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Antifungal protein
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PDB id
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1du5
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Contents |
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biological process
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killing of cells of other organism
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5 terms
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DOI no:
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Nat Struct Biol
3:19-23
(1996)
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PubMed id:
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The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family.
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M.A.Batalia,
A.F.Monzingo,
S.Ernst,
W.Roberts,
J.D.Robertus.
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ABSTRACT
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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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B.Petre,
I.Major,
N.Rouhier,
and
S.Duplessis
(2011).
Genome-wide analysis of eukaryote thaumatin-like proteins (TLPs) with an emphasis on poplar.
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BMC Plant Biol, 11,
33.
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Q.Wang,
F.Li,
X.Zhang,
Y.Zhang,
Y.Hou,
S.Zhang,
and
Z.Wu
(2011).
Purification and Characterization of a CkTLP Protein from Cynanchum komarovii Seeds that Confers Antifungal Activity.
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PLoS One, 6,
e16930.
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X.Ren,
Q.Kong,
P.Wang,
F.Jiang,
H.Wang,
T.Yu,
and
X.Zheng
(2011).
Molecular cloning of a PR-5 like protein gene from cherry tomato and analysis of the response of this gene to abiotic stresses.
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Mol Biol Rep, 38,
801-807.
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J.J.Liu,
A.Zamani,
and
A.K.Ekramoddoullah
(2010).
Expression profiling of a complex thaumatin-like protein family in western white pine.
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Planta, 231,
637-651.
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J.J.Liu,
R.Sturrock,
and
A.K.Ekramoddoullah
(2010).
The superfamily of thaumatin-like proteins: its origin, evolution, and expression towards biological function.
|
| |
Plant Cell Rep, 29,
419-436.
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J.P.Zhao,
and
X.H.Su
(2010).
Patterns of molecular evolution and predicted function in thaumatin-like proteins of Populus trichocarpa.
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Planta, 232,
949-962.
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N.J.Dafoe,
B.E.Gowen,
and
C.P.Constabel
(2010).
Thaumatin-like proteins are differentially expressed and localized in phloem tissues of hybrid poplar.
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BMC Plant Biol, 10,
191.
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X.Wang,
C.Tang,
L.Deng,
G.Cai,
X.Liu,
B.Liu,
Q.Han,
H.Buchenauer,
G.Wei,
D.Han,
L.Huang,
and
Z.Kang
(2010).
Characterization of a pathogenesis-related thaumatin-like protein gene TaPR5 from wheat induced by stripe rust fungus.
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Physiol Plant, 139,
27-38.
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F.Perri,
F.Romitelli,
F.Rufini,
F.Secundo,
E.Di Stasio,
B.Giardina,
and
A.Vitali
(2008).
Different structural behaviors evidenced in thaumatin-like proteins: a spectroscopic study.
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| |
Protein J, 27,
13-20.
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R.Ghosh,
and
C.Chakrabarti
(2008).
Crystal structure analysis of NP24-I: a thaumatin-like protein.
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Planta, 228,
883-890.
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PDB code:
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H.C.Fuchs,
B.Bohle,
Y.Dall'Antonia,
C.Radauer,
K.Hoffmann-Sommergruber,
A.Mari,
O.Scheiner,
W.Keller,
and
H.Breiteneder
(2006).
Natural and recombinant molecules of the cherry allergen Pru av 2 show diverse structural and B cell characteristics but similar T cell reactivity.
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Clin Exp Allergy, 36,
359-368.
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R.G.Shatters,
L.M.Boykin,
S.L.Lapointe,
W.B.Hunter,
and
A.A.Weathersbee
(2006).
Phylogenetic and structural relationships of the PR5 gene family reveal an ancient multigene family conserved in plants and select animal taxa.
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J Mol Evol, 63,
12-29.
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K.S.de Felipe,
S.Pampou,
O.S.Jovanovic,
C.D.Pericone,
S.F.Ye,
S.Kalachikov,
and
H.A.Shuman
(2005).
Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer.
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J Bacteriol, 187,
7716-7726.
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R.Ghosh,
and
C.Chakrabarti
(2005).
Crystallization and preliminary X-ray diffraction studies of NP24-I, an isoform of a thaumatin-like protein from ripe tomato fruits.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 61,
806-807.
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Y.Dall'Antonia,
T.Pavkov,
H.Fuchs,
H.Breiteneder,
and
W.Keller
(2005).
Crystallization and preliminary structure determination of the plant food allergen Pru av 2.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 61,
186-188.
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H.Breiteneder
(2004).
Thaumatin-like proteins -- a new family of pollen and fruit allergens.
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Allergy, 59,
479-481.
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K.Min,
S.C.Ha,
P.M.Hasegawa,
R.A.Bressan,
D.J.Yun,
and
K.K.Kim
(2004).
Crystal structure of osmotin, a plant antifungal protein.
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Proteins, 54,
170-173.
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PDB code:
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R.A.Salzman,
H.Koiwa,
J.I.Ibeas,
J.M.Pardo,
P.M.Hasegawa,
and
R.A.Bressan
(2004).
Inorganic cations mediate plant PR5 protein antifungal activity through fungal Mnn1- and Mnn4-regulated cell surface glycans.
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Mol Plant Microbe Interact, 17,
780-788.
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S.B.Cannon,
A.Mitra,
A.Baumgarten,
N.D.Young,
and
G.May
(2004).
The roles of segmental and tandem gene duplication in the evolution of large gene families in Arabidopsis thaliana.
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BMC Plant Biol, 4,
10.
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O.L.Franco,
D.J.Rigden,
F.R.Melo,
and
M.F.Grossi-De-Sá
(2002).
Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.
|
| |
Eur J Biochem, 269,
397-412.
|
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|
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R.I.Osmond,
M.Hrmova,
F.Fontaine,
A.Imberty,
and
G.B.Fincher
(2001).
Binding interactions between barley thaumatin-like proteins and (1,3)-beta-D-glucans. Kinetics, specificity, structural analysis and biological implications.
|
| |
Eur J Biochem, 268,
4190-4199.
|
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|
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|
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E.Töpfer-Petersen
(1999).
Molecules on the sperm's route to fertilization.
|
| |
J Exp Zool, 285,
259-266.
|
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|
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|
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J.Grenier,
C.Potvin,
J.Trudel,
and
A.Asselin
(1999).
Some thaumatin-like proteins hydrolyse polymeric beta-1,3-glucans.
|
| |
Plant J, 19,
473-480.
|
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|
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|
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B.Fritig,
T.Heitz,
and
M.Legrand
(1998).
Antimicrobial proteins in induced plant defense.
|
| |
Curr Opin Immunol, 10,
16-22.
|
 |
|
|
|
|
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D.J.Yun,
J.I.Ibeas,
H.Lee,
M.A.Coca,
M.L.Narasimhan,
Y.Uesono,
P.M.Hasegawa,
J.M.Pardo,
and
R.A.Bressan
(1998).
Osmotin, a plant antifungal protein, subverts signal transduction to enhance fungal cell susceptibility.
|
| |
Mol Cell, 1,
807-817.
|
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|
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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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