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Biomarker-based score for predicting in-hospital mortality of children admitted to the intensive care unit.

Journal of investigative medicine : the official publication of the American Federation for Clinical Research

Zhang Y, Shi Q, Zhong G, Lei X, Lin J, Fu Z, Dai J.
PMID: 34226249
J Investig Med. 2021 Dec;69(8):1458-1463. doi: 10.1136/jim-2021-001855. Epub 2021 Jul 05.

This study aims to establish a new scoring system based on biomarkers for predicting in-hospital mortality of children admitted to the pediatric intensive care unit (PICU). The biomarkers were chosen using the least absolute shrinkage and selection operator (LASSO)-logistic...

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Zhang Y, Shi Q, Zhong G, et al. Biomarker-based score for predicting in-hospital mortality of children admitted to the intensive care unit. J Investig Med. 2021;69(8):1458-1463doi: 10.1136/jim-2021-001855.
Zhang, Y., Shi, Q., Zhong, G., Lei, X., Lin, J., Fu, Z., & Dai, J. (2021). Biomarker-based score for predicting in-hospital mortality of children admitted to the intensive care unit. Journal of investigative medicine : the official publication of the American Federation for Clinical Research, 69(8), 1458-1463. https://doi.org/10.1136/jim-2021-001855
Zhang, Yin, et al. "Biomarker-based score for predicting in-hospital mortality of children admitted to the intensive care unit." Journal of investigative medicine : the official publication of the American Federation for Clinical Research vol. 69,8 (2021): 1458-1463. doi: https://doi.org/10.1136/jim-2021-001855
Zhang Y, Shi Q, Zhong G, Lei X, Lin J, Fu Z, Dai J. Biomarker-based score for predicting in-hospital mortality of children admitted to the intensive care unit. J Investig Med. 2021 Dec;69(8):1458-1463. doi: 10.1136/jim-2021-001855. Epub 2021 Jul 05. PMID: 34226249.
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Protein Conformational Landscapes and Catalysis. Influence of Active Site Conformations in the Reaction Catalyzed by L-Lactate Dehydrogenase.

ACS catalysis

Świderek K, Tuñón I, Martí S, Moliner V.
PMID: 25705562
ACS Catal. 2015 Jan 07;5(4):1172-1185. doi: 10.1021/cs501704f.

In the last decade L-Lactate Dehydrogenase (LDH) has become an extremely useful marker in both clinical diagnosis and in monitoring the course of many human diseases. It has been assumed from the 80s that the full catalytic process of...

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Świderek K, Tuñón I, Martí S, et al. Protein Conformational Landscapes and Catalysis. Influence of Active Site Conformations in the Reaction Catalyzed by L-Lactate Dehydrogenase. ACS Catal. 2015;5(4):1172-1185doi: 10.1021/cs501704f.
Świderek, K., Tuñón, I., Martí, S., & Moliner, V. (2015). Protein Conformational Landscapes and Catalysis. Influence of Active Site Conformations in the Reaction Catalyzed by L-Lactate Dehydrogenase. ACS catalysis, 5(4), 1172-1185. https://doi.org/10.1021/cs501704f
Świderek, Katarzyna, et al. "Protein Conformational Landscapes and Catalysis. Influence of Active Site Conformations in the Reaction Catalyzed by L-Lactate Dehydrogenase." ACS catalysis vol. 5,4 (2015): 1172-1185. doi: https://doi.org/10.1021/cs501704f
Świderek K, Tuñón I, Martí S, Moliner V. Protein Conformational Landscapes and Catalysis. Influence of Active Site Conformations in the Reaction Catalyzed by L-Lactate Dehydrogenase. ACS Catal. 2015 Jan 07;5(4):1172-1185. doi: 10.1021/cs501704f. PMID: 25705562; PMCID: PMC4333743.
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An alternative allosteric regulation mechanism of an acidophilic l-lactate dehydrogenase from Enterococcus mundtii 15-1A.

