Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 327 entries
Sorted by: Best Match Show Resources per page
Altered vitamin A metabolism in human liver slices corresponds to fibrogenesis.

Clinical and translational science

Czuba LC, Wu X, Huang W, Hollingshead N, Roberto JB, Kenerson HL, Yeung RS, Crispe IN, Isoherranen N.
PMID: 33382909
Clin Transl Sci. 2021 May;14(3):976-989. doi: 10.1111/cts.12962. Epub 2021 Feb 02.

All-trans-retinoic acid (atRA), the active metabolite of vitamin A, has antifibrogenic properties in vitro and in animal models. Liver vitamin A homeostasis is maintained by cell-specific enzymatic activities including storage in hepatic stellate cells (HSCs), secretion into circulation from...

Cite
Czuba LC, Wu X, Huang W, et al. Altered vitamin A metabolism in human liver slices corresponds to fibrogenesis. Clin Transl Sci. 2021;14(3):976-989doi: 10.1111/cts.12962.
Czuba, L. C., Wu, X., Huang, W., Hollingshead, N., Roberto, J. B., Kenerson, H. L., Yeung, R. S., Crispe, I. N., & Isoherranen, N. (2021). Altered vitamin A metabolism in human liver slices corresponds to fibrogenesis. Clinical and translational science, 14(3), 976-989. https://doi.org/10.1111/cts.12962
Czuba, Lindsay C, et al. "Altered vitamin A metabolism in human liver slices corresponds to fibrogenesis." Clinical and translational science vol. 14,3 (2021): 976-989. doi: https://doi.org/10.1111/cts.12962
Czuba LC, Wu X, Huang W, Hollingshead N, Roberto JB, Kenerson HL, Yeung RS, Crispe IN, Isoherranen N. Altered vitamin A metabolism in human liver slices corresponds to fibrogenesis. Clin Transl Sci. 2021 May;14(3):976-989. doi: 10.1111/cts.12962. Epub 2021 Feb 02. PMID: 33382909; PMCID: PMC8212748.
Copy Download .nbib Format: NLM
A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E.

Biotechnology for biofuels

Clarkson SM, Hamilton-Brehm SD, Giannone RJ, Engle NL, Tschaplinski TJ, Hettich RL, Elkins JG.
PMID: 25506391
Biotechnol Biofuels. 2014 Dec 03;7(1):165. doi: 10.1186/s13068-014-0165-z. eCollection 2014.

BACKGROUND: Chemical and physical pretreatment of lignocellulosic biomass improves substrate reactivity for increased microbial biofuel production, but also restricts growth via the release of furan aldehydes, such as furfural and 5-hydroxymethylfurfural (5-HMF). The physiological effects of these inhibitors on...

Cite
Clarkson SM, Hamilton-Brehm SD, Giannone RJ, et al. A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E. Biotechnol Biofuels. 2014;7(1):165doi: 10.1186/s13068-014-0165-z.
Clarkson, S. M., Hamilton-Brehm, S. D., Giannone, R. J., Engle, N. L., Tschaplinski, T. J., Hettich, R. L., & Elkins, J. G. (2014). A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E. Biotechnology for biofuels, 7(1), 165. https://doi.org/10.1186/s13068-014-0165-z
Clarkson, Sonya M, et al. "A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E." Biotechnology for biofuels vol. 7,1 (2014): 165. doi: https://doi.org/10.1186/s13068-014-0165-z
Clarkson SM, Hamilton-Brehm SD, Giannone RJ, Engle NL, Tschaplinski TJ, Hettich RL, Elkins JG. A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E. Biotechnol Biofuels. 2014 Dec 03;7(1):165. doi: 10.1186/s13068-014-0165-z. eCollection 2014. PMID: 25506391; PMCID: PMC4265447.
Copy Download .nbib Format: NLM
Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering.

Microbial cell factories

Hioki T, Yamashita D, Tohata M, Endo K, Kawahara A, Okuda M.
PMID: 34963446
Microb Cell Fact. 2021 Dec 28;20(1):231. doi: 10.1186/s12934-021-01724-x.

BACKGROUND: Most of the proteases classified into the M23 family in the MEROPS database exhibit staphylolytic activity and have potential as antibacterial agents. The M23 family is further classified into two subfamilies, M23A and M23B. Proteases of the M23A...

