-
1
-
-
55949092734
-
Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity
-
COI: 1:CAS:528:DC%2BD1cXhtleksrrJ, PID: 18948593
-
Andreasson C, Fiaux J, Rampelt H, Druffel-Augustin S, Bukau B (2008) Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity. Proc Natl Acad Sci U S A 105:16519–16524
-
(2008)
Proc Natl Acad Sci U S A
, vol.105
, pp. 16519-16524
-
-
Andreasson, C.1
Fiaux, J.2
Rampelt, H.3
Druffel-Augustin, S.4
Bukau, B.5
-
2
-
-
34548232285
-
The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host
-
Botha M, Pesce ER., Blatch GL (2007) The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host. Int J Biochem Cell Biol 39: 1781–803
-
(2007)
Int J Biochem Cell Biol
, vol.39
, pp. 1781-1803
-
-
Botha, M.1
Pesce, E.R.2
Blatch, G.L.3
-
3
-
-
60249092974
-
Select pyrimidinones inhibit the propagation of the malarial parasite, Plasmodium falciparum
-
COI: 1:CAS:528:DC%2BD1MXitVyisb8%3D, PID: 19195901
-
Chiang AN, Valderramos JC, Balachandran R, Chovatiya RJ, Mead BP, Schneider C, Bell SL, Klein MG, Huryn DM, Chen XS, Day BW, Fidock DA, Wipf P, Brodsky JL (2009) Select pyrimidinones inhibit the propagation of the malarial parasite, Plasmodium falciparum. Bioorg Med Chem 17:1527–1533
-
(2009)
Bioorg Med Chem
, vol.17
, pp. 1527-1533
-
-
Chiang, A.N.1
Valderramos, J.C.2
Balachandran, R.3
Chovatiya, R.J.4
Mead, B.P.5
Schneider, C.6
Bell, S.L.7
Klein, M.G.8
Huryn, D.M.9
Chen, X.S.10
Day, B.W.11
Fidock, D.A.12
Wipf, P.13
Brodsky, J.L.14
-
4
-
-
79953855334
-
Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: inhibition of the plasmodial chaperone PfHsp70-1
-
COI: 1:CAS:528:DC%2BC3MXnsl2lsLg%3D, PID: 21426241
-
Cockburn IL, Pesce ER, Pryzborski JM, Davies-Coleman MT, Clark PG, Keyzers RA, Stephens LL, Blatch GL (2011) Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: inhibition of the plasmodial chaperone PfHsp70-1. Biol Chem 392:431–438
-
(2011)
Biol Chem
, vol.392
, pp. 431-438
-
-
Cockburn, I.L.1
Pesce, E.R.2
Pryzborski, J.M.3
Davies-Coleman, M.T.4
Clark, P.G.5
Keyzers, R.A.6
Stephens, L.L.7
Blatch, G.L.8
-
5
-
-
84907612318
-
Selective modulation of plasmodial Hsp70s by small molecules with antimalarial activity
-
COI: 1:CAS:528:DC%2BC2cXhvFaltrjK, PID: 24854538
-
Cockburn IL, Boshoff A, Pesce E-R, Blatch GL (2014) Selective modulation of plasmodial Hsp70s by small molecules with antimalarial activity. Biol Chem 395:1353–1362
-
(2014)
Biol Chem
, vol.395
, pp. 1353-1362
-
-
Cockburn, I.L.1
Boshoff, A.2
Pesce, E.-R.3
Blatch, G.L.4
-
6
-
-
33745762927
-
Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
-
COI: 1:CAS:528:DC%2BD28XltlGksr4%3D, PID: 16688212
-
Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU (2006) Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 25:2519–2528
-
(2006)
EMBO J
, vol.25
, pp. 2519-2528
-
-
Dragovic, Z.1
Broadley, S.A.2
Shomura, Y.3
Bracher, A.4
Hartl, F.U.5
-
7
-
-
84863599206
-
Characterization of the Plasmodium falciparum Hsp70-α organising protein (PfHop)
-
COI: 1:CAS:528:DC%2BC38XitFGgsL0%3D, PID: 22005844
-
Gitau GW, Mandal P, Blatch GL, Przyborski J, Shonhai A (2012) Characterization of the Plasmodium falciparum Hsp70-α organising protein (PfHop). Cell Stress Chaperones 17:191–202
-
(2012)
Cell Stress Chaperones
