Dr. Asha M. Balakrishna, PhD
Publications:
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Karanth, N.G.K, Pasha, A., Amita Rani B.E., Asha,
M.B., Udayakumari, C.G. and Vijayashankar, Y.N.
(1999) Rapid tests for monitoring pesticide
residues in the environment.
Journ. Envir. Sci.
3, 1-10
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Balakrishna, A. M.,
Tan,
Y.-W., Mok, H.Q.-K., Saxena, A. and Swaminathan , K.
(2006) Crystallization and preliminary X-ray
diffraction analysis of Salmonella typhi PilS dimer.
Acta. Cryst. F62,
1024-1026
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Gayen, S., Balakrishna,
A. M.,
Biuković, G., Yulei, W., Hunke, C. and Grüber, G.
(2008)
Identification of critical residues
of subunit H in its interaction with subunit
E of the A-ATP synthase from Methanocaldococcus
jannaschii.
FEBS J. 275, 1803-1812
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Kumar, A., Manimekalai, M. S. S., Balakrishna, A.
M., Hunke, C., Weigelt, S., Sewald, N. and
Grüber, G. (2009) Spectroscopic and
crystallographic studies of the mutant R416W give
insight into the nucleotide binding traits of
subunit B of the A1AO ATP
synthase.
PROTEINS: Structure,
Function and Bioinformatics 75, 807-819
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Manimekalai, M. S. S., Kumar, A., Balakrishna, A.
M. and Grüber, G. (2009) A second
transient position of ATP on its trail to the
nucleotide-binding site of subunit B of the motor
protein A1AO
ATP synthase.
J. Struct. Biol. 166, 39-45
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Gayen, S., Balakrishna, A. M. and Grüber, G.
(2009)
NMR solution structure of the N–terminal domain of
subunit E (E1-52) of A1AO
ATP synthase
from Methanocaldococcus jannaschii.
J. Bioenerg. Biomembr. 41, 343-348
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Kumar,
A., Manimekalai, M. S. S., Balakrishna, A. M.,
Jeyakanthan, J., and Grüber, G. (2010)
Nucleotide-binding
states of subunit A of the A-ATP synthase and the
implication of P-loop switch in evolution. J.
Mol. Biol. 396,
301-320
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Balakrishna, A. M.1,
Hunke, C.1 and Grüber, G. (2010)
Purification and
crystallization of the entire recombinant subunit E
of the energy producer A1AO
ATP synthase.
Acta. Cryst.
F66, 324-326
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Grüber, A., Manimekalai, M. S. S., Balakrishna,
A. M., Hunke, C., Jeyakanthan, J., Preiser, P.
and Grüber, G. (2010) Structural
determination of functional units of the nucleotide
binding domain (NBD94) of the reticulocyte binding
protein Py235 of Plasmodium yoelii.
PLoS ONE 5,
9146-9157
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Balakrishna, A. M.,
Manimekalai, M. S. S,.
Hunke, C., Gayen, S., Rössle, M., Jeyakanthan, J.
and Grüber, G. (2010) Crystal and solution
structure of the C-terminal part of the
Methanocaldococcus jannaschii
A1AO
ATP synthase subunit E revealed by X-ray
diffraction and small-angle X-ray scattering.
J. Bioenerg. Biomembr.
42, 311-320
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Kumar,
A., Manimekalai, M. S. S., Balakrishna, A. M.,
Priya, R., Biuković, G., Jeyakanthan, J., and
Grüber, G. (2010) The critical roles of residues
P235 and F236 of subunit A of the motor protein
A-ATP synthase in P-loop formation and
nucleotide-binding.
J. Mol. Biol.
401, 892-905
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Balakrishna,
A. M., Hunke, C., and Grüber, G. (2012)
The structure of subunit E of the Pyrococcus
horikoshii OT3 A-ATP synthase gives insight into the
elasticity of the peripheral stalk.
J. Mol. Biol.,
420, 155-163
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Basak, S., Balakrishna, A. M., Manimekalai,
M. S. S., and Grüber, G. (2012) Crystallization
and preliminary X-ray crystallographic analysis of
subunit F, F1-94,
an essential coupling subunit of the eukaryotic V1VO
ATPase from Saccharomyces cerevisiae.
