Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 59 entries
Sorted by: Best Match Show Resources per page
SULF2 expression by immunohistochemistry and overall survival in oesophageal cancer: a cohort study.

BMJ open

Lui NS, van Zante A, Rosen SD, Jablons DM, Lemjabbar-Alaoui H.
PMID: 23180455
BMJ Open. 2012 Nov 23;2(6). doi: 10.1136/bmjopen-2012-001624. Print 2012.

OBJECTIVES: Oesophageal cancer is the eighth most commonly diagnosed cancer worldwide, and there is a need for biomarkers to improve diagnosis, prognosis and treatment. Sulfatases 2 (SULF2) is an extracellular endosulphatase that regulates several signalling pathways in carcinogenesis and...

Cite
Lui NS, van Zante A, Rosen SD, et al. SULF2 expression by immunohistochemistry and overall survival in oesophageal cancer: a cohort study. BMJ Open. 2012;2(6)doi: 10.1136/bmjopen-2012-001624.
Lui, N. S., van Zante, A., Rosen, S. D., Jablons, D. M., & Lemjabbar-Alaoui, H. (2012). SULF2 expression by immunohistochemistry and overall survival in oesophageal cancer: a cohort study. BMJ open, 2(6), . https://doi.org/10.1136/bmjopen-2012-001624
Lui, Natalie Shaubie, et al. "SULF2 expression by immunohistochemistry and overall survival in oesophageal cancer: a cohort study." BMJ open vol. 2,6 (2012). doi: https://doi.org/10.1136/bmjopen-2012-001624
Lui NS, van Zante A, Rosen SD, Jablons DM, Lemjabbar-Alaoui H. SULF2 expression by immunohistochemistry and overall survival in oesophageal cancer: a cohort study. BMJ Open. 2012 Nov 23;2(6). doi: 10.1136/bmjopen-2012-001624. Print 2012. PMID: 23180455; PMCID: PMC3532995.
Copy Download .nbib Format: NLM
Chondroitin sulfatases differentially regulate Wnt signaling in prostate stem cells through effects on SHP2, phospho-ERK1/2, and Dickkopf Wnt signaling pathway inhibitor (DKK3).

Oncotarget

Bhattacharyya S, Feferman L, Tobacman JK.
PMID: 29245974
Oncotarget. 2017 Oct 27;8(59):100242-100260. doi: 10.18632/oncotarget.22152. eCollection 2017 Nov 21.

The chondroitin sulfatases N-acetylgalactosamine-4-sulfatase (ARSB) and galactosamine-N-acetyl-6-sulfatase (GALNS) remove either the 4-sulfate group at the non-reducing end of chondroitin 4-sulfate (C4S) and dermatan sulfate, or the 6-sulfate group of chondroitin 6-sulfate, chondroitin 4,6-disulfate (chondroitin sulfate E), or keratan sulfate....

Cite
Bhattacharyya S, Feferman L, Tobacman JK. Chondroitin sulfatases differentially regulate Wnt signaling in prostate stem cells through effects on SHP2, phospho-ERK1/2, and Dickkopf Wnt signaling pathway inhibitor (DKK3). Oncotarget. 2017;8(59):100242-100260doi: 10.18632/oncotarget.22152.
Bhattacharyya, S., Feferman, L., & Tobacman, J. K. (2017). Chondroitin sulfatases differentially regulate Wnt signaling in prostate stem cells through effects on SHP2, phospho-ERK1/2, and Dickkopf Wnt signaling pathway inhibitor (DKK3). Oncotarget, 8(59), 100242-100260. https://doi.org/10.18632/oncotarget.22152
Bhattacharyya, Sumit, et al. "Chondroitin sulfatases differentially regulate Wnt signaling in prostate stem cells through effects on SHP2, phospho-ERK1/2, and Dickkopf Wnt signaling pathway inhibitor (DKK3)." Oncotarget vol. 8,59 (2017): 100242-100260. doi: https://doi.org/10.18632/oncotarget.22152
Bhattacharyya S, Feferman L, Tobacman JK. Chondroitin sulfatases differentially regulate Wnt signaling in prostate stem cells through effects on SHP2, phospho-ERK1/2, and Dickkopf Wnt signaling pathway inhibitor (DKK3). Oncotarget. 2017 Oct 27;8(59):100242-100260. doi: 10.18632/oncotarget.22152. eCollection 2017 Nov 21. PMID: 29245974; PMCID: PMC5725016.
Copy Download .nbib Format: NLM
Anaerobic Degradation of Sulfated Polysaccharides by Two Novel .