Cite
Hioki T, Yamashita D, Tohata M, et al. Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering. Microb Cell Fact. 2021;20(1):231doi: 10.1186/s12934-021-01724-x.
Hioki, T., Yamashita, D., Tohata, M., Endo, K., Kawahara, A., & Okuda, M. (2021). Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering. Microbial cell factories, 20(1), 231. https://doi.org/10.1186/s12934-021-01724-x
Hioki, Takahiro, et al. "Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering." Microbial cell factories vol. 20,1 (2021): 231. doi: https://doi.org/10.1186/s12934-021-01724-x
Hioki T, Yamashita D, Tohata M, Endo K, Kawahara A, Okuda M. Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering. Microb Cell Fact. 2021 Dec 28;20(1):231. doi: 10.1186/s12934-021-01724-x. PMID: 34963446.
Copy Download .nbib Format: NLM
Association of NQO2 With UDP-Glucuronosyltransferases Reduces Menadione Toxicity in Neuroblastoma Cells.

Frontiers in pharmacology

Chhour M, Perio P, Gayon R, Ternet-Fontebasso H, Ferry G, Nepveu F, Boutin JA, Sudor J, Reybier K.
PMID: 34040527
Front Pharmacol. 2021 May 10;12:660641. doi: 10.3389/fphar.2021.660641. eCollection 2021.

The balance between detoxification and toxicity is linked to enzymes of the drug metabolism Phase I (cytochrome P450 or oxidoreductases) and phase II conjugating enzymes (such as the UGTs). After the reduction of quinones, the product of the reaction,...

Cite
Chhour M, Perio P, Gayon R, et al. Association of NQO2 With UDP-Glucuronosyltransferases Reduces Menadione Toxicity in Neuroblastoma Cells. Front Pharmacol. 2021;12:660641doi: 10.3389/fphar.2021.660641.
Chhour, M., Perio, P., Gayon, R., Ternet-Fontebasso, H., Ferry, G., Nepveu, F., Boutin, J. A., Sudor, J., & Reybier, K. (2021). Association of NQO2 With UDP-Glucuronosyltransferases Reduces Menadione Toxicity in Neuroblastoma Cells. Frontiers in pharmacology, 12660641. https://doi.org/10.3389/fphar.2021.660641
Chhour, Monivan, et al. "Association of NQO2 With UDP-Glucuronosyltransferases Reduces Menadione Toxicity in Neuroblastoma Cells." Frontiers in pharmacology vol. 12 (2021): 660641. doi: https://doi.org/10.3389/fphar.2021.660641
Chhour M, Perio P, Gayon R, Ternet-Fontebasso H, Ferry G, Nepveu F, Boutin JA, Sudor J, Reybier K. Association of NQO2 With UDP-Glucuronosyltransferases Reduces Menadione Toxicity in Neuroblastoma Cells. Front Pharmacol. 2021 May 10;12:660641. doi: 10.3389/fphar.2021.660641. eCollection 2021. PMID: 34040527; PMCID: PMC8142080.
Copy Download .nbib Format: NLM
Metasecretome analysis of a lignocellulolytic microbial consortium grown on wheat straw, xylan and xylose.

Biotechnology for biofuels

Jiménez DJ, Maruthamuthu M, van Elsas JD.
PMID: 26628913
Biotechnol Biofuels. 2015 Dec 01;8:199. doi: 10.1186/s13068-015-0387-8. eCollection 2015.

BACKGROUND: Synergistic action of different enzymes is required to complete the degradation of plant biomass in order to release sugars which are useful for biorefining. However, the use of single strains is often not efficient, as crucial parts of...

Cite
Jiménez DJ, Maruthamuthu M, van Elsas JD. Metasecretome analysis of a lignocellulolytic microbial consortium grown on wheat straw, xylan and xylose. Biotechnol Biofuels. 2015;8:199doi: 10.1186/s13068-015-0387-8.
Jiménez, D. J., Maruthamuthu, M., & van Elsas, J. D. (2015). Metasecretome analysis of a lignocellulolytic microbial consortium grown on wheat straw, xylan and xylose. Biotechnology for biofuels, 8199. https://doi.org/10.1186/s13068-015-0387-8
Jiménez, Diego Javier, et al. "Metasecretome analysis of a lignocellulolytic microbial consortium grown on wheat straw, xylan and xylose." Biotechnology for biofuels vol. 8 (2015): 199. doi: https://doi.org/10.1186/s13068-015-0387-8
Jiménez DJ, Maruthamuthu M, van Elsas JD. Metasecretome analysis of a lignocellulolytic microbial consortium grown on wheat straw, xylan and xylose. Biotechnol Biofuels. 2015 Dec 01;8:199. doi: 10.1186/s13068-015-0387-8. eCollection 2015. PMID: 26628913; PMCID: PMC4666044.
Copy Download .nbib Format: NLM
Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering.

