Page 33 - 78_03
P. 33
M.
C.
AVENDAÑO
2.
Chorine,
V.;
(1945)
”Action
of
nicotinamide
on
bacilli
of
the
species
Mycobacterium”,
C.
R.
Acad.
Sci.
220,
150--151.
3.
Fox,
H.
H.;
(1952)
“The
chemical
approach
to
the
control
of
tuberculosis”,
Science
116,
129--134.
4.
Vilchèze,
C.;
Jacobs,
W.
R.;
(2007)
“The
Mechanism
of
Isoniazid
Killing:
Clarity
Through
the
Scope
of
Genetics”,
Annu.
Rev.
Microbiol.,
61,
35--50.
5.
Winder,
F.
G.;
Collins,
P.
B.;
(1970)
“Inhibition
by
isoniazid
of
synthesis
of
mycolic
acids
in
Mycobacterium
tuberculosis”,
J.
Gen.
Microbiol.
63,
41--48.
6.
Takayama,
K.;
Wang,
L.;
David,
H.
L.;
(1972)
“Effect
of
isoniazid
on
the
in
vivo
mycolic
acid
synthesis,
cell
growth,
and
viability
of
Mycobacterium
tuberculosis”,
Antimicrob.
Agents
Chemother.
2,
29--35.
7.
Davidson,
L.
A.;
Takayama,
K.;
(1979)
“Isoniazid
inhibition
of
the
synthesis
of
monounsaturated
long--chain
fatty
acids
in
Mycobacterium
tuberculosis
H37Ra”,
Antimicrob.
Agents
Chemother.
16,
104--105.
8.
Middlebrook,
G.;
(1954)
“Isoniazid
resistance
and
catalase
activity
of
tubercle
bacilli”,
Am.
Rev.
Tuberc.,
69,
471--472.
9.
Saroja.
D.;
Gopinathan,
K.
P.;
(1973)
“Transduction
of
isoniazid
susceptibility--resistance
and
streptomycin
resistance
in
mycobacteria”,
Antimicrob.
Agents
Chemother.,
4,
643--645.
10.
Zhang,
Y.;
Heym,
B.;
Allen,
B.;
Young,
D.;
Cole,
S.;
(1992)
“The
catalase--peroxidase
gene
and
isoniazid
resistance
of
Mycobacterium
tuberculosis”;
Nature,
358,
591--593.
11.
Jonson,
K.;
Schultz,
P.
G.;
(1994)
“Mechanistic
studies
of
the
oxidation
of
isoniazid
by
the
catalase
peroxidase
from
Mycobacterium
tuberculosis”,
J.
Am.
Chem.
Soc.,
116,
7425--7426.
12.
Lei,
B.;
Wei,
C.
J.;
Tu,
S.
C.;
(2000)
“Action
mechanism
of
antitubercular
isoniazid.
Activation
by
Mycobacterium
tuberculosis
KatG,
isolation,
and
characterization
of
inhA
inhibitor”,
J.
Biol.
Chem.,
275,
2520--2526.
13.
Winder,
F.;
(1960)
“Catalase
and
peroxidase
in
mycobacteria.
Possible
relationship
to
the
mode
of
action
of
isoniazid”,
Am.
Rev.
Respir.
Dis.,
81,
68--78.
14.
Hok,
T.
T.;
(1964)
“A
comparative
study
of
the
susceptibility
to
ethionamide,
thiosemicarbazone,
and
isoniazid
of
tubercle
bacilli
from
patients
never
treated
with
ethionamide
or
thiosemicarbazone”,
Am.
Rev.
Respir.
Dis.,
90,
468--469.
15.
Larsen,
M.
H.;
Vilcheze,
C.;
Kremer,
L.;
Besra,
G.
S.;
Parsons,
L.;
et
al.;
(2002)
“Overexpression
of
inhA,
but
not
kasA,
confers
resistance
to
isoniazid
and
ethionamide
in
Mycobacterium
smegmatis,
M.
bovis
BCG
and
M.
tuberculosis”,
Mol.
Microbiol.,
46,
453--466.
16.
Morlock,
G.
P.;
Metchock,
B--;
Sikes,
D.;
Crawford,
J.
T.;
Cooksey,
R.
C.;
(2003)
“ethA,
inhA,
and
katG
loci
of
ethionamide--resistant
clinical
Mycobacterium
tuberculosis
isolates”,
Antimicrob.
Agents
Chemother.,
47,
3799--3805.
17.
Parikh,
S.
L.;
Xiao,
G.;
Tonge,
P.
J.;
(2000)
“Inhibition
of
InhA,
the
enoyl
reductase
from
Mycobacterium
tuberculosis,
by
triclosan
and
isoniazid”,
Biochemistry,
39,
7645--7650.
18.
Rozwarski,
D.
A.;
Grant,
G.
A.;
Barton,
D.
H.;
Jacobs,
W.
R.;
Sacchettini,
J.
C.;
(1998)
“Modification
of
the
NADH
of
the
isoniazid
target
(InhA)
from
Mycobacterium
tuberculosis”,
Science
279,
98--102.
19.
Mdluli,
K.;
Slayden,
R.
A.;
Zhu,
Y.;
Ramaswamy,
S.;
Pan,
X.;
et
al.;
(1998)
“Inhibition
of
a
Mycobacterium
tuberculosis
beta--ketoacyl
ACP
synthase
by
isoniazid”,
Science,
280,
1607--1610.
20.
Argyrou,
A.;
Vetting,
M.
W.;
Aladegbami,
B.;
Blanchard,
J.
S.;
(2006)
“Mycobacterium
tuberculosis
dihydrofolate
reductase
is
a
target
for
isoniazid”,
Nat.
Struct.
Mol.
Biol.,
13,
408--413.
21.
Timmins,
G.
S.;
Master,
S.;
Rusnak,
F.;
Deretic,
V.;
(2004)
“Nitric
oxide
generated
from
isoniazid
activation
by
KatG:
source
of
nitric
oxide
and
activity
against
Mycobacterium
tuberculosis”;
Antimicrob.
Agents
Chemother.,
48,
3006--3009.
22.
Vilcheze,
C.;
Wang,
F.;
Arai,
M.;
Hazbon,
M.
H.;
Colangeli,
R.;
et
al.;
(2006)
“Transfer
of
a
point
mutation
in
Mycobacterium
tuberculosis
inhA
resolves
the
target
of
isoniazid”,
Nat.
Med.,
12,
1027--
1029.
296