, vol.17
, pp. 191-202
-
-
Gitau, G.W.1
Mandal, P.2
Blatch, G.L.3
Przyborski, J.4
Shonhai, A.5
-
8
-
-
0036678054
-
Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj-151 thermosensitivity and restores Hsp90-dependent activity
-
COI: 1:CAS:528:DC%2BD38XmsVKlsLw%3D, PID: 12181344
-
Goeckeler JL, Stephens A, Lee P, Caplan AJ, Brodsky JL (2002) Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj-151 thermosensitivity and restores Hsp90-dependent activity. Mol Biol Cell 13:2760–2770
-
(2002)
Mol Biol Cell
, vol.13
, pp. 2760-2770
-
-
Goeckeler, J.L.1
Stephens, A.2
Lee, P.3
Caplan, A.J.4
Brodsky, J.L.5
-
9
-
-
84867636034
-
Plasmodium falciparum-encoded exported hsp70/hsp40 chaperone/co-chaperone complexes within the host erythrocyte
-
PID: 22925632
-
Külzer S, Charnaud S, Dagan T, Riedel J, Mandal P, Pesce ER, Blatch GL, Crabb BS, Gilson PR, Przyborski JM (2012) Plasmodium falciparum-encoded exported hsp70/hsp40 chaperone/co-chaperone complexes within the host erythrocyte. Cell Microbiol 14:1784–1795
-
(2012)
Cell Microbiol
, vol.14
, pp. 1784-1795
-
-
Külzer, S.1
Charnaud, S.2
Dagan, T.3
Riedel, J.4
Mandal, P.5
Pesce, E.R.6
Blatch, G.L.7
Crabb, B.S.8
Gilson, P.R.9
Przyborski, J.M.10
-
10
-
-
0026320296
-
The Escherichia coli DnaK chaperone, the 70 kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein
-
COI: 1:CAS:528:DyaK3MXmtVWqsb4%3D, PID: 1830586
-
Liberek K, Skowyra D, Zylicz M, Johnson C, Georgopoulos C (1991) The Escherichia coli DnaK chaperone, the 70 kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein. J Biol Chem 266:14491–14496
-
(1991)
J Biol Chem
, vol.266
, pp. 14491-14496
-
-
Liberek, K.1
Skowyra, D.2
Zylicz, M.3
Johnson, C.4
Georgopoulos, C.5
-
11
-
-
84876910024
-
Cysteine-capped gold nanoparticles suppress aggregation of proteins exposed to heat stress
-
COI: 1:CAS:528:DC%2BC3sXivFelu7Y%3D, PID: 23436466
-
Luthuli SD, Chili MM, Revaprasadu N, Shonhai A (2013) Cysteine-capped gold nanoparticles suppress aggregation of proteins exposed to heat stress. IUBMB Life 65:454–461
-
(2013)
IUBMB Life
, vol.65
, pp. 454-461
-
-
Luthuli, S.D.1
Chili, M.M.2
Revaprasadu, N.3
Shonhai, A.4
-
12
-
-
34848869936
-
Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1
-
COI: 1:CAS:528:DC%2BD2sXht1CntLnJ, PID: 17923091
-
Liu Q, Hendrickson WA (2007) Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1. Cell 131:106–120
-
(2007)
Cell
, vol.131
, pp. 106-120
-
-
Liu, Q.1
Hendrickson, W.A.2
-
14
-
-
77951754467
-
Hsp110 chaperones control client fate determination in the Hsp70-Hsp90 chaperone system
-
COI: 1:CAS:528:DC%2BC3cXpslyku7c%3D, PID: 20237159
-
Mandal AK, Gibney PA, Nillegoda NB, Theodoraki MA, Caplan AJ, Morano KA (2010) Hsp110 chaperones control client fate determination in the Hsp70-Hsp90 chaperone system. Mol Biol Cell 21:1439–2448
-
(2010)
Mol Biol Cell
, vol.21
, pp. 1439-2448
-
-
Mandal, A.K.1
Gibney, P.A.2
Nillegoda, N.B.3
Theodoraki, M.A.4
Caplan, A.J.5
Morano, K.A.6
-
15
-
-
17044387386
-
Hsp70 chaperones: cellular functions and molecular mechanism
-
COI: 1:CAS:528:DC%2BD2MXktlymt78%3D, PID: 15770419
-
Mayer MP, Bukau B (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 62:670–684
-
(2005)
Cell Mol Life Sci
, vol.62
, pp. 670-684
-
-
Mayer, M.P.1