Frontiers in microbiology

van Vliet DM, Palakawong Na Ayudthaya S, Diop S, Villanueva L, Stams AJM, Sánchez-Andrea I.
PMID: 30833937
Front Microbiol. 2019 Feb 18;10:253. doi: 10.3389/fmicb.2019.00253. eCollection 2019.

The marine environment contains a large diversity of sulfated polysaccharides and other glycopolymers. Saccharolytic microorganisms degrade these compounds through hydrolysis, which includes the hydrolysis of sulfate groups from sugars by sulfatases. Various marine bacteria of the

Cite
van Vliet DM, Palakawong Na Ayudthaya S, Diop S, et al. Anaerobic Degradation of Sulfated Polysaccharides by Two Novel . Front Microbiol. 2019;10:253doi: 10.3389/fmicb.2019.00253.
van Vliet, D. M., Palakawong Na Ayudthaya, S., Diop, S., Villanueva, L., Stams, A. J. M., & Sánchez-Andrea, I. (2019). Anaerobic Degradation of Sulfated Polysaccharides by Two Novel . Frontiers in microbiology, 10253. https://doi.org/10.3389/fmicb.2019.00253
van Vliet, Daan M, et al. "Anaerobic Degradation of Sulfated Polysaccharides by Two Novel ." Frontiers in microbiology vol. 10 (2019): 253. doi: https://doi.org/10.3389/fmicb.2019.00253
van Vliet DM, Palakawong Na Ayudthaya S, Diop S, Villanueva L, Stams AJM, Sánchez-Andrea I. Anaerobic Degradation of Sulfated Polysaccharides by Two Novel . Front Microbiol. 2019 Feb 18;10:253. doi: 10.3389/fmicb.2019.00253. eCollection 2019. PMID: 30833937; PMCID: PMC6388578.
Copy Download .nbib Format: NLM
Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius.

mBio

Munoz-Munoz J, Ndeh D, Fernandez-Julia P, Walton G, Henrissat B, Gilbert HJ.
PMID: 34340552
mBio. 2021 Aug 31;12(4):e0136821. doi: 10.1128/mBio.01368-21. Epub 2021 Aug 03.

The human gut microbiota (HGM) contributes to the physiology and health of its host. The health benefits provided by dietary manipulation of the HGM require knowledge of how glycans, the major nutrients available to this ecosystem, are metabolized. Arabinogalactan...

Cite
Munoz-Munoz J, Ndeh D, Fernandez-Julia P, et al. Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius. mBio. 2021;12(4):e0136821doi: 10.1128/mBio.01368-21.
Munoz-Munoz, J., Ndeh, D., Fernandez-Julia, P., Walton, G., Henrissat, B., & Gilbert, H. J. (2021). Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius. mBio, 12(4), e0136821. https://doi.org/10.1128/mBio.01368-21
Munoz-Munoz, Jose, et al. "Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius." mBio vol. 12,4 (2021): e0136821. doi: https://doi.org/10.1128/mBio.01368-21
Munoz-Munoz J, Ndeh D, Fernandez-Julia P, Walton G, Henrissat B, Gilbert HJ. Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius. mBio. 2021 Aug 31;12(4):e0136821. doi: 10.1128/mBio.01368-21. Epub 2021 Aug 03. PMID: 34340552; PMCID: PMC8406133.
Copy Download .nbib Format: NLM
De Novo Whole-Genome Assembly of the Swede Midge (Contarinia nasturtii), a Specialist of Brassicaceae, Using Linked-Read Sequencing.

