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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L.Fernández,
J.Caballero,
J.I.Abreu,
and
M.Fernández
(2007).
Amino acid sequence autocorrelation vectors and Bayesian-regularized genetic neural networks for modeling protein conformational stability: gene V protein mutants.
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Proteins, 67,
834-852.
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A.Mozo-Villarías,
J.Cedano,
and
E.Querol
(2006).
Hydrophobicity density profiles to predict thermal stability enhancement in proteins.
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Protein J, 25,
529-535.
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J.Cheng,
A.Randall,
and
P.Baldi
(2006).
Prediction of protein stability changes for single-site mutations using support vector machines.
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Proteins, 62,
1125-1132.
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K.Saraboji,
M.M.Gromiha,
and
M.N.Ponnuswamy
(2006).
Average assignment method for predicting the stability of protein mutants.
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Biopolymers, 82,
80-92.
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Y.Hioki,
K.Ogasahara,
S.J.Lee,
J.Ma,
M.Ishida,
Y.Yamagata,
Y.Matsuura,
M.Ota,
M.Ikeguchi,
S.Kuramitsu,
and
K.Yutani
(2004).
The crystal structure of the tryptophan synthase beta subunit from the hyperthermophile Pyrococcus furiosus. Investigation of stabilization factors.
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Eur J Biochem, 271,
2624-2635.
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PDB code:
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H.Minagawa,
J.Shimada,
and
H.Kaneko
(2003).
Effect of mutations at Glu160 and Val198 on the thermostability of lactate oxidase.
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Eur J Biochem, 270,
3628-3633.
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A.L.Lomize,
M.Y.Reibarkh,
and
I.D.Pogozheva
(2002).
Interatomic potentials and solvation parameters from protein engineering data for buried residues.
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Protein Sci, 11,
1984-2000.
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J.Higo,
and
M.Nakasako
(2002).
Hydration structure of human lysozyme investigated by molecular dynamics simulation and cryogenic X-ray crystal structure analyses: on the correlation between crystal water sites, solvent density, and solvent dipole.
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J Comput Chem, 23,
1323-1336.
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PDB code:
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K.Takano,
Y.Yamagata,
and
K.Yutani
(2001).
Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme.
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Proteins, 44,
233-243.
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PDB codes:
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K.Takano,
Y.Yamagata,
and
K.Yutani
(2001).
Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein.
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Proteins, 45,
274-280.
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PDB codes:
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M.Joniau,
P.Haezebrouck,
K.Noyelle,
and
H.Van Dael
(2001).
Structural basis for the appearance of a molten globule state in chimeric molecules derived from lysozyme and alpha-lactalbumin.
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Proteins, 44,
1.
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J.Funahashi,
K.Takano,
Y.Yamagata,
and
K.Yutani
(2000).
Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions.
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Biochemistry, 39,
14448-14456.
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PDB codes:
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K.Takano,
Y.Yamagata,
and
K.Yutani
(2000).
Role of amino acid residues at turns in the conformational stability and folding of human lysozyme.
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Biochemistry, 39,
8655-8665.
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PDB codes:
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K.Takano,
K.Tsuchimori,
Y.Yamagata,
and
K.Yutani
(1999).
Effect of foreign N-terminal residues on the conformational stability of human lysozyme.
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Eur J Biochem, 266,
675-682.
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PDB codes:
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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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130 a.a.
_NA