Bukau, B.2
-
16
-
-
0033936317
-
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
-
COI: 1:CAS:528:DC%2BD3cXkslKnur0%3D
-
Mayer MP, Schröder H, Rüdiger S, Paal K, Laufen T, Bukau B (2000) Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat Struct Mol Biol 7:586–593
-
(2000)
Nat Struct Mol Biol
, vol.7
, pp. 586-593
-
-
Mayer, M.P.1
Schröder, H.2
Rüdiger, S.3
Paal, K.4
Laufen, T.5
Bukau, B.6
-
17
-
-
84883235332
-
Mutational analysis of Sse1 (Hsp110) suggest an integral role for this chaperone in yeast prion propagation in vivo
-
Moran C, Kinsella GK, Zhang Z, Perret S, Jones GW (2013) Mutational analysis of Sse1 (Hsp110) suggest an integral role for this chaperone in yeast prion propagation in vivo. G3-Genes Genoms Genet 3:1409–1418
-
(2013)
G3-Genes Genoms Genet
, vol.3
, pp. 1409-1418
-
-
Moran, C.1
Kinsella, G.K.2
Zhang, Z.3
Perret, S.4
Jones, G.W.5
-
18
-
-
84871752624
-
Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers
-
PID: 23250440
-
Muralidharan V, Oksman A, Pal P, Lindquist S, Goldberg DE (2012) Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers. Nat Commun 3:1310
-
(2012)
Nat Commun
, vol.3
, pp. 1310
-
-
Muralidharan, V.1
Oksman, A.2
Pal, P.3
Lindquist, S.4
Goldberg, D.E.5
-
19
-
-
77955682353
-
Chaperone expression profiles correlate with distinct physiological states of Plasmodium falciparum in malaria patients
-
PID: 20719001
-
Pallavi R, Archarya P, Chandran S, Daily JP, Tatu U (2010) Chaperone expression profiles correlate with distinct physiological states of Plasmodium falciparum in malaria patients. Malar J 9:236
-
(2010)
Malar J
, vol.9
, pp. 236
-
-
Pallavi, R.1
Archarya, P.2
Chandran, S.3
Daily, J.P.4
Tatu, U.5
-
20
-
-
51249122014
-
The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns
-
COI: 1:CAS:528:DC%2BD1cXhtFaisbzK, PID: 18674634
-
Pesce ER, Acharya P, Tatu U, Nicoll WS, Shonhai A, Hoppe HC, Blatch GL (2008) The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns. Int J Biochem Cell Biol 40:2914–2926
-
(2008)
Int J Biochem Cell Biol
, vol.40
, pp. 2914-2926
-
-
Pesce, E.R.1
Acharya, P.2
Tatu, U.3
Nicoll, W.S.4
Shonhai, A.5
Hoppe, H.C.6
Blatch, G.L.7
-
21
-
-
44649110104
-
Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
-
COI: 1:CAS:528:DC%2BD1cXnsF2gtbc%3D, PID: 18555782
-
Polier S, Dragovic Z, Hartl FU, Bracher A (2008) Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133:1068–1079
-
(2008)
Cell
, vol.133
, pp. 1068-1079
-
-
Polier, S.1
Dragovic, Z.2
Hartl, F.U.3
Bracher, A.4
-
22
-
-
77955559261
-
Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein
-
COI: 1:CAS:528:DC%2BC3cXhtVaqs7rK, PID: 20624400
-
Polier S, Hartl FU, Bracher A (2010) Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein. J Mol Biol 401:696–707
-
(2010)
J Mol Biol
, vol.401
, pp. 696-707
-
-
Polier, S.1
Hartl, F.U.2
Bracher, A.3
-
23
-
-
33745749328
-
Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
-
COI: 1:CAS:528:DC%2BD28XltlGksr8%3D, PID: 16688211
-
Raviol H, Sadlish H, Rodriguez F, Mayer MP, Bukau B (2006) Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J 25:2510–2518
-
(2006)
EMBO J
, vol.25
, pp. 2510-2518
-
-
Raviol, H.1
Sadlish, H.2
Rodriguez, F.3
Mayer, M.P.4
Bukau, B.5
-
24
-
-
45849091944
-