Microbial cell factories

Hioki T, Yamashita D, Tohata M, Endo K, Kawahara A, Okuda M.
PMID: 34963446
Microb Cell Fact. 2021 Dec 28;20(1):231. doi: 10.1186/s12934-021-01724-x.

BACKGROUND: Most of the proteases classified into the M23 family in the MEROPS database exhibit staphylolytic activity and have potential as antibacterial agents. The M23 family is further classified into two subfamilies, M23A and M23B. Proteases of the M23A...

Cite
Hioki T, Yamashita D, Tohata M, et al. Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering. Microb Cell Fact. 2021;20(1):231doi: 10.1186/s12934-021-01724-x.
Hioki, T., Yamashita, D., Tohata, M., Endo, K., Kawahara, A., & Okuda, M. (2021). Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering. Microbial cell factories, 20(1), 231. https://doi.org/10.1186/s12934-021-01724-x
Hioki, Takahiro, et al. "Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering." Microbial cell factories vol. 20,1 (2021): 231. doi: https://doi.org/10.1186/s12934-021-01724-x
Hioki T, Yamashita D, Tohata M, Endo K, Kawahara A, Okuda M. Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering. Microb Cell Fact. 2021 Dec 28;20(1):231. doi: 10.1186/s12934-021-01724-x. PMID: 34963446; PMCID: PMC8715609.
Copy Download .nbib Format: NLM
A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice.

Journal of proteomics

Cavalcante JDS, de Almeida CAS, Clasen MA, da Silva EL, de Barros LC, Marinho AD, Rossini BC, Marino CL, Carvalho PC, Jorge RJB, Dos Santos LD.
PMID: 34954398
J Proteomics. 2021 Dec 24;253:104464. doi: 10.1016/j.jprot.2021.104464. Epub 2021 Dec 24.

Bothrops spp. is responsible for about 70% of snakebites in Brazil, causing a diverse and complex pathophysiological condition. Bothrops leucurus is the main species of medical relevance found in the Atlantic coast in the Brazilian Northeast region. The pathophysiological...

Cite
Cavalcante JDS, de Almeida CAS, Clasen MA, et al. A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. J Proteomics. 2021;253:104464doi: 10.1016/j.jprot.2021.104464.
Cavalcante, J. D. S., de Almeida, C. A. S., Clasen, M. A., da Silva, E. L., de Barros, L. C., Marinho, A. D., Rossini, B. C., Marino, C. L., Carvalho, P. C., Jorge, R. J. B., & Dos Santos, L. D. (2021). A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. Journal of proteomics, 253104464. https://doi.org/10.1016/j.jprot.2021.104464
Cavalcante, Joeliton Dos Santos, et al. "A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice." Journal of proteomics vol. 253 (2021): 104464. doi: https://doi.org/10.1016/j.jprot.2021.104464
Cavalcante JDS, de Almeida CAS, Clasen MA, da Silva EL, de Barros LC, Marinho AD, Rossini BC, Marino CL, Carvalho PC, Jorge RJB, Dos Santos LD. A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. J Proteomics. 2021 Dec 24;253:104464. doi: 10.1016/j.jprot.2021.104464. Epub 2021 Dec 24. PMID: 34954398.
Copy Download .nbib Format: NLM
Industrial Acetogenic Biocatalysts: A Comparative Metabolic and Genomic Analysis.

Frontiers in microbiology

Bengelsdorf FR, Poehlein A, Linder S, Erz C, Hummel T, Hoffmeister S, Daniel R, Dürre P.
PMID: 27458439
Front Microbiol. 2016 Jul 07;7:1036. doi: 10.3389/fmicb.2016.01036. eCollection 2016.

Synthesis gas (syngas) fermentation by anaerobic acetogenic bacteria employing the Wood-Ljungdahl pathway is a bioprocess for production of biofuels and biocommodities. The major fermentation products of the most relevant biocatalytic strains (Clostridium ljungdahlii, C. autoethanogenum, C. ragsdalei, and C....

