298-19303
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Falla, T.J.1
Karunaratne, D.N.2
Hancock, R.E.W.3
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30
-
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0031022395
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Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids
-
Ladokhin AS, Selsted ME, White SH. Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids. Biophys J. 72:1997;794-805.
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(1997)
Biophys J
, vol.72
, pp. 794-805
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Ladokhin, A.S.1
Selsted, M.E.2
White, S.H.3
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31
-
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0029886161
-
Synthesis and solution structure of the antimicrobial peptide protegrin-1
-
Aumelas A, Mangoni M, Roumestand C, Chiche L, Despaux E, Grassy G, Calas B, Chavanieu A. Synthesis and solution structure of the antimicrobial peptide protegrin-1. Eur J Biochem. 237:1996;575-583.
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(1996)
Eur J Biochem
, vol.237
, pp. 575-583
-
-
Aumelas, A.1
Mangoni, M.2
Roumestand, C.3
Chiche, L.4
Despaux, E.5
Grassy, G.6
Calas, B.7
Chavanieu, A.8
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32
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0030198873
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Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes
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Fahrner RI, Dieckmann T, Harwig SS, Lehrer RI, Eisenberg D, Feigon J. Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes. Chem Biol. 3:1996;543-550.
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(1996)
Chem Biol
, vol.3
, pp. 543-550
-
-
Fahrner, R.I.1
Dieckmann, T.2
Harwig, S.S.3
Lehrer, R.I.4
Eisenberg, D.5
Feigon, J.6
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33
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0031033223
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P15s (15-kD antimicrobial proteins) are stored in the secondary granules of rabbit granulocytes: Implications for antibacterial synergy with the bactericidal/permeability-increasing protein in inflammatory fluids
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Zarember K, Elsbach P, Shin-Kim K, Weiss J. p15s (15-kD antimicrobial proteins) are stored in the secondary granules of rabbit granulocytes: implications for antibacterial synergy with the bactericidal/permeability-increasing protein in inflammatory fluids. Blood. 89:1997;672-679.
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(1997)
Blood
, vol.89
, pp. 672-679
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Zarember, K.1
Elsbach, P.2
Shin-Kim, K.3
Weiss, J.4
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34
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0031009432
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Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse
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Gallo RL, Kim KJ, Bernfield M, Kozak CA, Zanetti M, Merluzzi L, Gennaro R. Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse. J Biol Chem. 272:1997;13088-13093.
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(1997)
J Biol Chem
, vol.272
, pp. 13088-13093
-
-
Gallo, R.L.1
Kim, K.J.2
Bernfield, M.3
Kozak, C.A.4
Zanetti, M.5
Merluzzi, L.6
Gennaro, R.7
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35
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0030570714
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A novel murine cathelin-like protein expressed in bone marrow
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Popsueva AE, Zinovjeva MV, Visser JW, Zijlmans JM, Fibbe WE, Belyavsky AV. A novel murine cathelin-like protein expressed in bone marrow. FEBS Lett. 391:1996;5-8.
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(1996)
FEBS Lett
, vol.391
, pp. 5-8
-
-
Popsueva, A.E.1
Zinovjeva, M.V.2
Visser, J.W.3
Zijlmans, J.M.4
Fibbe, W.E.5
Belyavsky, A.V.6
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36
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0029924103
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Change in membrane permeability induced by protegrin 1: Implication of disulphide bridges for pore formation
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Mangoni ME, Aumelas A, Charnet P, Roumestand C, Chiche L, Despaux E, Grassy G, Calas B, Chavanieu A. Change in membrane permeability induced by protegrin 1: implication of disulphide bridges for pore formation. FEBS Lett. 383:1996;93-98.
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(1996)
FEBS Lett
, vol.383
, pp. 93-98
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-
Mangoni, M.E.1
Aumelas, A.2
Charnet, P.3
Roumestand, C.4
Chiche, L.5
Despaux, E.6
Grassy, G.7
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