Genome biology and evolution

Mori BA, Coutu C, Chen YH, Campbell EO, Dupuis JR, Erlandson MA, Hegedus DD.
PMID: 33662122
Genome Biol Evol. 2021 Mar 01;13(3). doi: 10.1093/gbe/evab036.

The swede midge, Contarinia nasturtii, is a cecidomyiid fly that feeds specifically on plants within the Brassicaceae. Plants in this family employ a glucosinolate-myrosinase defense system, which can be highly toxic to nonspecialist feeders. Feeding by C. nasturtii larvae...

Cite
Mori BA, Coutu C, Chen YH, et al. De Novo Whole-Genome Assembly of the Swede Midge (Contarinia nasturtii), a Specialist of Brassicaceae, Using Linked-Read Sequencing. Genome Biol Evol. 2021;13(3)doi: 10.1093/gbe/evab036.
Mori, B. A., Coutu, C., Chen, Y. H., Campbell, E. O., Dupuis, J. R., Erlandson, M. A., & Hegedus, D. D. (2021). De Novo Whole-Genome Assembly of the Swede Midge (Contarinia nasturtii), a Specialist of Brassicaceae, Using Linked-Read Sequencing. Genome biology and evolution, 13(3), . https://doi.org/10.1093/gbe/evab036
Mori, Boyd A, et al. "De Novo Whole-Genome Assembly of the Swede Midge (Contarinia nasturtii), a Specialist of Brassicaceae, Using Linked-Read Sequencing." Genome biology and evolution vol. 13,3 (2021). doi: https://doi.org/10.1093/gbe/evab036
Mori BA, Coutu C, Chen YH, Campbell EO, Dupuis JR, Erlandson MA, Hegedus DD. De Novo Whole-Genome Assembly of the Swede Midge (Contarinia nasturtii), a Specialist of Brassicaceae, Using Linked-Read Sequencing. Genome Biol Evol. 2021 Mar 01;13(3). doi: 10.1093/gbe/evab036. PMID: 33662122; PMCID: PMC8011032.
Copy Download .nbib Format: NLM
Hypertensive effects of transforming growth factor-β1 in vascular smooth muscles cells from spontaneously hypertensive rats are mediated by sulfatase 2.

Cytokine

Kim HS, Kim HY.
PMID: 34808537
Cytokine. 2021 Nov 20;150:155754. doi: 10.1016/j.cyto.2021.155754. Epub 2021 Nov 20.

Extracellular sulfatases (sulfatase 1 and sulfatase 2) mediate up- or down-regulatory effects of cytokines on angiotensin II (Ang II)-induced expression of hypertensive mediators in hypertensive cells. The overproduction of transforming growth factor-β1 (TGF-β1) is associated with chronic hypertension. In...

Cite
Kim HS, Kim HY. Hypertensive effects of transforming growth factor-β1 in vascular smooth muscles cells from spontaneously hypertensive rats are mediated by sulfatase 2. Cytokine. 2021;150:155754doi: 10.1016/j.cyto.2021.155754.
Kim, H. S., & Kim, H. Y. (2021). Hypertensive effects of transforming growth factor-β1 in vascular smooth muscles cells from spontaneously hypertensive rats are mediated by sulfatase 2. Cytokine, 150155754. https://doi.org/10.1016/j.cyto.2021.155754
Kim, Hee Sun, and Kim, Hye Young. "Hypertensive effects of transforming growth factor-β1 in vascular smooth muscles cells from spontaneously hypertensive rats are mediated by sulfatase 2." Cytokine vol. 150 (2021): 155754. doi: https://doi.org/10.1016/j.cyto.2021.155754
Kim HS, Kim HY. Hypertensive effects of transforming growth factor-β1 in vascular smooth muscles cells from spontaneously hypertensive rats are mediated by sulfatase 2. Cytokine. 2021 Nov 20;150:155754. doi: 10.1016/j.cyto.2021.155754. Epub 2021 Nov 20. PMID: 34808537.
Copy Download .nbib Format: NLM
Hypertensive effects of transforming growth factor-β1 in vascular smooth muscles cells from spontaneously hypertensive rats are mediated by sulfatase 2.