Structure of the Hsp110:Hsc70 nucleotide exchange machine
-
COI: 1:CAS:528:DC%2BD1cXpsFOgtLs%3D, PID: 18550409
-
Schuermann JP, Jiang J, Cuellar J, Llorca O, Wang L, Gimenez LE, Jin S, Taylor AB, Demeler B, Morano KA, Hart PJ, Valpuesta JM, Lafer EM, Sousa R (2008) Structure of the Hsp110:Hsc70 nucleotide exchange machine. Mol Cell 31:232–243
-
(2008)
Mol Cell
, vol.31
, pp. 232-243
-
-
Schuermann, J.P.1
Jiang, J.2
Cuellar, J.3
Llorca, O.4
Wang, L.5
Gimenez, L.E.6
Jin, S.7
Taylor, A.B.8
Demeler, B.9
Morano, K.A.10
Hart, P.J.11
Valpuesta, J.M.12
Lafer, E.M.13
Sousa, R.14
-
25
-
-
84884806955
-
A purine analog synergizes with chloroquine (CQ) by targeting Plasmodium falciparum Hsp90 (PfHsp90)
-
COI: 1:CAS:528:DC%2BC3sXhsFOrsbbM, PID: 24098696
-
Shahinas D, Folefoc A, Taldone T, Chiosis G, Crandall I, Pillai DR (2013) A purine analog synergizes with chloroquine (CQ) by targeting Plasmodium falciparum Hsp90 (PfHsp90). PLoS ONE 8, e75446
-
(2013)
PLoS ONE
, vol.8
-
-
Shahinas, D.1
Folefoc, A.2
Taldone, T.3
Chiosis, G.4
Crandall, I.5
Pillai, D.R.6
-
26
-
-
4644370187
-
Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum
-
COI: 1:CAS:528:DC%2BD2cXnslGgsrw%3D, PID: 15383301
-
Singh GP, Chandra BR, Bhattacharya A, Akhouri RR, Singh SK, Sharma A (2004) Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum. Mol Biochem Parasitol 137:307–319
-
(2004)
Mol Biochem Parasitol
, vol.137
, pp. 307-319
-
-
Singh, G.P.1
Chandra, B.R.2
Bhattacharya, A.3
Akhouri, R.R.4
Singh, S.K.5
Sharma, A.6
-
27
-
-
0035936826
-
Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors
-
COI: 1:CAS:528:DC%2BD3MXhsVeqt7s%3D, PID: 11222862
-
Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, Moarefi I (2001) Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291:1553–1557
-
(2001)
Science
, vol.291
, pp. 1553-1557
-
-
Sondermann, H.1
Scheufler, C.2
Schneider, C.3
Hohfeld, J.4
Hartl, F.U.5
Moarefi, I.6
-
28
-
-
13244278043
-
Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange
-
COI: 1:CAS:528:DC%2BD2MXhs1Oitrc%3D, PID: 15694338
-
Shomura Y, Dragovic Z, Chang HC, Tzvetkov N, Young JC, Brodsky JL, Guerriero V, Hartl FU, Bracher A (2005) Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Mol Cell 17:367–379
-
(2005)
Mol Cell
, vol.17
, pp. 367-379
-
-
Shomura, Y.1
Dragovic, Z.2
Chang, H.C.3
Tzvetkov, N.4
Young, J.C.5
Brodsky, J.L.6
Guerriero, V.7
Hartl, F.U.8
Bracher, A.9
-
29
-
-
74549179024
-
Plasmodial heat shock proteins: targets for chemotherapy
-
Shonhai A (2010) Plasmodial heat shock proteins: targets for chemotherapy. FEMS Immunol Med Microbiol 58: 61–74
-
(2010)
FEMS Immunol Med Microbiol
, vol.58
, pp. 61-74
-
-
Shonhai, A.1
-
30
-
-
25844526400
-
Plasmodium falciparum heat shock protein 70 is able to suppress the thermosensitivity of an Escherichia coli DnaK mutant strain
-
COI: 1:CAS:528:DC%2BD2MXhtVGntrrL
-
Shonhai A, Boshoff A, Blatch GL (2005) Plasmodium falciparum heat shock protein 70 is able to suppress the thermosensitivity of an Escherichia coli DnaK mutant strain. Mol Gen Genet 274:70–78
-
(2005)
Mol Gen Genet
, vol.274
, pp. 70-78
-
-
Shonhai, A.1
Boshoff, A.2
Blatch, G.L.3
-
31
-
-
34548461255
-
The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum
-
COI: 1:CAS:528:DC%2BD2sXhtVaksrfP, PID: 17766381
-