FEBS open bio

Matoba Y, Miyasako M, Matsuo K, Oda K, Noda M, Higashikawa F, Kumagai T, Sugiyama M.
PMID: 25379380
FEBS Open Bio. 2014 Sep 06;4:834-47. doi: 10.1016/j.fob.2014.08.006. eCollection 2014.

A plant-derived Enterococcus mundtii 15-1A, that has been previously isolated from Brassica rapa L. subsp. nipposinica (L.H. Bailey) Hanelt var. linearifolia by our group, possesses two kinds of l-lactate dehydrogenase (l-LDH): LDH-1 and LDH-2. LDH-1 was activated under low...

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Matoba Y, Miyasako M, Matsuo K, et al. An alternative allosteric regulation mechanism of an acidophilic l-lactate dehydrogenase from Enterococcus mundtii 15-1A. FEBS Open Bio. 2014;4:834-47doi: 10.1016/j.fob.2014.08.006.
Matoba, Y., Miyasako, M., Matsuo, K., Oda, K., Noda, M., Higashikawa, F., Kumagai, T., & Sugiyama, M. (2014). An alternative allosteric regulation mechanism of an acidophilic l-lactate dehydrogenase from Enterococcus mundtii 15-1A. FEBS open bio, 4834-47. https://doi.org/10.1016/j.fob.2014.08.006
Matoba, Yasuyuki, et al. "An alternative allosteric regulation mechanism of an acidophilic l-lactate dehydrogenase from Enterococcus mundtii 15-1A." FEBS open bio vol. 4 (2014): 834-47. doi: https://doi.org/10.1016/j.fob.2014.08.006
Matoba Y, Miyasako M, Matsuo K, Oda K, Noda M, Higashikawa F, Kumagai T, Sugiyama M. An alternative allosteric regulation mechanism of an acidophilic l-lactate dehydrogenase from Enterococcus mundtii 15-1A. FEBS Open Bio. 2014 Sep 06;4:834-47. doi: 10.1016/j.fob.2014.08.006. eCollection 2014. PMID: 25379380; PMCID: PMC4219987.
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Enzymatic Determination of Citric Acid in Honey by Using Polyvinylpolypyrrolidone Clarification.

Journal of agricultural and food chemistry

Mato I, Huidobro JF, Cendón V, Muniategui S, Fernández-Muiño MA, Sancho MT.
PMID: 10554209
J Agric Food Chem. 1998 Jan 19;46(1):141-144. doi: 10.1021/jf970418p.

To characterize honey types, a citric acid determination may be useful. A citric acid determination on honey was carried out with previous polyvinylpolypyrrolidone (PVPP) clarification followed by the Boehringer-Mannheim GmbH enzymatic test. The sample solution was prepared from 2...

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Mato I, Huidobro JF, Cendón V, et al. Enzymatic Determination of Citric Acid in Honey by Using Polyvinylpolypyrrolidone Clarification. J Agric Food Chem. 1998;46(1):141-144doi: 10.1021/jf970418p.
Mato, I., Huidobro, J. F., Cendón, V., Muniategui, S., Fernández-Muiño, M. A., & Sancho, M. T. (1998). Enzymatic Determination of Citric Acid in Honey by Using Polyvinylpolypyrrolidone Clarification. Journal of agricultural and food chemistry, 46(1), 141-144. https://doi.org/10.1021/jf970418p
Mato, et al. "Enzymatic Determination of Citric Acid in Honey by Using Polyvinylpolypyrrolidone Clarification." Journal of agricultural and food chemistry vol. 46,1 (1998): 141-144. doi: https://doi.org/10.1021/jf970418p
Mato I, Huidobro JF, Cendón V, Muniategui S, Fernández-Muiño MA, Sancho MT. Enzymatic Determination of Citric Acid in Honey by Using Polyvinylpolypyrrolidone Clarification. J Agric Food Chem. 1998 Jan 19;46(1):141-144. doi: 10.1021/jf970418p. PMID: 10554209.
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Combined inactivation of the Clostridium cellulolyticum lactate and malate dehydrogenase genes substantially increases ethanol yield from cellulose and switchgrass fermentations.

