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Proteomic analysis of differentially expressed proteins induced by salicylic acid in suspension-cultured ginseng cells.

Saudi journal of biological sciences

Sun J, Fu J, Zhou R.
PMID: 24600313
Saudi J Biol Sci. 2014 Apr;21(2):185-90. doi: 10.1016/j.sjbs.2013.09.011. Epub 2013 Oct 09.

In this study, optimized 2-DE sample preparation methodologies were established for suspension-cultured ginseng cells. Three commonly used protein extraction methods (Trichloroacetic acid-acetone, urea/thiourea and phenol extraction method) were evaluated for proteomic analysis of suspension cultures of ginseng. A comparative...

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Sun J, Fu J, Zhou R. Proteomic analysis of differentially expressed proteins induced by salicylic acid in suspension-cultured ginseng cells. Saudi J Biol Sci. 2013;21(2):185-90doi: 10.1016/j.sjbs.2013.09.011.
Sun, J., Fu, J., & Zhou, R. (2014). Proteomic analysis of differentially expressed proteins induced by salicylic acid in suspension-cultured ginseng cells. Saudi journal of biological sciences, 21(2), 185-90. https://doi.org/10.1016/j.sjbs.2013.09.011
Sun, Jiaman, et al. "Proteomic analysis of differentially expressed proteins induced by salicylic acid in suspension-cultured ginseng cells." Saudi journal of biological sciences vol. 21,2 (2014): 185-90. doi: https://doi.org/10.1016/j.sjbs.2013.09.011
Sun J, Fu J, Zhou R. Proteomic analysis of differentially expressed proteins induced by salicylic acid in suspension-cultured ginseng cells. Saudi J Biol Sci. 2014 Apr;21(2):185-90. doi: 10.1016/j.sjbs.2013.09.011. Epub 2013 Oct 09. PMID: 24600313; PMCID: PMC3942860.
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Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120 : Presence in vegetative cells and heterocysts.

Planta

Jāger KM, Bergman B.
PMID: 24193540
Planta. 1991 Dec;183(1):120-5. doi: 10.1007/BF00197575.

The occurrence and distribution of a multifunctional chaperonin-60 (cpn60), the GroEL protein, was demonstrated in the cyanobacterium Anabaena PCC 7120 by using a rabbit anti-GroEL (Escherichia coli) antibody. Western-blot analysis showed a distinct cross-reaction with a protein of approx....

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Jāger KM, Bergman B. Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120 : Presence in vegetative cells and heterocysts. Planta. 1991;183(1):120-5doi: 10.1007/BF00197575.
Jāger, K. M., & Bergman, B. (1991). Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120 : Presence in vegetative cells and heterocysts. Planta, 183(1), 120-5. https://doi.org/10.1007/BF00197575
Jāger, K M, and Bergman, B. "Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120 : Presence in vegetative cells and heterocysts." Planta vol. 183,1 (1991): 120-5. doi: https://doi.org/10.1007/BF00197575
Jāger KM, Bergman B. Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120 : Presence in vegetative cells and heterocysts. Planta. 1991 Dec;183(1):120-5. doi: 10.1007/BF00197575. PMID: 24193540.
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Correction: Chaperonin 60 sustains osteoblast autophagy and counteracts glucocorticoid aggravation of osteoporosis by chaperoning RPTOR.

Cell death & disease

Lian WS, Ko JY, Chen YS, Ke HC, Wu SL, Kuo CW, Wang FS.
PMID: 31582745
Cell Death Dis. 2019 Oct 03;10(10):741. doi: 10.1038/s41419-019-1991-5.

Following publication of this article, the authors realized that there were 1) errors made in the author affiliations and that 2) a typo in a grant number needed to be corrected. The corrected author affiliations and grant numbers are...

