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Showing 1 to 9 of 9 entries
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Fatty-acid synthesis in chloroplasts from mustard (Sinapis alba L.) cotyledons: formation of acetyl coenzyme A by intraplastid glycolytic enzymes and a pyruvate dehydrogenase complex.

Planta

Liedvogel B, Bäuerle R.
PMID: 24232754
Planta. 1986 Dec;169(4):481-9. doi: 10.1007/BF00392096.

Chloroplasts from the cotyledons of mustard (Sinapis alba L.) seedlings were isolated on Percoll gradients, and showed a high degree of intactness (92%) and purity as judged by electron microscopy and marker-enzyme analysis (cytoplasmic contamination lower than 0.4% on...

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Liedvogel B, Bäuerle R. Fatty-acid synthesis in chloroplasts from mustard (Sinapis alba L.) cotyledons: formation of acetyl coenzyme A by intraplastid glycolytic enzymes and a pyruvate dehydrogenase complex. Planta. 1986;169(4):481-9doi: 10.1007/BF00392096.
Liedvogel, B., & Bäuerle, R. (1986). Fatty-acid synthesis in chloroplasts from mustard (Sinapis alba L.) cotyledons: formation of acetyl coenzyme A by intraplastid glycolytic enzymes and a pyruvate dehydrogenase complex. Planta, 169(4), 481-9. https://doi.org/10.1007/BF00392096
Liedvogel, B, and Bäuerle, R. "Fatty-acid synthesis in chloroplasts from mustard (Sinapis alba L.) cotyledons: formation of acetyl coenzyme A by intraplastid glycolytic enzymes and a pyruvate dehydrogenase complex." Planta vol. 169,4 (1986): 481-9. doi: https://doi.org/10.1007/BF00392096
Liedvogel B, Bäuerle R. Fatty-acid synthesis in chloroplasts from mustard (Sinapis alba L.) cotyledons: formation of acetyl coenzyme A by intraplastid glycolytic enzymes and a pyruvate dehydrogenase complex. Planta. 1986 Dec;169(4):481-9. doi: 10.1007/BF00392096. PMID: 24232754.
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ENO1 silencing impaires hypoxia-induced gemcitabine chemoresistance associated with redox modulation in pancreatic cancer cells.

American journal of translational research

Wang L, Bi R, Yin H, Liu H, Li L.
PMID: 31396350
Am J Transl Res. 2019 Jul 15;11(7):4470-4480. eCollection 2019.

Resistance to Gemcitabine (GEM) is a crucial problem in treatment of pancreatic cancer. Many studies indicate the direct impact of glycolytic enzyme on chemoresistance. However, it still has not been known whether Enolase 1 (ENO1), a multifunctional glycolytic enzyme,...

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Wang L, Bi R, Yin H, et al. ENO1 silencing impaires hypoxia-induced gemcitabine chemoresistance associated with redox modulation in pancreatic cancer cells. Am J Transl Res. 2019;11(7):4470-4480
Wang, L., Bi, R., Yin, H., Liu, H., & Li, L. (2019). ENO1 silencing impaires hypoxia-induced gemcitabine chemoresistance associated with redox modulation in pancreatic cancer cells. American journal of translational research, 11(7), 4470-4480.
Wang, Lei, et al. "ENO1 silencing impaires hypoxia-induced gemcitabine chemoresistance associated with redox modulation in pancreatic cancer cells." American journal of translational research vol. 11,7 (2019): 4470-4480.
Wang L, Bi R, Yin H, Liu H, Li L. ENO1 silencing impaires hypoxia-induced gemcitabine chemoresistance associated with redox modulation in pancreatic cancer cells. Am J Transl Res. 2019 Jul 15;11(7):4470-4480. eCollection 2019. PMID: 31396350; PMCID: PMC6684912.
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Extract of Syzygium aromaticum suppress eEF1A protein expression and fungal growth.

Journal of applied microbiology

Wang Y, Ding Y, Wang S, Chen H, Zhang H, Chen W, Gu Z, Chen YQ.
PMID: 28445616
J Appl Microbiol. 2017 Jul;123(1):80-91. doi: 10.1111/jam.13478. Epub 2017 Jun 09.