Cite
Bengelsdorf FR, Poehlein A, Linder S, et al. Industrial Acetogenic Biocatalysts: A Comparative Metabolic and Genomic Analysis. Front Microbiol. 2016;7:1036doi: 10.3389/fmicb.2016.01036.
Bengelsdorf, F. R., Poehlein, A., Linder, S., Erz, C., Hummel, T., Hoffmeister, S., Daniel, R., & Dürre, P. (2016). Industrial Acetogenic Biocatalysts: A Comparative Metabolic and Genomic Analysis. Frontiers in microbiology, 71036. https://doi.org/10.3389/fmicb.2016.01036
Bengelsdorf, Frank R, et al. "Industrial Acetogenic Biocatalysts: A Comparative Metabolic and Genomic Analysis." Frontiers in microbiology vol. 7 (2016): 1036. doi: https://doi.org/10.3389/fmicb.2016.01036
Bengelsdorf FR, Poehlein A, Linder S, Erz C, Hummel T, Hoffmeister S, Daniel R, Dürre P. Industrial Acetogenic Biocatalysts: A Comparative Metabolic and Genomic Analysis. Front Microbiol. 2016 Jul 07;7:1036. doi: 10.3389/fmicb.2016.01036. eCollection 2016. PMID: 27458439; PMCID: PMC4935695.
Copy Download .nbib Format: NLM
A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice.

Journal of proteomics

Cavalcante JDS, de Almeida CAS, Clasen MA, da Silva EL, de Barros LC, Marinho AD, Rossini BC, Marino CL, Carvalho PC, Jorge RJB, Dos Santos LD.
PMID: 34954398
J Proteomics. 2022 Feb 20;253:104464. doi: 10.1016/j.jprot.2021.104464. Epub 2021 Dec 24.

Bothrops spp. is responsible for about 70% of snakebites in Brazil, causing a diverse and complex pathophysiological condition. Bothrops leucurus is the main species of medical relevance found in the Atlantic coast in the Brazilian Northeast region. The pathophysiological...

Cite
Cavalcante JDS, de Almeida CAS, Clasen MA, et al. A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. J Proteomics. 2021;253:104464doi: 10.1016/j.jprot.2021.104464.
Cavalcante, J. D. S., de Almeida, C. A. S., Clasen, M. A., da Silva, E. L., de Barros, L. C., Marinho, A. D., Rossini, B. C., Marino, C. L., Carvalho, P. C., Jorge, R. J. B., & Dos Santos, L. D. (2022). A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. Journal of proteomics, 253104464. https://doi.org/10.1016/j.jprot.2021.104464
Cavalcante, Joeliton Dos Santos, et al. "A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice." Journal of proteomics vol. 253 (2022): 104464. doi: https://doi.org/10.1016/j.jprot.2021.104464
Cavalcante JDS, de Almeida CAS, Clasen MA, da Silva EL, de Barros LC, Marinho AD, Rossini BC, Marino CL, Carvalho PC, Jorge RJB, Dos Santos LD. A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. J Proteomics. 2022 Feb 20;253:104464. doi: 10.1016/j.jprot.2021.104464. Epub 2021 Dec 24. PMID: 34954398.
Copy Download .nbib Format: NLM
Xylo- and cello-oligosaccharide oxidation by gluco-oligosaccharide oxidase from Sarocladium strictum and variants with reduced substrate inhibition.

Biotechnology for biofuels

Vuong TV, Vesterinen AH, Foumani M, Juvonen M, Seppälä J, Tenkanen M, Master ER.
PMID: 24119501
Biotechnol Biofuels. 2013 Oct 12;6(1):148. doi: 10.1186/1754-6834-6-148.

BACKGROUND: The oxidation of carbohydrates from lignocellulose can facilitate the synthesis of new biopolymers and biochemicals, and also reduce sugar metabolism by lignocellulolytic microorganisms, reserving aldonates for fermentation to biofuels. Although oxidoreductases that oxidize cellulosic hydrolysates have been well...

Cite
Vuong TV, Vesterinen AH, Foumani M, et al. Xylo- and cello-oligosaccharide oxidation by gluco-oligosaccharide oxidase from Sarocladium strictum and variants with reduced substrate inhibition. Biotechnol Biofuels. 2013;6(1):148doi: 10.1186/1754-6834-6-148.
Vuong, T. V., Vesterinen, A. H., Foumani, M., Juvonen, M., Seppälä, J., Tenkanen, M., & Master, E. R. (2013). Xylo- and cello-oligosaccharide oxidation by gluco-oligosaccharide oxidase from Sarocladium strictum and variants with reduced substrate inhibition. Biotechnology for biofuels, 6(1), 148. https://doi.org/10.1186/1754-6834-6-148
Vuong, Thu V, et al. "Xylo- and cello-oligosaccharide oxidation by gluco-oligosaccharide oxidase from Sarocladium strictum and variants with reduced substrate inhibition." Biotechnology for biofuels vol. 6,1 (2013): 148. doi: https://doi.org/10.1186/1754-6834-6-148
Vuong TV, Vesterinen AH, Foumani M, Juvonen M, Seppälä J, Tenkanen M, Master ER. Xylo- and cello-oligosaccharide oxidation by gluco-oligosaccharide oxidase from Sarocladium strictum and variants with reduced substrate inhibition. Biotechnol Biofuels. 2013 Oct 12;6(1):148. doi: 10.1186/1754-6834-6-148. PMID: 24119501; PMCID: PMC4015748.
Copy Download .nbib Format: NLM
A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice.