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Lian WS, Ko JY, Chen YS, et al. Correction: Chaperonin 60 sustains osteoblast autophagy and counteracts glucocorticoid aggravation of osteoporosis by chaperoning RPTOR. Cell Death Dis. 2019;10(10):741doi: 10.1038/s41419-019-1991-5.
Lian, W. S., Ko, J. Y., Chen, Y. S., Ke, H. C., Wu, S. L., Kuo, C. W., & Wang, F. S. (2019). Correction: Chaperonin 60 sustains osteoblast autophagy and counteracts glucocorticoid aggravation of osteoporosis by chaperoning RPTOR. Cell death & disease, 10(10), 741. https://doi.org/10.1038/s41419-019-1991-5
Lian, Wei-Shiung, et al. "Correction: Chaperonin 60 sustains osteoblast autophagy and counteracts glucocorticoid aggravation of osteoporosis by chaperoning RPTOR." Cell death & disease vol. 10,10 (2019): 741. doi: https://doi.org/10.1038/s41419-019-1991-5
Lian WS, Ko JY, Chen YS, Ke HC, Wu SL, Kuo CW, Wang FS. Correction: Chaperonin 60 sustains osteoblast autophagy and counteracts glucocorticoid aggravation of osteoporosis by chaperoning RPTOR. Cell Death Dis. 2019 Oct 03;10(10):741. doi: 10.1038/s41419-019-1991-5. PMID: 31582745; PMCID: PMC6776642.
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Comparative Proteome Analysis of Wheat Flag Leaves and Developing Grains Under Water Deficit.

Frontiers in plant science

Deng X, Liu Y, Xu X, Liu D, Zhu G, Yan X, Wang Z, Yan Y.
PMID: 29692790
Front Plant Sci. 2018 Apr 10;9:425. doi: 10.3389/fpls.2018.00425. eCollection 2018.

In this study, we performed the first comparative proteomic analysis of wheat flag leaves and developing grains in response to drought stress. Drought stress caused a significant decrease in several important physiological and biochemical parameters and grain yield traits,...

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Deng X, Liu Y, Xu X, et al. Comparative Proteome Analysis of Wheat Flag Leaves and Developing Grains Under Water Deficit. Front Plant Sci. 2018;9:425doi: 10.3389/fpls.2018.00425.
Deng, X., Liu, Y., Xu, X., Liu, D., Zhu, G., Yan, X., Wang, Z., & Yan, Y. (2018). Comparative Proteome Analysis of Wheat Flag Leaves and Developing Grains Under Water Deficit. Frontiers in plant science, 9425. https://doi.org/10.3389/fpls.2018.00425
Deng, Xiong, et al. "Comparative Proteome Analysis of Wheat Flag Leaves and Developing Grains Under Water Deficit." Frontiers in plant science vol. 9 (2018): 425. doi: https://doi.org/10.3389/fpls.2018.00425
Deng X, Liu Y, Xu X, Liu D, Zhu G, Yan X, Wang Z, Yan Y. Comparative Proteome Analysis of Wheat Flag Leaves and Developing Grains Under Water Deficit. Front Plant Sci. 2018 Apr 10;9:425. doi: 10.3389/fpls.2018.00425. eCollection 2018. PMID: 29692790; PMCID: PMC5902686.
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Toward a better understanding of preeclampsia: Comparative proteomic analysis of preeclamptic placentas.

Proteomics. Clinical applications

Kim YN, Kim HK, Warda M, Kim N, Park WS, Prince Adel B, Jeong DH, Lee DS, Kim KT, Han J.
PMID: 21136660
Proteomics Clin Appl. 2007 Dec;1(12):1625-36. doi: 10.1002/prca.200700034. Epub 2007 Nov 16.

Preeclampsia (PE), a pregnancy-specific syndrome of hypertension, proteinuria, and other systemic disturbances, is a state of widespread endothelial dysfunction secondary to defective placentation. Morphologically, the current data displayed degenerative and apoptotic changes in the mitochondria and villous trophoblasts of...