Biotechnology for biofuels

Li Y, Tschaplinski TJ, Engle NL, Hamilton CY, Rodriguez M, Liao JC, Schadt CW, Guss AM, Yang Y, Graham DE.
PMID: 22214220
Biotechnol Biofuels. 2012 Jan 04;5(1):2. doi: 10.1186/1754-6834-5-2.

BACKGROUND: The model bacterium Clostridium cellulolyticum efficiently degrades crystalline cellulose and hemicellulose, using cellulosomes to degrade lignocellulosic biomass. Although it imports and ferments both pentose and hexose sugars to produce a mixture of ethanol, acetate, lactate, H2 and CO2,...

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Li Y, Tschaplinski TJ, Engle NL, et al. Combined inactivation of the Clostridium cellulolyticum lactate and malate dehydrogenase genes substantially increases ethanol yield from cellulose and switchgrass fermentations. Biotechnol Biofuels. 2012;5(1):2doi: 10.1186/1754-6834-5-2.
Li, Y., Tschaplinski, T. J., Engle, N. L., Hamilton, C. Y., Rodriguez, M., Liao, J. C., Schadt, C. W., Guss, A. M., Yang, Y., & Graham, D. E. (2012). Combined inactivation of the Clostridium cellulolyticum lactate and malate dehydrogenase genes substantially increases ethanol yield from cellulose and switchgrass fermentations. Biotechnology for biofuels, 5(1), 2. https://doi.org/10.1186/1754-6834-5-2
Li, Yongchao, et al. "Combined inactivation of the Clostridium cellulolyticum lactate and malate dehydrogenase genes substantially increases ethanol yield from cellulose and switchgrass fermentations." Biotechnology for biofuels vol. 5,1 (2012): 2. doi: https://doi.org/10.1186/1754-6834-5-2
Li Y, Tschaplinski TJ, Engle NL, Hamilton CY, Rodriguez M, Liao JC, Schadt CW, Guss AM, Yang Y, Graham DE. Combined inactivation of the Clostridium cellulolyticum lactate and malate dehydrogenase genes substantially increases ethanol yield from cellulose and switchgrass fermentations. Biotechnol Biofuels. 2012 Jan 04;5(1):2. doi: 10.1186/1754-6834-5-2. PMID: 22214220; PMCID: PMC3268733.
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The effects of lactate on nitrosylmyoglobin formation from nitrite and metmyoglobin in a cured meat system.

Food chemistry

McClure BN, Sebranek JG, Kim YH, Sullivan GA.
PMID: 25212339
Food Chem. 2011 Dec 01;129(3):1072-9. doi: 10.1016/j.foodchem.2011.05.077. Epub 2011 May 25.

Two experiments were conducted to determine the effects of lactate on nitrite during meat curing. In the first experiment, using a model system, eight reaction components including nitrite and lactate, were used to assess the effect of each component...

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McClure BN, Sebranek JG, Kim YH, et al. The effects of lactate on nitrosylmyoglobin formation from nitrite and metmyoglobin in a cured meat system. Food Chem. 2011;129(3):1072-9doi: 10.1016/j.foodchem.2011.05.077.
McClure, B. N., Sebranek, J. G., Kim, Y. H., & Sullivan, G. A. (2011). The effects of lactate on nitrosylmyoglobin formation from nitrite and metmyoglobin in a cured meat system. Food chemistry, 129(3), 1072-9. https://doi.org/10.1016/j.foodchem.2011.05.077
McClure, Brooke N, et al. "The effects of lactate on nitrosylmyoglobin formation from nitrite and metmyoglobin in a cured meat system." Food chemistry vol. 129,3 (2011): 1072-9. doi: https://doi.org/10.1016/j.foodchem.2011.05.077
McClure BN, Sebranek JG, Kim YH, Sullivan GA. The effects of lactate on nitrosylmyoglobin formation from nitrite and metmyoglobin in a cured meat system. Food Chem. 2011 Dec 01;129(3):1072-9. doi: 10.1016/j.foodchem.2011.05.077. Epub 2011 May 25. PMID: 25212339.
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Proteomic analysis of effluents from perfused human heart for transplantation: identification of potential biomarkers for ischemic heart damage.