Journal of proteomics

Cavalcante JDS, de Almeida CAS, Clasen MA, da Silva EL, de Barros LC, Marinho AD, Rossini BC, Marino CL, Carvalho PC, Jorge RJB, Dos Santos LD.
PMID: 34954398
J Proteomics. 2021 Dec 24;253:104464. doi: 10.1016/j.jprot.2021.104464. Epub 2021 Dec 24.

Bothrops spp. is responsible for about 70% of snakebites in Brazil, causing a diverse and complex pathophysiological condition. Bothrops leucurus is the main species of medical relevance found in the Atlantic coast in the Brazilian Northeast region. The pathophysiological...

Cite
Cavalcante JDS, de Almeida CAS, Clasen MA, et al. A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. J Proteomics. 2021;253:104464doi: 10.1016/j.jprot.2021.104464.
Cavalcante, J. D. S., de Almeida, C. A. S., Clasen, M. A., da Silva, E. L., de Barros, L. C., Marinho, A. D., Rossini, B. C., Marino, C. L., Carvalho, P. C., Jorge, R. J. B., & Dos Santos, L. D. (2021). A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. Journal of proteomics, 253104464. https://doi.org/10.1016/j.jprot.2021.104464
Cavalcante, Joeliton Dos Santos, et al. "A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice." Journal of proteomics vol. 253 (2021): 104464. doi: https://doi.org/10.1016/j.jprot.2021.104464
Cavalcante JDS, de Almeida CAS, Clasen MA, da Silva EL, de Barros LC, Marinho AD, Rossini BC, Marino CL, Carvalho PC, Jorge RJB, Dos Santos LD. A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. J Proteomics. 2021 Dec 24;253:104464. doi: 10.1016/j.jprot.2021.104464. Epub 2021 Dec 24. PMID: 34954398.
Copy Download .nbib Format: NLM
A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice.

Journal of proteomics

Cavalcante JDS, de Almeida CAS, Clasen MA, da Silva EL, de Barros LC, Marinho AD, Rossini BC, Marino CL, Carvalho PC, Jorge RJB, Dos Santos LD.
PMID: 34954398
J Proteomics. 2021 Dec 24;253:104464. doi: 10.1016/j.jprot.2021.104464. Epub 2021 Dec 24.

Bothrops spp. is responsible for about 70% of snakebites in Brazil, causing a diverse and complex pathophysiological condition. Bothrops leucurus is the main species of medical relevance found in the Atlantic coast in the Brazilian Northeast region. The pathophysiological...

Cite
Cavalcante JDS, de Almeida CAS, Clasen MA, et al. A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. J Proteomics. 2021;253:104464doi: 10.1016/j.jprot.2021.104464.
Cavalcante, J. D. S., de Almeida, C. A. S., Clasen, M. A., da Silva, E. L., de Barros, L. C., Marinho, A. D., Rossini, B. C., Marino, C. L., Carvalho, P. C., Jorge, R. J. B., & Dos Santos, L. D. (2021). A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. Journal of proteomics, 253104464. https://doi.org/10.1016/j.jprot.2021.104464
Cavalcante, Joeliton Dos Santos, et al. "A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice." Journal of proteomics vol. 253 (2021): 104464. doi: https://doi.org/10.1016/j.jprot.2021.104464
Cavalcante JDS, de Almeida CAS, Clasen MA, da Silva EL, de Barros LC, Marinho AD, Rossini BC, Marino CL, Carvalho PC, Jorge RJB, Dos Santos LD. A fingerprint of plasma proteome alteration after local tissue damage induced by Bothrops leucurus snake venom in mice. J Proteomics. 2021 Dec 24;253:104464. doi: 10.1016/j.jprot.2021.104464. Epub 2021 Dec 24. PMID: 34954398.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 327 entries