AIMS: Clove extract has therapeutic potential as an antifungal drug, yet the mechanism of action remains ambiguous. Current study aimed to address the molecular process of the antifungal activity exerted by clove extract.METHODS AND RESULTS: The antifungal assay results...

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Wang Y, Ding Y, Wang S, et al. Extract of Syzygium aromaticum suppress eEF1A protein expression and fungal growth. J Appl Microbiol. 2017;123(1):80-91doi: 10.1111/jam.13478.
Wang, Y., Ding, Y., Wang, S., Chen, H., Zhang, H., Chen, W., Gu, Z., & Chen, Y. Q. (2017). Extract of Syzygium aromaticum suppress eEF1A protein expression and fungal growth. Journal of applied microbiology, 123(1), 80-91. https://doi.org/10.1111/jam.13478
Wang, Y, et al. "Extract of Syzygium aromaticum suppress eEF1A protein expression and fungal growth." Journal of applied microbiology vol. 123,1 (2017): 80-91. doi: https://doi.org/10.1111/jam.13478
Wang Y, Ding Y, Wang S, Chen H, Zhang H, Chen W, Gu Z, Chen YQ. Extract of Syzygium aromaticum suppress eEF1A protein expression and fungal growth. J Appl Microbiol. 2017 Jul;123(1):80-91. doi: 10.1111/jam.13478. Epub 2017 Jun 09. PMID: 28445616.
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Characteristics of S100B and Neuron Specific Enolase in Differentiating Acute Vertigo Cases with Central Cause; a Diagnostic Accuracy Study.

Archives of academic emergency medicine

Mozafari J, Motamed H, Masoumi K, Hanafi MG, Fahimi MA, Derakhshani Z, Ehyaie F.
PMID: 32021984
Arch Acad Emerg Med. 2019 Dec 28;8(1):e3. eCollection 2020.

INTRODUCTION: Differentiating central vertigo from peripheral ones poses a challenge to specialists. The present study aimed to examine the potential screening value of S100B and neuron-specific enolase (NSE) in this regard.METHODS: This prospective cross-sectional study recruited adult acute vertigo...

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Mozafari J, Motamed H, Masoumi K, et al. Characteristics of S100B and Neuron Specific Enolase in Differentiating Acute Vertigo Cases with Central Cause; a Diagnostic Accuracy Study. Arch Acad Emerg Med. 2019;8(1):e3
Mozafari, J., Motamed, H., Masoumi, K., Hanafi, M. G., Fahimi, M. A., Derakhshani, Z., & Ehyaie, F. (2020). Characteristics of S100B and Neuron Specific Enolase in Differentiating Acute Vertigo Cases with Central Cause; a Diagnostic Accuracy Study. Archives of academic emergency medicine, 8(1), e3.
Mozafari, Javad, et al. "Characteristics of S100B and Neuron Specific Enolase in Differentiating Acute Vertigo Cases with Central Cause; a Diagnostic Accuracy Study." Archives of academic emergency medicine vol. 8,1 (2020): e3.
Mozafari J, Motamed H, Masoumi K, Hanafi MG, Fahimi MA, Derakhshani Z, Ehyaie F. Characteristics of S100B and Neuron Specific Enolase in Differentiating Acute Vertigo Cases with Central Cause; a Diagnostic Accuracy Study. Arch Acad Emerg Med. 2019 Dec 28;8(1):e3. eCollection 2020. PMID: 32021984; PMCID: PMC6946037.
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Co-opting of nonATP-generating glycolytic enzymes for TBSV replication.

Virology

Molho M, Chuang C, Nagy PD.
PMID: 33799077
Virology. 2021 Jul;559:15-29. doi: 10.1016/j.virol.2021.03.011. Epub 2021 Mar 22.

Positive-strand RNA viruses build viral replication organelles (VROs) with the help of co-opted host factors. The energy requirement of intensive viral replication processes is less understood. Previous studies on tomato bushy stunt virus (TBSV) showed that tombusviruses hijack two...