Proteome science

Li H, Li J, Wang Y, Yang T.
PMID: 22443514
Proteome Sci. 2012 Mar 23;10(1):21. doi: 10.1186/1477-5956-10-21.

BACKGROUND: Biomarkers released from the heart at early stage of ischemia are very important to diagnosis of ischemic heart disease and salvage myocytes from death. Known specific markers for blood tests including CK-MB, cardiac troponin T (cTnT) and cardiac...

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Li H, Li J, Wang Y, et al. Proteomic analysis of effluents from perfused human heart for transplantation: identification of potential biomarkers for ischemic heart damage. Proteome Sci. 2012;10(1):21doi: 10.1186/1477-5956-10-21.
Li, H., Li, J., Wang, Y., & Yang, T. (2012). Proteomic analysis of effluents from perfused human heart for transplantation: identification of potential biomarkers for ischemic heart damage. Proteome science, 10(1), 21. https://doi.org/10.1186/1477-5956-10-21
Li, Hong, et al. "Proteomic analysis of effluents from perfused human heart for transplantation: identification of potential biomarkers for ischemic heart damage." Proteome science vol. 10,1 (2012): 21. doi: https://doi.org/10.1186/1477-5956-10-21
Li H, Li J, Wang Y, Yang T. Proteomic analysis of effluents from perfused human heart for transplantation: identification of potential biomarkers for ischemic heart damage. Proteome Sci. 2012 Mar 23;10(1):21. doi: 10.1186/1477-5956-10-21. PMID: 22443514; PMCID: PMC3349588.
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Coulometric determination of NAD+ and NADH in normal and cancer cells using LDH, RVC and a polymer mediator.

Talanta

Torabi F, Ramanathan K, Larsson PO, Gorton L, Svanberg K, Okamoto Y, Danielsson B, Khayyami M.
PMID: 18967769
Talanta. 1999 Nov 15;50(4):787-97. doi: 10.1016/s0039-9140(99)00134-4.

An electrochemical method for the measurement of NAD(+) and NADH in normal and cancer tissues using flow injection analysis (FIA) is reported. Reticulated vitreous carbon (RVC) electrodes with entrapped l-lactate dehydrogenase (LDH) and a new redox polymer containing covalently...

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Torabi F, Ramanathan K, Larsson PO, et al. Coulometric determination of NAD+ and NADH in normal and cancer cells using LDH, RVC and a polymer mediator. Talanta. 1999;50(4):787-97doi: 10.1016/s0039-9140(99)00134-4.
Torabi, F., Ramanathan, K., Larsson, P. O., Gorton, L., Svanberg, K., Okamoto, Y., Danielsson, B., & Khayyami, M. (1999). Coulometric determination of NAD+ and NADH in normal and cancer cells using LDH, RVC and a polymer mediator. Talanta, 50(4), 787-97. https://doi.org/10.1016/s0039-9140(99)00134-4
Torabi, F, et al. "Coulometric determination of NAD+ and NADH in normal and cancer cells using LDH, RVC and a polymer mediator." Talanta vol. 50,4 (1999): 787-97. doi: https://doi.org/10.1016/s0039-9140(99)00134-4
Torabi F, Ramanathan K, Larsson PO, Gorton L, Svanberg K, Okamoto Y, Danielsson B, Khayyami M. Coulometric determination of NAD+ and NADH in normal and cancer cells using LDH, RVC and a polymer mediator. Talanta. 1999 Nov 15;50(4):787-97. doi: 10.1016/s0039-9140(99)00134-4. PMID: 18967769.
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Regulatory Mechanisms of L-Lactic Acid and Taste Substances in Chinese Acid Rice Soup (Rice-Acid) Fermented With a .