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Kim YN, Kim HK, Warda M, et al. Toward a better understanding of preeclampsia: Comparative proteomic analysis of preeclamptic placentas. Proteomics Clin Appl. 2007;1(12):1625-36doi: 10.1002/prca.200700034.
Kim, Y. N., Kim, H. K., Warda, M., Kim, N., Park, W. S., Prince, A. d. e. l. . B., Jeong, D. H., Lee, D. S., Kim, K. T., & Han, J. (2007). Toward a better understanding of preeclampsia: Comparative proteomic analysis of preeclamptic placentas. Proteomics. Clinical applications, 1(12), 1625-36. https://doi.org/10.1002/prca.200700034
Kim, Young Nam, et al. "Toward a better understanding of preeclampsia: Comparative proteomic analysis of preeclamptic placentas." Proteomics. Clinical applications vol. 1,12 (2007): 1625-36. doi: https://doi.org/10.1002/prca.200700034
Kim YN, Kim HK, Warda M, Kim N, Park WS, Prince Adel B, Jeong DH, Lee DS, Kim KT, Han J. Toward a better understanding of preeclampsia: Comparative proteomic analysis of preeclamptic placentas. Proteomics Clin Appl. 2007 Dec;1(12):1625-36. doi: 10.1002/prca.200700034. Epub 2007 Nov 16. PMID: 21136660.
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Editorial: Type I Chaperonins: Mechanism and Beyond.

Frontiers in molecular biosciences

Breiman A, Azem A.
PMID: 30131963
Front Mol Biosci. 2018 Jul 31;5:72. doi: 10.3389/fmolb.2018.00072. eCollection 2018.

No abstract available.

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Breiman A, Azem A. Editorial: Type I Chaperonins: Mechanism and Beyond. Front Mol Biosci. 2018;5:72doi: 10.3389/fmolb.2018.00072.
Breiman, A., & Azem, A. (2018). Editorial: Type I Chaperonins: Mechanism and Beyond. Frontiers in molecular biosciences, 572. https://doi.org/10.3389/fmolb.2018.00072
Breiman, Adina, and Azem, Abdussalam. "Editorial: Type I Chaperonins: Mechanism and Beyond." Frontiers in molecular biosciences vol. 5 (2018): 72. doi: https://doi.org/10.3389/fmolb.2018.00072
Breiman A, Azem A. Editorial: Type I Chaperonins: Mechanism and Beyond. Front Mol Biosci. 2018 Jul 31;5:72. doi: 10.3389/fmolb.2018.00072. eCollection 2018. PMID: 30131963; PMCID: PMC6090153.
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Detection of blueberry stunt phytoplasma in Eastern Canada using cpn60-based molecular diagnostic assays.

Scientific reports

Hammond C, Pérez-López E, Town J, Vincent C, Moreau D, Dumonceaux T.
PMID: 34764366
Sci Rep. 2021 Nov 11;11(1):22118. doi: 10.1038/s41598-021-01439-4.

Blueberry stunt phytoplasma (BBSP; 'Candidatus Phytoplasma asteris') is an insect-vectored plant pathogen that causes severe yield losses in blueberry (Vaccinium corymbosum), which is the most valuable fruit crop in Canada. Rapid, field-based diagnostic assays are desirable tools for the...

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Hammond C, Pérez-López E, Town J, et al. Detection of blueberry stunt phytoplasma in Eastern Canada using cpn60-based molecular diagnostic assays. Sci Rep. 2021;11(1):22118doi: 10.1038/s41598-021-01439-4.
Hammond, C., Pérez-López, E., Town, J., Vincent, C., Moreau, D., & Dumonceaux, T. (2021). Detection of blueberry stunt phytoplasma in Eastern Canada using cpn60-based molecular diagnostic assays. Scientific reports, 11(1), 22118. https://doi.org/10.1038/s41598-021-01439-4
Hammond, Christine, et al. "Detection of blueberry stunt phytoplasma in Eastern Canada using cpn60-based molecular diagnostic assays." Scientific reports vol. 11,1 (2021): 22118. doi: https://doi.org/10.1038/s41598-021-01439-4
Hammond C, Pérez-López E, Town J, Vincent C, Moreau D, Dumonceaux T. Detection of blueberry stunt phytoplasma in Eastern Canada using cpn60-based molecular diagnostic assays. Sci Rep. 2021 Nov 11;11(1):22118. doi: 10.1038/s41598-021-01439-4. PMID: 34764366; PMCID: PMC8586236.
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Characterization of Thylakoid-Derived Lipid-Protein Particles Bearing the Large Subunit of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase.

Plant physiology

Smith MD, Ghosh S, Dumbroff EB, Thompson JE.
PMID: 12223858
Plant Physiol. 1997 Nov;115(3):1073-1082. doi: 10.1104/pp.115.3.1073.