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Molho M, Chuang C, Nagy PD. Co-opting of nonATP-generating glycolytic enzymes for TBSV replication. Virology. 2021;559:15-29doi: 10.1016/j.virol.2021.03.011.
Molho, M., Chuang, C., & Nagy, P. D. (2021). Co-opting of nonATP-generating glycolytic enzymes for TBSV replication. Virology, 55915-29. https://doi.org/10.1016/j.virol.2021.03.011
Molho, Melissa, et al. "Co-opting of nonATP-generating glycolytic enzymes for TBSV replication." Virology vol. 559 (2021): 15-29. doi: https://doi.org/10.1016/j.virol.2021.03.011
Molho M, Chuang C, Nagy PD. Co-opting of nonATP-generating glycolytic enzymes for TBSV replication. Virology. 2021 Jul;559:15-29. doi: 10.1016/j.virol.2021.03.011. Epub 2021 Mar 22. PMID: 33799077.
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Comparison of Prognostic Performance between Neuron-Specific Enolase and S100 Calcium-Binding Protein B Obtained from the Cerebrospinal Fluid of Out-of-Hospital Cardiac Arrest Survivors Who Underwent Targeted Temperature Management.

Journal of clinical medicine

Kang C, Jeong W, Park JS, You Y, Min JH, Cho YC, Ahn HJ.
PMID: 33917473
J Clin Med. 2021 Apr 06;10(7). doi: 10.3390/jcm10071531.

We compared the prognostic performances of serum neuron-specific enolase (sNSE), cerebrospinal fluid (CSF) NSE (cNSE), and CSF S100 calcium-binding protein B (cS100B) in out-of-hospital cardiac arrest (OHCA) survivors. This prospective observational study enrolled 45 patients. All samples were obtained...

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Kang C, Jeong W, Park JS, et al. Comparison of Prognostic Performance between Neuron-Specific Enolase and S100 Calcium-Binding Protein B Obtained from the Cerebrospinal Fluid of Out-of-Hospital Cardiac Arrest Survivors Who Underwent Targeted Temperature Management. J Clin Med. 2021;10(7)doi: 10.3390/jcm10071531.
Kang, C., Jeong, W., Park, J. S., You, Y., Min, J. H., Cho, Y. C., & Ahn, H. J. (2021). Comparison of Prognostic Performance between Neuron-Specific Enolase and S100 Calcium-Binding Protein B Obtained from the Cerebrospinal Fluid of Out-of-Hospital Cardiac Arrest Survivors Who Underwent Targeted Temperature Management. Journal of clinical medicine, 10(7), . https://doi.org/10.3390/jcm10071531
Kang, Changshin, et al. "Comparison of Prognostic Performance between Neuron-Specific Enolase and S100 Calcium-Binding Protein B Obtained from the Cerebrospinal Fluid of Out-of-Hospital Cardiac Arrest Survivors Who Underwent Targeted Temperature Management." Journal of clinical medicine vol. 10,7 (2021). doi: https://doi.org/10.3390/jcm10071531
Kang C, Jeong W, Park JS, You Y, Min JH, Cho YC, Ahn HJ. Comparison of Prognostic Performance between Neuron-Specific Enolase and S100 Calcium-Binding Protein B Obtained from the Cerebrospinal Fluid of Out-of-Hospital Cardiac Arrest Survivors Who Underwent Targeted Temperature Management. J Clin Med. 2021 Apr 06;10(7). doi: 10.3390/jcm10071531. PMID: 33917473; PMCID: PMC8038742.
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Rearrangement of enzyme patterns in maize callus and suspension cultures : Is it relevant to the changes in the growing cells of the intact plant?.

Planta

Zeleneva IV, Khavkin EE.
PMID: 24309697
Planta. 1980 Mar;148(2):108-15. doi: 10.1007/BF00386410.

The development of enzyme patterns was followed in the course of: (a) the irreversible cell differentiation via division and expansion to maturity in the root tip and coleoptile of the intact seedlings, (b) the irreversible cell dedifferentation associated with...