Frontiers in microbiology

Liu N, Qin L, Miao S.
PMID: 34093453
Front Microbiol. 2021 May 21;12:594631. doi: 10.3389/fmicb.2021.594631. eCollection 2021.

Rice-acid has abundant taste substances and health protection function due to the various bioactive compounds it contains, including organic acids. L-lactic acid is the most abundant organic acid in rice-acid, but the regulatory mechanisms of L-lactic acid accumulation in...

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Liu N, Qin L, Miao S. Regulatory Mechanisms of L-Lactic Acid and Taste Substances in Chinese Acid Rice Soup (Rice-Acid) Fermented With a . Front Microbiol. 2021;12:594631doi: 10.3389/fmicb.2021.594631.
Liu, N., Qin, L., & Miao, S. (2021). Regulatory Mechanisms of L-Lactic Acid and Taste Substances in Chinese Acid Rice Soup (Rice-Acid) Fermented With a . Frontiers in microbiology, 12594631. https://doi.org/10.3389/fmicb.2021.594631
Liu, Na, et al. "Regulatory Mechanisms of L-Lactic Acid and Taste Substances in Chinese Acid Rice Soup (Rice-Acid) Fermented With a ." Frontiers in microbiology vol. 12 (2021): 594631. doi: https://doi.org/10.3389/fmicb.2021.594631
Liu N, Qin L, Miao S. Regulatory Mechanisms of L-Lactic Acid and Taste Substances in Chinese Acid Rice Soup (Rice-Acid) Fermented With a . Front Microbiol. 2021 May 21;12:594631. doi: 10.3389/fmicb.2021.594631. eCollection 2021. PMID: 34093453; PMCID: PMC8176858.
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Phylogenetics and biochemistry elucidate the evolutionary link between l-malate and l-lactate dehydrogenases and disclose an intermediate group of sequences with mix functional properties.

Biochimie

Brochier-Armanet C, Madern D.
PMID: 34418486
Biochimie. 2021 Dec;191:140-153. doi: 10.1016/j.biochi.2021.08.004. Epub 2021 Aug 18.

The NAD(P)-dependent malate dehydrogenases (MDH) (EC 1.1.1.37) and NAD-dependent lactate dehydrogenases (LDH) (EC. 1.1.1.27) form a large superfamily that has been characterized in organisms belonging to the three Domains of Life. MDH catalyzes the reversible conversion of the oxaloacetate...

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Brochier-Armanet C, Madern D. Phylogenetics and biochemistry elucidate the evolutionary link between l-malate and l-lactate dehydrogenases and disclose an intermediate group of sequences with mix functional properties. Biochimie. 2021;191:140-153doi: 10.1016/j.biochi.2021.08.004.
Brochier-Armanet, C., & Madern, D. (2021). Phylogenetics and biochemistry elucidate the evolutionary link between l-malate and l-lactate dehydrogenases and disclose an intermediate group of sequences with mix functional properties. Biochimie, 191140-153. https://doi.org/10.1016/j.biochi.2021.08.004
Brochier-Armanet, Céline, and Madern, Dominique. "Phylogenetics and biochemistry elucidate the evolutionary link between l-malate and l-lactate dehydrogenases and disclose an intermediate group of sequences with mix functional properties." Biochimie vol. 191 (2021): 140-153. doi: https://doi.org/10.1016/j.biochi.2021.08.004
Brochier-Armanet C, Madern D. Phylogenetics and biochemistry elucidate the evolutionary link between l-malate and l-lactate dehydrogenases and disclose an intermediate group of sequences with mix functional properties. Biochimie. 2021 Dec;191:140-153. doi: 10.1016/j.biochi.2021.08.004. Epub 2021 Aug 18. PMID: 34418486.
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Characterization of a Novel Thermostable Dye-Linked l-Lactate Dehydrogenase Complex and Its Application in Electrochemical Detection.

