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Contents |
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192 a.a.
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45 a.a.
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103 a.a.
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* Residue conservation analysis
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PDB id:
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Toxin
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Title:
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Cholera toxin
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Structure:
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Cholera toxin. Chain: a. Synonym: ctx, choleragen. Cholera toxin. Chain: c. Synonym: ctx, choleragen. Cholera toxin. Chain: d, e, f, g, h. Synonym: ctx, choleragen
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Source:
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Vibrio cholerae. Organism_taxid: 44104. Strain: 569b. Other_details: commercially obtained from list biological laboratory, campber ca95008. Laboratory, campber ca95008
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Biol. unit:
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Heptamer (from
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Resolution:
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Authors:
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R.-G.Zhang,E.Westbrook
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Key ref:
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R.G.Zhang
et al.
(1995).
The three-dimensional crystal structure of cholera toxin.
J Mol Biol,
251,
563-573.
PubMed id:
DOI:
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Date:
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10-Jan-96
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Release date:
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01-Aug-96
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PROCHECK
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Headers
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References
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P01555
(CHTA_VIBCH) -
Cholera enterotoxin subunit A from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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Seq:
Struc:
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258 a.a.
192 a.a.*
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DOI no:
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J Mol Biol
251:563-573
(1995)
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PubMed id:
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The three-dimensional crystal structure of cholera toxin.
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R.G.Zhang,
D.L.Scott,
M.L.Westbrook,
S.Nance,
B.D.Spangler,
G.G.Shipley,
E.M.Westbrook.
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ABSTRACT
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The clinical manifestations of cholera are largely attributable to the actions
of a secreted hexameric AB5 enterotoxin (choleragen). We have independently
solved and refined the three-dimensional structure of choleragen at 2.5 A
resolution. The structure of the crystalline toxin closely resembles that
described for the heat-labile enterotoxin from Escherichia coli (LT) with which
it shares 80% sequence homology. In both cases, the wedge-shaped A subunit is
loosely held high above the plane of the pentameric B subunits by the tethering
A2 chain. The most striking difference between the two toxins occurs at the
carboxyl terminus of the A2 chain. Whereas the last 14 residues of the A2 chain
of LT threading through the central pore of the B5 assembly form an extended
chain with a terminal loop, the A2 chain of choleragen remains a nearly
continuous alpha-helix throughout its length. The four carboxyl-terminal
residues of the A2 chain (KDEL sequence), disordered in the crystal structure of
LT, are clearly visible in choleragen's electron-density map. In the
accompanying article we describe the three-dimensional structure of the isolated
B pentamer of cholera toxin (choleragenoid). Comparison of the crystalline
coordinates of choleragen, choleragenoid, and LT provides a solid
three-dimensional foundation for further experimental investigation. These
structures, along with those of related toxins from Shigella dysenteria and
Bordetella pertussis, offer a first step towards the rational design of new
vaccines and anti-microbial agents.
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Selected figure(s)
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Figure 3.
Figure 3. Representative electron-density for cholera toxin. Stereo view of the 2Fo--Fc electron-density map at the junction
between the A subunit and the B pentamer. The long A2 a-helix (orange) can be seen as it begins its descent into the
central pore. Residues belonging to the A1 chain or to the B pentamer are indicated (Pro120 and Ala(4)75, respectively).
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Figure 9.
Figure 9. Cross-section through the central ``channel'' of choleragen. The A1 chain, A2 chain, and the B subunits are
colored cyan, gold, and lavender, respectively. Side-chains contributing to the A2/B interface are shaded according to
charge potential: green, non-polar; red, negatively charged; blue, positively charged. The Trp88 of opposed B subunits
are shown to assist with orientation. Yellow spheres represent well-resolved water molecules. TheA2/B interface is initially
quite non-polar but becomes quite polar deeper in the channel. The carboxyl terminus of the A2 chain presumably interacts
with the surface of the membrane during GM1 binding. The sequence of the terminal four residues (KDEL) is identical
to that shown to act as endoplasmic retention signal (Lewis & Pelham, 1990; Joseph et al., 1978, 1979).