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Zeleneva IV, Khavkin EE. Rearrangement of enzyme patterns in maize callus and suspension cultures : Is it relevant to the changes in the growing cells of the intact plant?. Planta. 1980;148(2):108-15doi: 10.1007/BF00386410.
Zeleneva, I. V., & Khavkin, E. E. (1980). Rearrangement of enzyme patterns in maize callus and suspension cultures : Is it relevant to the changes in the growing cells of the intact plant?. Planta, 148(2), 108-15. https://doi.org/10.1007/BF00386410
Zeleneva, I V, and Khavkin, E E. "Rearrangement of enzyme patterns in maize callus and suspension cultures : Is it relevant to the changes in the growing cells of the intact plant?." Planta vol. 148,2 (1980): 108-15. doi: https://doi.org/10.1007/BF00386410
Zeleneva IV, Khavkin EE. Rearrangement of enzyme patterns in maize callus and suspension cultures : Is it relevant to the changes in the growing cells of the intact plant?. Planta. 1980 Mar;148(2):108-15. doi: 10.1007/BF00386410. PMID: 24309697.
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Co-opting of nonATP-generating glycolytic enzymes for TBSV replication.

Virology

Molho M, Chuang C, Nagy PD.
PMID: 33799077
Virology. 2021 Jul;559:15-29. doi: 10.1016/j.virol.2021.03.011. Epub 2021 Mar 22.

Positive-strand RNA viruses build viral replication organelles (VROs) with the help of co-opted host factors. The energy requirement of intensive viral replication processes is less understood. Previous studies on tomato bushy stunt virus (TBSV) showed that tombusviruses hijack two...

Cite
Molho M, Chuang C, Nagy PD. Co-opting of nonATP-generating glycolytic enzymes for TBSV replication. Virology. 2021;559:15-29doi: 10.1016/j.virol.2021.03.011.
Molho, M., Chuang, C., & Nagy, P. D. (2021). Co-opting of nonATP-generating glycolytic enzymes for TBSV replication. Virology, 55915-29. https://doi.org/10.1016/j.virol.2021.03.011
Molho, Melissa, et al. "Co-opting of nonATP-generating glycolytic enzymes for TBSV replication." Virology vol. 559 (2021): 15-29. doi: https://doi.org/10.1016/j.virol.2021.03.011
Molho M, Chuang C, Nagy PD. Co-opting of nonATP-generating glycolytic enzymes for TBSV replication. Virology. 2021 Jul;559:15-29. doi: 10.1016/j.virol.2021.03.011. Epub 2021 Mar 22. PMID: 33799077.
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Candidate antigens specifically detected by cerebrospinal fluid-IgG in oligoclonal IgG bands-positive multiple sclerosis patients.

Proteomics. Clinical applications

Nakamura M, Kuramasu A, Nakashima I, Fujihara K, Itoyama Y.
PMID: 21136723
Proteomics Clin Appl. 2007 Jul;1(7):681-7. doi: 10.1002/prca.200700182. Epub 2007 Jun 08.

The aim of the present study was to detect antigenic proteins that react specifically with cerebrospinal fluid (CSF)-IgG from oligoclonal IgG bands (OB)-positive multiple sclerosis (MS) patients. To identify such antigenic proteins, we developed a rat brain proteome map...

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Nakamura M, Kuramasu A, Nakashima I, et al. Candidate antigens specifically detected by cerebrospinal fluid-IgG in oligoclonal IgG bands-positive multiple sclerosis patients. Proteomics Clin Appl. 2007;1(7):681-7doi: 10.1002/prca.200700182.
Nakamura, M., Kuramasu, A., Nakashima, I., Fujihara, K., & Itoyama, Y. (2007). Candidate antigens specifically detected by cerebrospinal fluid-IgG in oligoclonal IgG bands-positive multiple sclerosis patients. Proteomics. Clinical applications, 1(7), 681-7. https://doi.org/10.1002/prca.200700182
Nakamura, Masashi, et al. "Candidate antigens specifically detected by cerebrospinal fluid-IgG in oligoclonal IgG bands-positive multiple sclerosis patients." Proteomics. Clinical applications vol. 1,7 (2007): 681-7. doi: https://doi.org/10.1002/prca.200700182
Nakamura M, Kuramasu A, Nakashima I, Fujihara K, Itoyama Y. Candidate antigens specifically detected by cerebrospinal fluid-IgG in oligoclonal IgG bands-positive multiple sclerosis patients. Proteomics Clin Appl. 2007 Jul;1(7):681-7. doi: 10.1002/prca.200700182. Epub 2007 Jun 08. PMID: 21136723.
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Showing 1 to 9 of 9 entries