International journal of molecular sciences

Satomura T, Uno K, Kurosawa N, Sakuraba H, Ohshima T, Suye SI.
PMID: 34948373
Int J Mol Sci. 2021 Dec 17;22(24). doi: 10.3390/ijms222413570.

Flavoenzyme dye-linked l-lactate dehydrogenase (Dye-LDH) is primarily involved in energy generation through electron transfer and exhibits potential utility in electrochemical devices. In this study, a gene encoding a Dye-LDH homolog was identified in a hyperthermophilic archaeon,

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Satomura T, Uno K, Kurosawa N, et al. Characterization of a Novel Thermostable Dye-Linked l-Lactate Dehydrogenase Complex and Its Application in Electrochemical Detection. Int J Mol Sci. 2021;22(24)doi: 10.3390/ijms222413570.
Satomura, T., Uno, K., Kurosawa, N., Sakuraba, H., Ohshima, T., & Suye, S. I. (2021). Characterization of a Novel Thermostable Dye-Linked l-Lactate Dehydrogenase Complex and Its Application in Electrochemical Detection. International journal of molecular sciences, 22(24), . https://doi.org/10.3390/ijms222413570
Satomura, Takenori, et al. "Characterization of a Novel Thermostable Dye-Linked l-Lactate Dehydrogenase Complex and Its Application in Electrochemical Detection." International journal of molecular sciences vol. 22,24 (2021). doi: https://doi.org/10.3390/ijms222413570
Satomura T, Uno K, Kurosawa N, Sakuraba H, Ohshima T, Suye SI. Characterization of a Novel Thermostable Dye-Linked l-Lactate Dehydrogenase Complex and Its Application in Electrochemical Detection. Int J Mol Sci. 2021 Dec 17;22(24). doi: 10.3390/ijms222413570. PMID: 34948373.
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Construction of a Bile-responsive Expression System in .

Food science of animal resources

Chae JP, Pajarillo EA, Hwang IC, Kang DK.
PMID: 30882070
Food Sci Anim Resour. 2019 Feb;39(1):13-22. doi: 10.5851/kosfa.2018.e58. Epub 2019 Feb 28.

This study aimed to develop a bile-responsive expression system for lactobacilli. The promoters of four genes, encoding phosphoenolpyruvate-dependent sugar phosphotransferase (mannose-specific), L-lactate dehydrogenase (LDH), HPr kinase, and D-alanine-D-alanine ligase, respectively, which were highly expressed by bile addition in

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Chae JP, Pajarillo EA, Hwang IC, et al. Construction of a Bile-responsive Expression System in . Food Sci Anim Resour. 2019;39(1):13-22doi: 10.5851/kosfa.2018.e58.
Chae, J. P., Pajarillo, E. A., Hwang, I. C., & Kang, D. K. (2019). Construction of a Bile-responsive Expression System in . Food science of animal resources, 39(1), 13-22. https://doi.org/10.5851/kosfa.2018.e58
Chae, Jong Pyo, et al. "Construction of a Bile-responsive Expression System in ." Food science of animal resources vol. 39,1 (2019): 13-22. doi: https://doi.org/10.5851/kosfa.2018.e58
Chae JP, Pajarillo EA, Hwang IC, Kang DK. Construction of a Bile-responsive Expression System in . Food Sci Anim Resour. 2019 Feb;39(1):13-22. doi: 10.5851/kosfa.2018.e58. Epub 2019 Feb 28. PMID: 30882070; PMCID: PMC6413156.
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Showing 13 to 24 of 75 entries