Cytokine

Kim HS, Kim HY.
PMID: 34808537
Cytokine. 2021 Nov 20;150:155754. doi: 10.1016/j.cyto.2021.155754. Epub 2021 Nov 20.

Extracellular sulfatases (sulfatase 1 and sulfatase 2) mediate up- or down-regulatory effects of cytokines on angiotensin II (Ang II)-induced expression of hypertensive mediators in hypertensive cells. The overproduction of transforming growth factor-β1 (TGF-β1) is associated with chronic hypertension. In...

Cite
Kim HS, Kim HY. Hypertensive effects of transforming growth factor-β1 in vascular smooth muscles cells from spontaneously hypertensive rats are mediated by sulfatase 2. Cytokine. 2021;150:155754doi: 10.1016/j.cyto.2021.155754.
Kim, H. S., & Kim, H. Y. (2021). Hypertensive effects of transforming growth factor-β1 in vascular smooth muscles cells from spontaneously hypertensive rats are mediated by sulfatase 2. Cytokine, 150155754. https://doi.org/10.1016/j.cyto.2021.155754
Kim, Hee Sun, and Kim, Hye Young. "Hypertensive effects of transforming growth factor-β1 in vascular smooth muscles cells from spontaneously hypertensive rats are mediated by sulfatase 2." Cytokine vol. 150 (2021): 155754. doi: https://doi.org/10.1016/j.cyto.2021.155754
Kim HS, Kim HY. Hypertensive effects of transforming growth factor-β1 in vascular smooth muscles cells from spontaneously hypertensive rats are mediated by sulfatase 2. Cytokine. 2021 Nov 20;150:155754. doi: 10.1016/j.cyto.2021.155754. Epub 2021 Nov 20. PMID: 34808537.
Copy Download .nbib Format: NLM
Sulfatase 1 mediates IL-10-induced dimethylarginine dimethylaminohydrolase-1 expression and antiproliferative effects in vascular smooth muscle cells of spontaneously hypertensive rats.

Cytokine

Kim HY, Kim HS.
PMID: 33128921
Cytokine. 2021 Jan;137:155344. doi: 10.1016/j.cyto.2020.155344. Epub 2020 Oct 28.

The extracellular sulfatases (exSulfs) sulfatase 1 (Sulf1) and sulfatase 2 (Sulf2) are well-known regulators of cell signaling and metabolism. In addition, exSulfs mediate the up- or downregulatory effects of cytokines on angiotensin II (Ang II)-induced expression of hypertensive mediators...

Cite
Kim HY, Kim HS. Sulfatase 1 mediates IL-10-induced dimethylarginine dimethylaminohydrolase-1 expression and antiproliferative effects in vascular smooth muscle cells of spontaneously hypertensive rats. Cytokine. 2020;137:155344doi: 10.1016/j.cyto.2020.155344.
Kim, H. Y., & Kim, H. S. (2021). Sulfatase 1 mediates IL-10-induced dimethylarginine dimethylaminohydrolase-1 expression and antiproliferative effects in vascular smooth muscle cells of spontaneously hypertensive rats. Cytokine, 137155344. https://doi.org/10.1016/j.cyto.2020.155344
Kim, Hye Young, and Kim, Hee Sun. "Sulfatase 1 mediates IL-10-induced dimethylarginine dimethylaminohydrolase-1 expression and antiproliferative effects in vascular smooth muscle cells of spontaneously hypertensive rats." Cytokine vol. 137 (2021): 155344. doi: https://doi.org/10.1016/j.cyto.2020.155344
Kim HY, Kim HS. Sulfatase 1 mediates IL-10-induced dimethylarginine dimethylaminohydrolase-1 expression and antiproliferative effects in vascular smooth muscle cells of spontaneously hypertensive rats. Cytokine. 2021 Jan;137:155344. doi: 10.1016/j.cyto.2020.155344. Epub 2020 Oct 28. PMID: 33128921.
Copy Download .nbib Format: NLM
Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius.