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1995,
251,
563-573)
copyright 1995.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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E.B.Watkins,
C.E.Miller,
J.Majewski,
and
T.L.Kuhl
(2011).
Membrane texture induced by specific protein binding and receptor clustering: active roles for lipids in cellular function.
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Proc Natl Acad Sci U S A,
108,
6975-6980.
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D.E.Saslowsky,
J.A.Cho,
H.Chinnapen,
R.H.Massol,
D.J.Chinnapen,
J.S.Wagner,
H.E.De Luca,
W.Kam,
B.H.Paw,
and
W.I.Lencer
(2010).
Intoxication of zebrafish and mammalian cells by cholera toxin depends on the flotillin/reggie proteins but not Derlin-1 or -2.
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J Clin Invest,
120,
4399-4409.
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J.Zrimi,
A.Ng Ling,
E.Giri-Rachman Arifin,
G.Feverati,
and
C.Lesieur
(2010).
Cholera toxin B subunits assemble into pentamers--proposition of a fly-casting mechanism.
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PLoS One,
5,
e15347.
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S.Ramasamy,
C.Q.Liu,
H.Tran,
A.Gubala,
P.Gauci,
J.McAllister,
and
T.Vo
(2010).
Principles of antidote pharmacology: an update on prophylaxis, post-exposure treatment recommendations and research initiatives for biological agents.
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Br J Pharmacol,
161,
721-748.
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M.L.Forster,
J.J.Mahn,
and
B.Tsai
(2009).
Generating an Unfoldase from Thioredoxin-like Domains.
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J Biol Chem,
284,
13045-13056.
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C.E.Miller,
J.Majewski,
E.B.Watkins,
and
T.L.Kuhl
(2008).
Part I: an x-ray scattering study of cholera toxin penetration and induced phase transformations in lipid membranes.
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Biophys J,
95,
629-640.
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G.Zhang
(2008).
Design, synthesis, and evaluation of bisubstrate analog inhibitors of cholera toxin.
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Bioorg Med Chem Lett,
18,
3724-3727.
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J.Baysarowich,
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and
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Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr.
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Proc Natl Acad Sci U S A,
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PDB code:
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M.K.Sharma,
N.K.Singh,
D.Jani,
R.Sisodia,
M.Thungapathra,
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Expression of toxin co-regulated pilus subunit A (TCPA) of Vibrio cholerae and its immunogenic epitopes fused to cholera toxin B subunit in transgenic tomato (Solanum lycopersicum).
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Plant Cell Rep,
27,
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Mol Biotechnol,
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R.S.Ampapathi,
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Order-disorder-order transitions mediate the activation of cholera toxin.
|
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J Mol Biol,
377,
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A.H.Pande,
P.Scaglione,
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K.N.Nemec,
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R.K.Holmes,
S.A.Tatulian,
and
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Conformational instability of the cholera toxin A1 polypeptide.
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J Mol Biol,
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J.Kato,
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Enhanced sensitivity to cholera toxin in ADP-ribosylarginine hydrolase-deficient mice.
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Mol Cell Biol,
27,
5534-5543.
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P.Scheerer,
A.Kramer,
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Structure of an anti-cholera toxin antibody Fab in complex with an epitope-derived D-peptide: a case of polyspecific recognition.
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J Mol Recognit,
20,
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PDB code:
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S.Sakaguchi,
and
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Recent developments in mucosal vaccines against prion diseases.
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Expert Rev Vaccines,
6,
821-834.
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T.Shimizu,
S.Kawakami,
T.Sato,
T.Sasaki,
M.Higashide,
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and
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The serine 31 residue of the B subunit of Shiga toxin 2 is essential for secretion in enterohemorrhagic Escherichia coli.
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Infect Immun,
75,
2189-2200.
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A.R.Morrison,
J.Moss,
L.A.Stevens,
J.E.Evans,
C.Farrell,
E.Merithew,
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D.L.Greiner,
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A.A.Rossini,
and
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ART2, a T cell surface mono-ADP-ribosyltransferase, generates extracellular poly(ADP-ribose).