Shonhai A, Boshoff A, Blatch GL (2007) The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum. Protein Sci 16:1803–1818
-
(2007)
Protein Sci
, vol.16
, pp. 1803-1818
-
-
Shonhai, A.1
Boshoff, A.2
Blatch, G.L.3
-
32
-
-
54249123736
-
Structure-function study of Plasmodium falciparum Hsp70 using three dimensional modelling and in-vitro analyses
-
COI: 1:CAS:528:DC%2BD1cXht1Sru7bE, PID: 19075824
-
Shonhai A, Botha M, de Beer TAP, Boshoff A, Blatch GL (2008) Structure-function study of Plasmodium falciparum Hsp70 using three dimensional modelling and in-vitro analyses. Protein Pept Lett 15:1117–1125
-
(2008)
Protein Pept Lett
, vol.15
, pp. 1117-1125
-
-
Shonhai, A.1
Botha, M.2
de Beer, T.A.P.3
Boshoff, A.4
Blatch, G.L.5
-
33
-
-
79952172924
-
Intracellular protozoan parasites of humans: the role of molecular chaperones in development and pathogenesis
-
COI: 1:CAS:528:DC%2BC3MXhsl2rtrk%3D, PID: 20955165
-
Shonhai A, Maier AG, Przyborski JM, Blatch GL (2011) Intracellular protozoan parasites of humans: the role of molecular chaperones in development and pathogenesis. Protein Pept Lett 18:143–157
-
(2011)
Protein Pept Lett
, vol.18
, pp. 143-157
-
-
Shonhai, A.1
Maier, A.G.2
Przyborski, J.M.3
Blatch, G.L.4
-
34
-
-
44849132073
-
Slot-blot analysis of 3-nitrotyrosine-modified brain proteins
-
COI: 1:CAS:528:DC%2BD1cXntF2hsLg%3D, PID: 18423227
-
Sultana R, Butterfield AD (2008) Slot-blot analysis of 3-nitrotyrosine-modified brain proteins. Methods Enzymol 440:309–316
-
(2008)
Methods Enzymol
, vol.440
, pp. 309-316
-
-
Sultana, R.1
Butterfield, A.D.2
-
35
-
-
33846020582
-
Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker
-
Vogel M, Mayer MP, Bukau B (2005) Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J Biol Chem 281:38705–38711
-
(2005)
J Biol Chem
, vol.281
, pp. 38705-38711
-
-
Vogel, M.1
Mayer, M.P.2
Bukau, B.3
-
36
-
-
84939144676
-
Overexpression, purification and characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) protein
-
PID: 26083397
-
Zininga T, Achilonu I, Hoppe H, Prinsloo E, Dirr HW, Shonhai A (2015a) Overexpression, purification and characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) protein. PLoS ONE 10, e0129445
-
(2015)
PLoS ONE
, vol.10
-
-
Zininga, T.1
Achilonu, I.2
Hoppe, H.3
Prinsloo, E.4
Dirr, H.W.5
Shonhai, A.6
-
37
-
-
84942883615
-
Plasmodium falciparum Hop (PfHop) interacts with the Hsp70 chaperone in a nucleotide-dependent fashion and exhibits ligand selectivity
-
PID: 26267894
-
Zininga T, Makumire S, Gitau GW, Njunge JM, Pooe OJ, Klimek H, Scheurr R, Raifer H, Prinsloo E, Przyborski JM, Hoppe H, Shonhai A (2015b) Plasmodium falciparum Hop (PfHop) interacts with the Hsp70 chaperone in a nucleotide-dependent fashion and exhibits ligand selectivity. PLoS ONE 10, e0135326
-
(2015)
PLoS ONE
, vol.10
-
-
Zininga, T.1
Makumire, S.2
Gitau, G.W.3
Njunge, J.M.4
Pooe, O.J.5
Klimek, H.6
Scheurr, R.7
Raifer, H.8
Prinsloo, E.9
Przyborski, J.M.10
Hoppe, H.11
Shonhai, A.12
-
38
-
-
84921932367
-
Are heat shock proteins druggable candidates?
-
Zininga T, Shonhai A (2014) Are heat shock proteins druggable candidates? Am J Biochem Biotechnol 10:208–210
-
(2014)
Am J Biochem Biotechnol
, vol.10
, pp. 208-210
-
-
Zininga, T.1
Shonhai, A.2
|