mBio

Munoz-Munoz J, Ndeh D, Fernandez-Julia P, Walton G, Henrissat B, Gilbert HJ.
PMID: 34340552
mBio. 2021 Aug 31;12(4):e0136821. doi: 10.1128/mBio.01368-21. Epub 2021 Aug 03.

The human gut microbiota (HGM) contributes to the physiology and health of its host. The health benefits provided by dietary manipulation of the HGM require knowledge of how glycans, the major nutrients available to this ecosystem, are metabolized. Arabinogalactan...

Cite
Munoz-Munoz J, Ndeh D, Fernandez-Julia P, et al. Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius. mBio. 2021;12(4):e0136821doi: 10.1128/mBio.01368-21.
Munoz-Munoz, J., Ndeh, D., Fernandez-Julia, P., Walton, G., Henrissat, B., & Gilbert, H. J. (2021). Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius. mBio, 12(4), e0136821. https://doi.org/10.1128/mBio.01368-21
Munoz-Munoz, Jose, et al. "Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius." mBio vol. 12,4 (2021): e0136821. doi: https://doi.org/10.1128/mBio.01368-21
Munoz-Munoz J, Ndeh D, Fernandez-Julia P, Walton G, Henrissat B, Gilbert HJ. Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius. mBio. 2021 Aug 31;12(4):e0136821. doi: 10.1128/mBio.01368-21. Epub 2021 Aug 03. PMID: 34340552; PMCID: PMC8406133.
Copy Download .nbib Format: NLM
Structural analysis of the sulfatase AmAS from Akkermansia muciniphila.

Acta crystallographica. Section D, Structural biology

Li CC, Tang XY, Zhu YB, Song YJ, Zhao NL, Huang Q, Mou XY, Luo GH, Liu TG, Tong AP, Tang H, Bao R.
PMID: 34866616
Acta Crystallogr D Struct Biol. 2021 Dec 01;77:1614-1623. doi: 10.1107/S2059798321010317. Epub 2021 Nov 29.

Akkermansia muciniphila, an anaerobic Gram-negative bacterium, is a major intestinal commensal bacterium that can modulate the host immune response. It colonizes the mucosal layer and produces nutrients for the gut mucosa and other commensal bacteria. It is believed that...

Cite
Li CC, Tang XY, Zhu YB, et al. Structural analysis of the sulfatase AmAS from Akkermansia muciniphila. Acta Crystallogr D Struct Biol. 2021;77:1614-1623doi: 10.1107/S2059798321010317.
Li, C. C., Tang, X. Y., Zhu, Y. B., Song, Y. J., Zhao, N. L., Huang, Q., Mou, X. Y., Luo, G. H., Liu, T. G., Tong, A. P., Tang, H., & Bao, R. (2021). Structural analysis of the sulfatase AmAS from Akkermansia muciniphila. Acta crystallographica. Section D, Structural biology, 771614-1623. https://doi.org/10.1107/S2059798321010317
Li, Chang Cheng, et al. "Structural analysis of the sulfatase AmAS from Akkermansia muciniphila." Acta crystallographica. Section D, Structural biology vol. 77 (2021): 1614-1623. doi: https://doi.org/10.1107/S2059798321010317
Li CC, Tang XY, Zhu YB, Song YJ, Zhao NL, Huang Q, Mou XY, Luo GH, Liu TG, Tong AP, Tang H, Bao R. Structural analysis of the sulfatase AmAS from Akkermansia muciniphila. Acta Crystallogr D Struct Biol. 2021 Dec 01;77:1614-1623. doi: 10.1107/S2059798321010317. Epub 2021 Nov 29. PMID: 34866616.
Copy Download .nbib Format: NLM
The gut microbiota: a major player in the toxicity of environmental pollutants?.

NPJ biofilms and microbiomes

Claus SP, Guillou H, Ellero-Simatos S.
PMID: 28721242
NPJ Biofilms Microbiomes. 2016 May 04;2:16003. doi: 10.1038/npjbiofilms.2016.3. eCollection 2016.

Exposure to environmental chemicals has been linked to various health disorders, including obesity, type 2 diabetes, cancer and dysregulation of the immune and reproductive systems, whereas the gastrointestinal microbiota critically contributes to a variety of host metabolic and immune...

Cite
Claus SP, Guillou H, Ellero-Simatos S. The gut microbiota: a major player in the toxicity of environmental pollutants?. NPJ Biofilms Microbiomes. 2016;2:16003doi: 10.1038/npjbiofilms.2016.3.
Claus, S. P., Guillou, H., & Ellero-Simatos, S. (2016). The gut microbiota: a major player in the toxicity of environmental pollutants?. NPJ biofilms and microbiomes, 216003. https://doi.org/10.1038/npjbiofilms.2016.3
Claus, Sandrine P, et al. "The gut microbiota: a major player in the toxicity of environmental pollutants?." NPJ biofilms and microbiomes vol. 2 (2016): 16003. doi: https://doi.org/10.1038/npjbiofilms.2016.3
Claus SP, Guillou H, Ellero-Simatos S. The gut microbiota: a major player in the toxicity of environmental pollutants?. NPJ Biofilms Microbiomes. 2016 May 04;2:16003. doi: 10.1038/npjbiofilms.2016.3. eCollection 2016. PMID: 28721242; PMCID: PMC5515271.
Copy Download .nbib Format: NLM
Quantification of the enzyme activities of iduronate-2-sulfatase, .

Molecular genetics and metabolism reports

Mashima R, Ohira M, Okuyama T, Tatsumi A.
PMID: 29326871
Mol Genet Metab Rep. 2017 Dec 21;14:36-40. doi: 10.1016/j.ymgmr.2017.12.001. eCollection 2018 Mar.

Mucopolysaccharidosis (MPS) is a genetic disorder characterized by the accumulation of glycosaminoglycans in the body. Of the multiple MPS disease subtypes, several are caused by defects in sulfatases. Specifically, a defect in iduronate-2-sulfatase (ID2S) leads to MPS II, whereas

Cite
Mashima R, Ohira M, Okuyama T, et al. Quantification of the enzyme activities of iduronate-2-sulfatase, . Mol Genet Metab Rep. 2017;14:36-40doi: 10.1016/j.ymgmr.2017.12.001.
Mashima, R., Ohira, M., Okuyama, T., & Tatsumi, A. (2018). Quantification of the enzyme activities of iduronate-2-sulfatase, . Molecular genetics and metabolism reports, 1436-40. https://doi.org/10.1016/j.ymgmr.2017.12.001
Mashima, Ryuichi, et al. "Quantification of the enzyme activities of iduronate-2-sulfatase, ." Molecular genetics and metabolism reports vol. 14 (2018): 36-40. doi: https://doi.org/10.1016/j.ymgmr.2017.12.001
Mashima R, Ohira M, Okuyama T, Tatsumi A. Quantification of the enzyme activities of iduronate-2-sulfatase, . Mol Genet Metab Rep. 2017 Dec 21;14:36-40. doi: 10.1016/j.ymgmr.2017.12.001. eCollection 2018 Mar. PMID: 29326871; PMCID: PMC5758840.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 59 entries