Acta Cryst. F68, 1055-1059
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Alag, R., Balakrishna, A. M., Rajan, S.,
Qureshi, I., Shin, J., Lescar, J., Grüber, G., and
Yoon, H. S. (2013) Structural insights into
substrate binding by PvFKBP35, a peptidylprolyl cis-trans
isomerase from the human malarial parasite
Plasmodium vivax.
Eukaryotic Cell, in press
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Basak, S., Lim, J., Manimekalai, M. S. S.,
Balakrishna, A. M., and Grüber, G. (2013)
Crystal- and NMR structures give insights into the
role and dynamics of subunit F of the eukaryotic V-ATPase
from Saccharomyces cerevisiae.
J. Biol. Chem.
288, 11930-11939
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Balakrishna, A. M., Seelert, H., Marx, S.-H.
Dencher, N.A., and Grüber, G. (2014)
Crystallographic structure of the turbine c-ring
from spinach chloroplast F-ATP synthase.
Biosci. Rep.
34, e00102
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Dip, P. V., Kamariah, N., Manimekalai, M. S. S.,
Nartey, W., Balakrishna, A. M., Eisenhaber,
F., Eisenhaber, B. and Grüber, G. (2014) Structure, mechanism and ensemble
formation of the Alkylhydroperoxide Reductase
subunits AhpC and AhpF from Escherichia coli.
Acta
Crystallogr. D70, 2848-2862
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Balakrishna, A. M., Basak, S., Manimekalai,
M. S. S., and Grüber, G.* (2015) Crystal
structure of subunits D and F in complex give
insight into energy transmission of the eukaryotic
V-ATPase from Saccharomyces cerevisiae.
J.
Biol. Chem. 290, 3183-3196
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Balakrishna, A. M., Manimekalai, M. S. S.,
and Grüber, G. (2015) Protein-protein
interactions within the ensemble, Eukaryotic V-ATPase,
and its concerted interactions with cellular
machineries.
Progr. Biophys. Mol. Biol.
119, 84-93
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Kumar, A., Balakrishna, A. M.1, Nartey, W.1, Manimekalai, M. S. S., and Grüber, G. (2016)
Redox chemistry of Mycobacterium tuberculosis
alkylhydroperoxide reductase E (AhpE): Structural
and mechanistic insight into a mycoredoxin-1
independent reductive pathway of AhpE via mycothiol.
Free Rad. Biol. Med.
97, 588-601
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Singal, B., Balakrishna, A., Nartey, W.,
Manimekalai, M.S.S., Jeyakanthan, J. and Grüber, G.*
(2017) Crystallographic and solution structure of
the N-terminal domain of the Rel protein from
Mycobacterium tuberculosis.
FEBS Letters
591, 2323-2337
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Toh, Y.K., Balakrishna, A.M., Manimekalai,
M.S.S., Chionh, B.B., Seetharaman, R.R.C.,
Eisenhaber, B., Eisenhaber, F. and Grüber, G. (2017)
Novel insights into the vancomycin-resistant
Enterococcus faecalis (V583) alkylhydroperoxide
reductase subunit F.
Biochim. Biophys. Acta-General Subject
1861, 3201-3214
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Pan, A., Balakrishna, A.M., Nartey, W.,
Kohlmeier, A., Dip, P.V., Bhushan, S., Grüber, G.*
(2018) Atomic structure and enzymatic insights
into the vancomycin-resistant Enterococcus faecalis
(V583) alkylhydroperoxide reductase subunit C.
Free Rad. Biol. Med.
115, 252-265
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Toh, Y.K., Balakrishna, A., Shin, J., Neelagandan, K., Grüber, A., Eisenhaber, F.,
Eisenhaber, B. and Grüber, G.* (2019) Effect of
the additional cysteine 503 of vancomycin-resistant
Enterococcus faecalis (V583) alkylhydroperoxide
reductase subunit F (AhpF) and the mechanism of AhpF
and subunit C assembling.
Free Rad. Med. Biol.
138, 10-22
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(Authors have equal contribution)
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