Lipid-protein particles bearing the 55-kD ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) (EC 4.1.1.39) large subunit (RLSU) and no detectable corresponding Rubisco small subunit (RSSU) were isolated from the stroma of intact chloroplasts by flotation centrifugation. Stromal RLSU-bearing particles appear to originate from...

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Smith MD, Ghosh S, Dumbroff EB, et al. Characterization of Thylakoid-Derived Lipid-Protein Particles Bearing the Large Subunit of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase. Plant Physiol. 1997;115(3):1073-1082doi: 10.1104/pp.115.3.1073.
Smith, M. D., Ghosh, S., Dumbroff, E. B., & Thompson, J. E. (1997). Characterization of Thylakoid-Derived Lipid-Protein Particles Bearing the Large Subunit of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase. Plant physiology, 115(3), 1073-1082. https://doi.org/10.1104/pp.115.3.1073
Smith, M. D., et al. "Characterization of Thylakoid-Derived Lipid-Protein Particles Bearing the Large Subunit of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase." Plant physiology vol. 115,3 (1997): 1073-1082. doi: https://doi.org/10.1104/pp.115.3.1073
Smith MD, Ghosh S, Dumbroff EB, Thompson JE. Characterization of Thylakoid-Derived Lipid-Protein Particles Bearing the Large Subunit of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase. Plant Physiol. 1997 Nov;115(3):1073-1082. doi: 10.1104/pp.115.3.1073. PMID: 12223858; PMCID: PMC158571.
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Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones.

Expert reviews in molecular medicine

Ranford JC, Coates AR, Henderson B.
PMID: 14585136
Expert Rev Mol Med. 2000 Sep 15;2(8):1-17. doi: 10.1017/S1462399400002015.

The chaperonins are a subgroup of oligomeric molecular chaperones; the best-studied examples are chaperonin 60 (GroEL) and chaperonin 10 (GroES), both from the bacterium Escherichia coli. At the end of the 20th century, the paradigm of chaperonins as protein...

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Ranford JC, Coates AR, Henderson B. Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones. Expert Rev Mol Med. 2000;2(8):1-17doi: 10.1017/S1462399400002015.
Ranford, J. C., Coates, A. R., & Henderson, B. (2000). Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones. Expert reviews in molecular medicine, 2(8), 1-17. https://doi.org/10.1017/S1462399400002015
Ranford, J C, et al. "Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones." Expert reviews in molecular medicine vol. 2,8 (2000): 1-17. doi: https://doi.org/10.1017/S1462399400002015
Ranford JC, Coates AR, Henderson B. Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones. Expert Rev Mol Med. 2000 Sep 15;2(8):1-17. doi: 10.1017/S1462399400002015. PMID: 14585136.
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ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

Current biology : CB

Saibil HR, Zheng D, Roseman AM, Hunter AS, Watson GM, Chen S, Auf Der Mauer A, O'Hara BP, Wood SP, Mann NH, Barnett LK, Ellis RJ.
PMID: 15335746
Curr Biol. 1993 May 01;3(5):265-73. doi: 10.1016/0960-9822(93)90176-o.

BACKGROUND: The chaperonins, a family of molecular chaperones, are large oligomeric proteins that bind nonnative intermediates of protein folding. They couple the release and correct folding of their ligands to the binding and hydrolysis of ATP. Chaperonin 60 (cpn60)...

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Saibil HR, Zheng D, Roseman AM, et al. ATP induces large quaternary rearrangements in a cage-like chaperonin structure. Curr Biol. 1993;3(5):265-73doi: 10.1016/0960-9822(93)90176-o.
Saibil, H. R., Zheng, D., Roseman, A. M., Hunter, A. S., Watson, G. M., Chen, S., Auf Der Mauer, A., O'Hara, B. P., Wood, S. P., Mann, N. H., Barnett, L. K., & Ellis, R. J. (1993). ATP induces large quaternary rearrangements in a cage-like chaperonin structure. Current biology : CB, 3(5), 265-73. https://doi.org/10.1016/0960-9822(93)90176-o
Saibil, H R, et al. "ATP induces large quaternary rearrangements in a cage-like chaperonin structure." Current biology : CB vol. 3,5 (1993): 265-73. doi: https://doi.org/10.1016/0960-9822(93)90176-o
Saibil HR, Zheng D, Roseman AM, Hunter AS, Watson GM, Chen S, Auf Der Mauer A, O'Hara BP, Wood SP, Mann NH, Barnett LK, Ellis RJ. ATP induces large quaternary rearrangements in a cage-like chaperonin structure. Curr Biol. 1993 May 01;3(5):265-73. doi: 10.1016/0960-9822(93)90176-o. PMID: 15335746.
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Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding.