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J Biol Chem,
281,
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D.R.Hill,
L.Ford,
and
D.G.Lalloo
(2006).
Oral cholera vaccines: use in clinical practice.
|
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Lancet Infect Dis,
6,
361-373.
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D.C.Smith,
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K.R.Jennings,
L.M.Roberts,
and
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(2006).
Gas phase characterization of the noncovalent quaternary structure of cholera toxin and the cholera toxin B subunit pentamer.
|
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Biophys J,
90,
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K.P.Holbourn,
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and
K.R.Acharya
(2006).
A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins.
|
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FEBS J,
273,
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D.Sentz,
and
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(2006).
The cholera toxin A1(3) subdomain is essential for interaction with ADP-ribosylation factor 6 and full toxic activity but is not required for translocation from the endoplasmic reticulum to the cytosol.
|
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Infect Immun,
74,
2259-2267.
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J.Mueller-Dieckmann,
M.S.Weiss,
and
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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase.
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C.J.O'Neal,
M.G.Jobling,
R.K.Holmes,
and
W.G.Hol
(2005).
Structural basis for the activation of cholera toxin by human ARF6-GTP.
|
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Science,
309,
1093-1096.
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PDB codes:
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R.S.Blumberg,
R.S.Pitman,
C.T.Taylor,
and
S.P.Colgan
(2005).
Cholera toxin potentiates influences of IFN-gamma through activation of NF-kappaB and release of tumor necrosis factor-alpha.
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J Interferon Cytokine Res,
25,
209-219.
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H.Sugawa,
A.Komesu,
M.Tadano,
and
T.Arakawa
(2005).
Heteropentameric cholera toxin B subunit chimeric molecules genetically fused to a vaccine antigen induce systemic and mucosal immune responses: a potential new strategy to target recombinant vaccine antigens to mucosal immune systems.
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Infect Immun,
73,
5654-5665.
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J.Majewski,
R.Faller,
S.Satija,
and
T.L.Kuhl
(2004).
Cholera toxin assault on lipid monolayers containing ganglioside GM1.
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Biophys J,
86,
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L.H.Coye,
and
C.M.Collins
(2004).
Identification of SpyA, a novel ADP-ribosyltransferase of Streptococcus pyogenes.
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Mol Microbiol,
54,
89-98.
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C.Bourgeois,
I.Okazaki,
E.Cavanaugh,
M.Nightingale,
and
J.Moss
(2003).
Identification of regulatory domains in ADP-ribosyltransferase-1 that determine transferase and NAD glycohydrolase activities.
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J Biol Chem,
278,
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F.Biet,
L.Kremer,
I.Wolowczuk,
M.Delacre,
and
C.Locht
(2003).
Immune response induced by recombinant Mycobacterium bovis BCG producing the cholera toxin B subunit.
|
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Infect Immun,
71,
2933-2937.
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J.K.Tinker,
J.L.Erbe,
W.G.Hol,
and
R.K.Holmes
(2003).
Cholera holotoxin assembly requires a hydrophobic domain at the A-B5 interface: mutational analysis and development of an in vitro assembly system.
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Infect Immun,
71,
4093-4101.
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Y.Fujinaga,
A.A.Wolf,
C.Rodighiero,
H.Wheeler,
B.Tsai,
L.Allen,
M.G.Jobling,
T.Rapoport,
R.K.Holmes,
and
W.I.Lencer
(2003).
Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulm.
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Mol Biol Cell,
14,
4783-4793.
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M.J.Cliff,
R.Carter,
R.F.James,
A.R.Clarke,
and
T.R.Hirst
(2002).
A kinetic model of intermediate formation during assembly of cholera toxin B-subunit pentamers.
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J Biol Chem,
277,
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G.Wallerström,
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J.Angström,
and
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(2002).
Detoxification of cholera toxin without removal of its immunoadjuvanticity by the addition of (STa-related) peptides to the catalytic subunit. A potential new strategy to generate immunostimulants for vaccination.
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J Biol Chem,
277,
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(2002).
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(1999).
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|
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J Biol Chem,
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|
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PDB codes:
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|
S.M.Kavic,
E.J.Frehm,
and
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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