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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M.Jagodzinska,
F.Huguenot,
G.Candiani,
and
M.Zanda
(2009).
Assessing the bioisosterism of the trifluoromethyl group with a protease probe.
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ChemMedChem, 4,
49-51.
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M.Rouffet,
C.Denhez,
E.Bourguet,
F.Bohr,
and
D.Guillaume
(2009).
In silico study of MMP inhibition.
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Org Biomol Chem, 7,
3817-3825.
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M.Fernández,
L.Fernández,
J.Caballero,
J.I.Abreu,
and
G.Reyes
(2008).
Proteochemometric modeling of the inhibition complexes of matrix metalloproteinases with N-hydroxy-2-[(phenylsulfonyl)amino]acetamide derivatives using topological autocorrelation interaction matrix and model ensemble averaging.
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Chem Biol Drug Des, 72,
65-78.
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A.B.Hamze,
S.Wei,
H.Bahudhanapati,
S.Kota,
K.R.Acharya,
and
K.Brew
(2007).
Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors.
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Protein Sci, 16,
1905-1913.
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A.Khandelwal,
and
S.Balaz
(2007).
Improved estimation of ligand-macromolecule binding affinities by linear response approach using a combination of multi-mode MD simulation and QM/MM methods.
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J Comput Aided Mol Des, 21,
131-137.
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A.R.Johnson,
A.G.Pavlovsky,
D.F.Ortwine,
F.Prior,
C.F.Man,
D.A.Bornemeier,
C.A.Banotai,
W.T.Mueller,
P.McConnell,
C.Yan,
V.Baragi,
C.Lesch,
W.H.Roark,
M.Wilson,
K.Datta,
R.Guzman,
H.K.Han,
and
R.D.Dyer
(2007).
Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects.
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J Biol Chem, 282,
27781-27791.
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PDB codes:
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L.R.Pal,
and
C.Guda
(2006).
Tracing the origin of functional and conserved domains in the human proteome: implications for protein evolution at the modular level.
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BMC Evol Biol, 6,
91.
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Y.Zhao,
W.Feng,
Y.Yang,
L.Ling,
and
R.Chen
(2006).
Comparison of properties of tumor necrosis factor-alpha converting enzyme (TACE) and some matrix metalloproteases (MMPs) in catalytic domains.
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J Huazhong Univ Sci Technolog Med Sci, 26,
637-639.
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A.L.Banerjee,
S.Tobwala,
M.K.Haldar,
M.Swanson,
B.C.Roy,
S.Mallik,
and
D.K.Srivastava
(2005).
Inhibition of matrix metalloproteinase-9 by "multi-prong" surface binding groups.
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Chem Commun (Camb), 0,
2549-2551.
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H.Yi,
J.Gruszczynska-Biegala,
D.Wood,
Z.Zhao,
and
A.Zolkiewska
(2005).
Cooperation of the metalloprotease, disintegrin, and cysteine-rich domains of ADAM12 during inhibition of myogenic differentiation.
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J Biol Chem, 280,
23475-23483.
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B.E.Turk,
T.Y.Wong,
R.Schwarzenbacher,
E.T.Jarrell,
S.H.Leppla,
R.J.Collier,
R.C.Liddington,
and
L.C.Cantley
(2004).
The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor.
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Nat Struct Mol Biol, 11,
60-66.
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PDB codes:
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I.Svab,
D.Alexandru,
G.Vitos,
and
M.L.Flonta
(2004).
Binding affinities for sulfonamide inhibitors with matrix metalloproteinase-2 using a linear response method.
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J Cell Mol Med, 8,
551-562.
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V.Lukacova,
Y.Zhang,
M.Mackov,
P.Baricic,
S.Raha,
J.A.Calvo,
and
S.Balaz
(2004).
Similarity of binding sites of human matrix metalloproteinases.
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J Biol Chem, 279,
14194-14200.
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H.I.Park,
Y.Jin,
D.R.Hurst,
C.A.Monroe,
S.Lee,
M.A.Schwartz,
and
Q.X.Sang
(2003).
The intermediate S1' pocket of the endometase/matrilysin-2 active site revealed by enzyme inhibition kinetic studies, protein sequence analyses, and homology modeling.
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J Biol Chem, 278,
51646-51653.
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S.Steinbacher,
J.Kaiser,
W.Eisenreich,
R.Huber,
A.Bacher,
and
F.Rohdich
(2003).
Structural basis of fosmidomycin action revealed by the complex with 2-C-methyl-D-erythritol 4-phosphate synthase (IspC). Implications for the catalytic mechanism and anti-malaria drug development.
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J Biol Chem, 278,
18401-18407.
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PDB codes:
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W.Bode,
and
K.Maskos
(2003).
Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases.
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Biol Chem, 384,
863-872.
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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
codes are
shown on the right.
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159 a.a.
_CA
_ZN
