Výsledky vyhledávání - "T.N.C. Ramya"

Akademický článek

Harnessing the acceptor substrate promiscuity of Clostridium botulinum Maf glycosyltransferase to glyco-engineer mini-flagellin protein chimeras

Autor: Sonali Sunsunwal, Aasawari Khairnar, Srikrishna Subramanian, T.N.C. Ramya

Publikováno v: Communications Biology, Vol 7, Iss 1, Pp 1-14 (2024)

Abstract Several bacterial flagellins are O-glycosylated with nonulosonic acids on surface-exposed Serine/Threonine residues by Maf glycosyltransferases. The Clostridium botulinum Maf glycosyltransferase (CbMaf) displays considerable donor substrate

Externí odkaz: https://doaj.org/article/2e3255aa06034dfe9bac287224fd7784

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Akademický článek

A comparative study of the substrate preference of the sialidases, CpNanI, HpNanH, and BbSia2 towards 2-Aminobenzamide-labeled 3′-Sialyllactose, 6′-Sialyllactose, and Sialyllacto-N-tetraose-b

Autor: Madhu Lata, T.N.C. Ramya

Publikováno v: Biochemistry and Biophysics Reports, Vol 39, Iss , Pp 101791- (2024)

Sialidases catalyze the removal of terminal sialic acids from sialylated biomolecules, and their substrate preference is frequently indicated in terms of the glycosidic linkages cleaved (α2-3, α2-6, and α2-8) without mention of the remaining sub-t

Externí odkaz: https://doaj.org/article/b9c92585b57e468c8b96166ef9a57d5c

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Akademický článek

A comparative study of the efficacy of alginate lyases in the presence of metal ions elevated in the cystic fibrosis lung milieu

Autor: Neetu, T.N.C. Ramya

Publikováno v: Biochemistry and Biophysics Reports, Vol 40, Iss , Pp 101821- (2024)

Pseudomonas aeruginosa, a common cause of morbidity in cystic fibrosis, chronically infects the patient's lungs by forming an alginate-containing biofilm. Alginate lyases are polysaccharide lyases that lyse alginate and are, therefore, potential biof

Externí odkaz: https://doaj.org/article/5b68ad12ab154bedbffdf50496c0654e

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Akademický článek

Biofilm inhibitory effect of alginate lyases on mucoid P. aeruginosa from a cystic fibrosis patient

Autor: Sonal Mahajan, Sonali Sunsunwal, Vikas Gautam, Meenu Singh, T.N.C. Ramya

Publikováno v: Biochemistry and Biophysics Reports, Vol 26, Iss , Pp 101028- (2021)

Chronic mucoid Pseudomonas aeruginosa infections are a major scourge in cystic fibrosis patients. Mucoid P. aeruginosa displays structured alginate-rich biofilms that are resistant to antibiotics. Here, we have assessed the efficacy of a panel of alg

Externí odkaz: https://doaj.org/article/8cc67b2a37504af9b3b0a1f2f74c21ce

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New carbohydrate binding domains identified by phage display based functional metagenomic screens of human gut microbiota

Autor: Akil Akhtar, Madhu Lata, Sonali Sunsunwal, Amit Yadav, Kajal LNU, srikrishna subramanian, T.N.C. Ramya

Publikováno v: Communications Biology. 6

Uncultured microbes represent a huge untapped biological resource of novel genes and gene products. Although recent genomic and metagenomic sequencing efforts have led to the identification of numerous genes that are homologous to existing annotated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::922c9ab97e95aeffd4069a391c536d3a
https://doi.org/10.1038/s42003-023-04718-0

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Biofilm inhibitory effect of alginate lyases on mucoid P. aeruginosa from a cystic fibrosis patient

Autor: Meenu Singh, T.N.C. Ramya, Sonali Sunsunwal, