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Functional characterization of hydroxyproline-O-galactosyltransferases for Arabidopsis arabinogalactan-protein synthesis.

BMC plant biology

Kaur D, Held MA, Smith MR, Showalter AM.
PMID: 34903166
BMC Plant Biol. 2021 Dec 13;21(1):590. doi: 10.1186/s12870-021-03362-2.

BACKGROUND: Arabinogalactan-proteins (AGPs) are structurally complex hydroxyproline-rich cell wall glycoproteins ubiquitous in the plant kingdom. AGPs biosynthesis involves a series of post-translational modifications including the addition of type II arabinogalactans to non-contiguous Hyp residues. To date, eight Hyp-galactosyltransferases (Hyp-GALTs;...

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Kaur D, Held MA, Smith MR, et al. Functional characterization of hydroxyproline-O-galactosyltransferases for Arabidopsis arabinogalactan-protein synthesis. BMC Plant Biol. 2021;21(1):590doi: 10.1186/s12870-021-03362-2.
Kaur, D., Held, M. A., Smith, M. R., & Showalter, A. M. (2021). Functional characterization of hydroxyproline-O-galactosyltransferases for Arabidopsis arabinogalactan-protein synthesis. BMC plant biology, 21(1), 590. https://doi.org/10.1186/s12870-021-03362-2
Kaur, Dasmeet, et al. "Functional characterization of hydroxyproline-O-galactosyltransferases for Arabidopsis arabinogalactan-protein synthesis." BMC plant biology vol. 21,1 (2021): 590. doi: https://doi.org/10.1186/s12870-021-03362-2
Kaur D, Held MA, Smith MR, Showalter AM. Functional characterization of hydroxyproline-O-galactosyltransferases for Arabidopsis arabinogalactan-protein synthesis. BMC Plant Biol. 2021 Dec 13;21(1):590. doi: 10.1186/s12870-021-03362-2. PMID: 34903166; PMCID: PMC8667403.
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Heparan Sulfate Proteoglycans: Key Mediators of Stem Cell Function.

Frontiers in cell and developmental biology

Ravikumar M, Smith RAA, Nurcombe V, Cool SM.
PMID: 33330458
Front Cell Dev Biol. 2020 Nov 19;8:581213. doi: 10.3389/fcell.2020.581213. eCollection 2020.

Heparan sulfate proteoglycans (HSPGs) are an evolutionarily ancient subclass of glycoproteins with exquisite structural complexity. They are ubiquitously expressed across tissues and have been found to exert a multitude of effects on cell behavior and the surrounding microenvironment. Evidence...

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Ravikumar M, Smith RAA, Nurcombe V, et al. Heparan Sulfate Proteoglycans: Key Mediators of Stem Cell Function. Front Cell Dev Biol. 2020;8:581213doi: 10.3389/fcell.2020.581213.
Ravikumar, M., Smith, R. A. A., Nurcombe, V., & Cool, S. M. (2020). Heparan Sulfate Proteoglycans: Key Mediators of Stem Cell Function. Frontiers in cell and developmental biology, 8581213. https://doi.org/10.3389/fcell.2020.581213
Ravikumar, Maanasa, et al. "Heparan Sulfate Proteoglycans: Key Mediators of Stem Cell Function." Frontiers in cell and developmental biology vol. 8 (2020): 581213. doi: https://doi.org/10.3389/fcell.2020.581213
Ravikumar M, Smith RAA, Nurcombe V, Cool SM. Heparan Sulfate Proteoglycans: Key Mediators of Stem Cell Function. Front Cell Dev Biol. 2020 Nov 19;8:581213. doi: 10.3389/fcell.2020.581213. eCollection 2020. PMID: 33330458; PMCID: PMC7710810.
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Physical tuning of galectin-3 signaling.

Proceedings of the National Academy of Sciences of the United States of America

Farhadi SA, Liu R, Becker MW, Phelps EA, Hudalla GA.
PMID: 33941700
Proc Natl Acad Sci U S A. 2021 May 11;118(19). doi: 10.1073/pnas.2024117118.

Galectin-3 (Gal3) exhibits dynamic oligomerization and promiscuous binding, which can lead to concomitant activation of synergistic, antagonistic, or noncooperative signaling pathways that alter cell behavior. Conferring signaling pathway selectivity through mutations in the Gal3-glycan binding interface is challenged by...

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Farhadi SA, Liu R, Becker MW, et al. Physical tuning of galectin-3 signaling. Proc Natl Acad Sci U S A. 2021;118(19)doi: 10.1073/pnas.2024117118.
Farhadi, S. A., Liu, R., Becker, M. W., Phelps, E. A., & Hudalla, G. A. (2021). Physical tuning of galectin-3 signaling. Proceedings of the National Academy of Sciences of the United States of America, 118(19), . https://doi.org/10.1073/pnas.2024117118
Farhadi, Shaheen A, et al. "Physical tuning of galectin-3 signaling." Proceedings of the National Academy of Sciences of the United States of America vol. 118,19 (2021). doi: https://doi.org/10.1073/pnas.2024117118
Farhadi SA, Liu R, Becker MW, Phelps EA, Hudalla GA. Physical tuning of galectin-3 signaling. Proc Natl Acad Sci U S A. 2021 May 11;118(19). doi: 10.1073/pnas.2024117118. PMID: 33941700; PMCID: PMC8126866.
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Heterologous humoral immunity to human and zoonotic coronaviruses: Aiming for the achilles heel.

Seminars in immunology

Ng KW, Faulkner N, Wrobel AG, Gamblin SJ, Kassiotis G.
PMID: 34716096
Semin Immunol. 2021 Jun;55:101507. doi: 10.1016/j.smim.2021.101507. Epub 2021 Oct 25.

Coronaviruses are evolutionarily successful RNA viruses, common to multiple avian, amphibian and mammalian hosts. Despite their ubiquity and potential impact, knowledge of host immunity to coronaviruses remains incomplete, partly owing to the lack of overt pathogenicity of endemic human...

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Ng KW, Faulkner N, Wrobel AG, et al. Heterologous humoral immunity to human and zoonotic coronaviruses: Aiming for the achilles heel. Semin Immunol. 2021;55:101507doi: 10.1016/j.smim.2021.101507.
Ng, K. W., Faulkner, N., Wrobel, A. G., Gamblin, S. J., & Kassiotis, G. (2021). Heterologous humoral immunity to human and zoonotic coronaviruses: Aiming for the achilles heel. Seminars in immunology, 55101507. https://doi.org/10.1016/j.smim.2021.101507
Ng, Kevin W, et al. "Heterologous humoral immunity to human and zoonotic coronaviruses: Aiming for the achilles heel." Seminars in immunology vol. 55 (2021): 101507. doi: https://doi.org/10.1016/j.smim.2021.101507
Ng KW, Faulkner N, Wrobel AG, Gamblin SJ, Kassiotis G. Heterologous humoral immunity to human and zoonotic coronaviruses: Aiming for the achilles heel. Semin Immunol. 2021 Jun;55:101507. doi: 10.1016/j.smim.2021.101507. Epub 2021 Oct 25. PMID: 34716096; PMCID: PMC8542444.
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Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region.

Organic & biomolecular chemistry

Gao J, Lin PH, Nick ST, Liu K, Yu K, Hohenester E, Huang X.
PMID: 33899899
Org Biomol Chem. 2021 Apr 26;19(15):3374-3378. doi: 10.1039/d1ob00317h.

Proteoglycans (PGs) play important roles in many biological processes including tumor progression, cell adhesion, and regulation of growth factor activities. With glycosaminoglycan chains attached to the core proteins in nature, PGs are highly challenging synthetic targets due to the...

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Gao J, Lin PH, Nick ST, et al. Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region. Org Biomol Chem. 2021;19(15):3374-3378doi: 10.1039/d1ob00317h.
Gao, J., Lin, P. H., Nick, S. T., Liu, K., Yu, K., Hohenester, E., & Huang, X. (2021). Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region. Organic & biomolecular chemistry, 19(15), 3374-3378. https://doi.org/10.1039/d1ob00317h
Gao, Jia, et al. "Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region." Organic & biomolecular chemistry vol. 19,15 (2021): 3374-3378. doi: https://doi.org/10.1039/d1ob00317h
Gao J, Lin PH, Nick ST, Liu K, Yu K, Hohenester E, Huang X. Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region. Org Biomol Chem. 2021 Apr 26;19(15):3374-3378. doi: 10.1039/d1ob00317h. PMID: 33899899; PMCID: PMC8084078.
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Precision N-glycoproteomics reveals elevated LacdiNAc as a novel signature of intrahepatic cholangiocarcinoma.

Molecular oncology

Li J, Zhao T, Li J, Shen J, Jia L, Zhu B, Dang L, Ma C, Liu D, Mu F, Hu L, Sun S.
PMID: 34855283
Mol Oncol. 2021 Dec 02; doi: 10.1002/1878-0261.13147. Epub 2021 Dec 02.

Primary liver cancer, mainly comprising hepatocellular carcinoma (HCC) and intrahepatic cholangiocarcinoma (ICC), remains a major global health problem. Although ICC is clinically different from HCC, their molecular differences are still largely unclear. In this study, precision N-glycoproteomic analysis was...

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Li J, Zhao T, Li J, et al. Precision N-glycoproteomics reveals elevated LacdiNAc as a novel signature of intrahepatic cholangiocarcinoma. Mol Oncol. 2021;doi: 10.1002/1878-0261.13147.
Li, J., Zhao, T., Li, J., Shen, J., Jia, L., Zhu, B., Dang, L., Ma, C., Liu, D., Mu, F., Hu, L., & Sun, S. (2021). Precision N-glycoproteomics reveals elevated LacdiNAc as a novel signature of intrahepatic cholangiocarcinoma. Molecular oncology, . https://doi.org/10.1002/1878-0261.13147
Li, Jun, et al. "Precision N-glycoproteomics reveals elevated LacdiNAc as a novel signature of intrahepatic cholangiocarcinoma." Molecular oncology vol. (2021). doi: https://doi.org/10.1002/1878-0261.13147
Li J, Zhao T, Li J, Shen J, Jia L, Zhu B, Dang L, Ma C, Liu D, Mu F, Hu L, Sun S. Precision N-glycoproteomics reveals elevated LacdiNAc as a novel signature of intrahepatic cholangiocarcinoma. Mol Oncol. 2021 Dec 02; doi: 10.1002/1878-0261.13147. Epub 2021 Dec 02. PMID: 34855283.
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Search for evolutionary roots of land plant arabinogalactan-proteins in charophytes: presence of a rhamnogalactan-protein in Spirogyra pratensis (Zygnematophyceae).

The Plant journal : for cell and molecular biology

Pfeifer L, Utermöhlen J, Happ K, Permann C, Holzinger A, von Schwartzenberg K, Classen B.
PMID: 34767672
Plant J. 2021 Nov 12; doi: 10.1111/tpj.15577. Epub 2021 Nov 12.

Charophyte green algae (CGA) are assigned to be the closest relatives of land plants and therefore enlighten processes in the colonization of terrestrial habitats. For the transition from water to land, plants needed significant physiological and structural changes, as...

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Pfeifer L, Utermöhlen J, Happ K, et al. Search for evolutionary roots of land plant arabinogalactan-proteins in charophytes: presence of a rhamnogalactan-protein in Spirogyra pratensis (Zygnematophyceae). Plant J. 2021;doi: 10.1111/tpj.15577.
Pfeifer, L., Utermöhlen, J., Happ, K., Permann, C., Holzinger, A., von Schwartzenberg, K., & Classen, B. (2021). Search for evolutionary roots of land plant arabinogalactan-proteins in charophytes: presence of a rhamnogalactan-protein in Spirogyra pratensis (Zygnematophyceae). The Plant journal : for cell and molecular biology, . https://doi.org/10.1111/tpj.15577
Pfeifer, Lukas, et al. "Search for evolutionary roots of land plant arabinogalactan-proteins in charophytes: presence of a rhamnogalactan-protein in Spirogyra pratensis (Zygnematophyceae)." The Plant journal : for cell and molecular biology vol. (2021). doi: https://doi.org/10.1111/tpj.15577
Pfeifer L, Utermöhlen J, Happ K, Permann C, Holzinger A, von Schwartzenberg K, Classen B. Search for evolutionary roots of land plant arabinogalactan-proteins in charophytes: presence of a rhamnogalactan-protein in Spirogyra pratensis (Zygnematophyceae). Plant J. 2021 Nov 12; doi: 10.1111/tpj.15577. Epub 2021 Nov 12. PMID: 34767672.
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Preliminary Evaluation of a Recombinant Rift Valley Fever Virus Glycoprotein Subunit Vaccine Providing Full Protection against Heterologous Virulent Challenge in Cattle.

Vaccines

Wilson WC, Faburay B, Trujillo JD, Ragan I, Sunwoo SY, Morozov I, Shivanna V, Balogh A, Urbaniak K, McVey DS, Bold D, Gaudreault NN, Schirtzinger EE, Ma W, Richt JA.
PMID: 34358166
Vaccines (Basel). 2021 Jul 06;9(7). doi: 10.3390/vaccines9070748.

Rift Valley fever virus (RVFV) is a mosquito-borne zoonotic pathogen that causes periodic outbreaks of abortion in ruminant species and hemorrhagic disease in humans in sub-Saharan Africa. These outbreaks have a significant impact on veterinary and public health. Its...

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Wilson WC, Faburay B, Trujillo JD, et al. Preliminary Evaluation of a Recombinant Rift Valley Fever Virus Glycoprotein Subunit Vaccine Providing Full Protection against Heterologous Virulent Challenge in Cattle. Vaccines (Basel). 2021;9(7)doi: 10.3390/vaccines9070748.
Wilson, W. C., Faburay, B., Trujillo, J. D., Ragan, I., Sunwoo, S. Y., Morozov, I., Shivanna, V., Balogh, A., Urbaniak, K., McVey, D. S., Bold, D., Gaudreault, N. N., Schirtzinger, E. E., Ma, W., & Richt, J. A. (2021). Preliminary Evaluation of a Recombinant Rift Valley Fever Virus Glycoprotein Subunit Vaccine Providing Full Protection against Heterologous Virulent Challenge in Cattle. Vaccines, 9(7), . https://doi.org/10.3390/vaccines9070748
Wilson, William C, et al. "Preliminary Evaluation of a Recombinant Rift Valley Fever Virus Glycoprotein Subunit Vaccine Providing Full Protection against Heterologous Virulent Challenge in Cattle." Vaccines vol. 9,7 (2021). doi: https://doi.org/10.3390/vaccines9070748
Wilson WC, Faburay B, Trujillo JD, Ragan I, Sunwoo SY, Morozov I, Shivanna V, Balogh A, Urbaniak K, McVey DS, Bold D, Gaudreault NN, Schirtzinger EE, Ma W, Richt JA. Preliminary Evaluation of a Recombinant Rift Valley Fever Virus Glycoprotein Subunit Vaccine Providing Full Protection against Heterologous Virulent Challenge in Cattle. Vaccines (Basel). 2021 Jul 06;9(7). doi: 10.3390/vaccines9070748. PMID: 34358166; PMCID: PMC8310273.
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Thiopurines activate an antiviral unfolded protein response that blocks influenza A virus glycoprotein accumulation.

Journal of virology

Slaine PD, Kleer M, Duguay BA, Pringle ES, Kadijk E, Ying S, Balgi A, Roberge M, McCormick C, Khaperskyy DA.
PMID: 33762409
J Virol. 2021 Mar 24; doi: 10.1128/JVI.00453-21. Epub 2021 Mar 24.

Influenza A viruses (IAVs) utilize host shutoff mechanisms to limit antiviral gene expression and redirect translation machinery to the synthesis of viral proteins. Previously, we showed that IAV replication is sensitive to protein synthesis inhibitors that block translation initiation...

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Slaine PD, Kleer M, Duguay BA, et al. Thiopurines activate an antiviral unfolded protein response that blocks influenza A virus glycoprotein accumulation. J Virol. 2021;doi: 10.1128/JVI.00453-21.
Slaine, P. D., Kleer, M., Duguay, B. A., Pringle, E. S., Kadijk, E., Ying, S., Balgi, A., Roberge, M., McCormick, C., & Khaperskyy, D. A. (2021). Thiopurines activate an antiviral unfolded protein response that blocks influenza A virus glycoprotein accumulation. Journal of virology, . https://doi.org/10.1128/JVI.00453-21
Slaine, Patrick D, et al. "Thiopurines activate an antiviral unfolded protein response that blocks influenza A virus glycoprotein accumulation." Journal of virology vol. (2021). doi: https://doi.org/10.1128/JVI.00453-21
Slaine PD, Kleer M, Duguay BA, Pringle ES, Kadijk E, Ying S, Balgi A, Roberge M, McCormick C, Khaperskyy DA. Thiopurines activate an antiviral unfolded protein response that blocks influenza A virus glycoprotein accumulation. J Virol. 2021 Mar 24; doi: 10.1128/JVI.00453-21. Epub 2021 Mar 24. PMID: 33762409; PMCID: PMC8139708.
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Enhanced curcumin loaded nanocellulose: a possible inhalable nanotherapeutic to treat COVID-19.

Cellulose (London, England)

Gunathilake TMSU, Ching YC, Uyama H, Hai ND, Chuah CH.
PMID: 35002106
Cellulose (Lond). 2022 Jan 04;1-20. doi: 10.1007/s10570-021-04391-8. Epub 2022 Jan 04.

Nanocellulose/polyvinyl alcohol/curcumin (CNC/PVA/curcumin) nanoparticles with enhanced drug loading properties were developed by the dispersion of nanocellulose in curcumin/polyvinyl alcohol aqueous medium. Due to the physical and chemical nature of sulphuric acid hydrolyzed nanocellulose and the antiviral properties of curcumin,...

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Gunathilake TMSU, Ching YC, Uyama H, et al. Enhanced curcumin loaded nanocellulose: a possible inhalable nanotherapeutic to treat COVID-19. Cellulose (Lond). 2022;1-20doi: 10.1007/s10570-021-04391-8.
Gunathilake, T. M. S. U., Ching, Y. C., Uyama, H., Hai, N. D., & Chuah, C. H. (2022). Enhanced curcumin loaded nanocellulose: a possible inhalable nanotherapeutic to treat COVID-19. Cellulose (London, England), 1-20. https://doi.org/10.1007/s10570-021-04391-8
Gunathilake, Thennakoon M Sampath U, et al. "Enhanced curcumin loaded nanocellulose: a possible inhalable nanotherapeutic to treat COVID-19." Cellulose (London, England) vol. (2022): 1-20. doi: https://doi.org/10.1007/s10570-021-04391-8
Gunathilake TMSU, Ching YC, Uyama H, Hai ND, Chuah CH. Enhanced curcumin loaded nanocellulose: a possible inhalable nanotherapeutic to treat COVID-19. Cellulose (Lond). 2022 Jan 04;1-20. doi: 10.1007/s10570-021-04391-8. Epub 2022 Jan 04. PMID: 35002106; PMCID: PMC8725427.
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Pannexin 3 channels in health and disease.

Purinergic signalling

O'Donnell BL, Penuela S.
PMID: 34250568
Purinergic Signal. 2021 Dec;17(4):577-589. doi: 10.1007/s11302-021-09805-7. Epub 2021 Jul 12.

Pannexin 3 (PANX3) is a member of the pannexin family of single membrane channel-forming glycoproteins. Originally thought to have a limited localization in cartilage, bone, and skin, PANX3 has now been detected in a variety of other tissues including...

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O'Donnell BL, Penuela S. Pannexin 3 channels in health and disease. Purinergic Signal. 2021;17(4):577-589doi: 10.1007/s11302-021-09805-7.
O'Donnell, B. L., & Penuela, S. (2021). Pannexin 3 channels in health and disease. Purinergic signalling, 17(4), 577-589. https://doi.org/10.1007/s11302-021-09805-7
O'Donnell, Brooke L, and Penuela, Silvia. "Pannexin 3 channels in health and disease." Purinergic signalling vol. 17,4 (2021): 577-589. doi: https://doi.org/10.1007/s11302-021-09805-7
O'Donnell BL, Penuela S. Pannexin 3 channels in health and disease. Purinergic Signal. 2021 Dec;17(4):577-589. doi: 10.1007/s11302-021-09805-7. Epub 2021 Jul 12. PMID: 34250568.
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Glycosylation and calcium as a code for tandem EGF-like repeat structure and dynamics.

[No authors listed]
UIID-NSF: 472

Proteins carry out many different tasks that are necessary for life. The specific task performed depends on the 3-dimensional structure of the protein molecule. In nature, a protein's structure can be purposely altered through interaction with ions, like calcium,...

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Glycosylation and calcium as a code for tandem EGF-like repeat structure and dynamics. ;
(). Glycosylation and calcium as a code for tandem EGF-like repeat structure and dynamics. .
"Glycosylation and calcium as a code for tandem EGF-like repeat structure and dynamics." vol. ().
Glycosylation and calcium as a code for tandem EGF-like repeat structure and dynamics. UIID-NSF: 472.
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Showing 2533 to 2544 of 2544 entries