Scientific reports

Nguyen B, Ma R, Tang WK, Shi D, Tolia NH.
PMID: 33723304
Sci Rep. 2021 Mar 15;11(1):5930. doi: 10.1038/s41598-021-85197-3.

Plasmodium falciparum harbors group 1 and group 2 chaperonin systems to mediate the folding of cellular proteins in different cellular locations. Two distinct group 1 chaperonins operate in the organelles of mitochondria and apicoplasts, while group 2 chaperonins function...

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Nguyen B, Ma R, Tang WK, et al. Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding. Sci Rep. 2021;11(1):5930doi: 10.1038/s41598-021-85197-3.
Nguyen, B., Ma, R., Tang, W. K., Shi, D., & Tolia, N. H. (2021). Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding. Scientific reports, 11(1), 5930. https://doi.org/10.1038/s41598-021-85197-3
Nguyen, Brian, et al. "Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding." Scientific reports vol. 11,1 (2021): 5930. doi: https://doi.org/10.1038/s41598-021-85197-3
Nguyen B, Ma R, Tang WK, Shi D, Tolia NH. Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding. Sci Rep. 2021 Mar 15;11(1):5930. doi: 10.1038/s41598-021-85197-3. PMID: 33723304; PMCID: PMC7960994.
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Assembly of in Vitro-Synthesized Large Subunits into Ribulose Bisphosphate Carboxylase/Oxygenase Is Sensitive to CI-, Requires ATP, and Does Not Proceed When Large Subunits Are Synthesized at Temperatures [greater than or equal to]32[deg]C.

Plant physiology

Hubbs AE, Roy H.
PMID: 12231707
Plant Physiol. 1993 Feb;101(2):523-533. doi: 10.1104/pp.101.2.523.

In higher plants, ribulose bisphosphate carboxylase/oxygenase (Rubisco) consists of eight large "L" subunits, synthesized in chloroplasts, and eight small "S" subunits, synthesized as precursors in the cytosol. Assembly of these into holoenzyme occurs in the chloroplast stroma after import...

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Hubbs AE, Roy H. Assembly of in Vitro-Synthesized Large Subunits into Ribulose Bisphosphate Carboxylase/Oxygenase Is Sensitive to CI-, Requires ATP, and Does Not Proceed When Large Subunits Are Synthesized at Temperatures [greater than or equal to]32[deg]C. Plant Physiol. 1993;101(2):523-533doi: 10.1104/pp.101.2.523.
Hubbs, A. E., & Roy, H. (1993). Assembly of in Vitro-Synthesized Large Subunits into Ribulose Bisphosphate Carboxylase/Oxygenase Is Sensitive to CI-, Requires ATP, and Does Not Proceed When Large Subunits Are Synthesized at Temperatures [greater than or equal to]32[deg]C. Plant physiology, 101(2), 523-533. https://doi.org/10.1104/pp.101.2.523
Hubbs, A. E., and Roy, H.. "Assembly of in Vitro-Synthesized Large Subunits into Ribulose Bisphosphate Carboxylase/Oxygenase Is Sensitive to CI-, Requires ATP, and Does Not Proceed When Large Subunits Are Synthesized at Temperatures [greater than or equal to]32[deg]C." Plant physiology vol. 101,2 (1993): 523-533. doi: https://doi.org/10.1104/pp.101.2.523
Hubbs AE, Roy H. Assembly of in Vitro-Synthesized Large Subunits into Ribulose Bisphosphate Carboxylase/Oxygenase Is Sensitive to CI-, Requires ATP, and Does Not Proceed When Large Subunits Are Synthesized at Temperatures [greater than or equal to]32[deg]C. Plant Physiol. 1993 Feb;101(2):523-533. doi: 10.1104/pp.101.2.523. PMID: 12231707; PMCID: PMC160600.
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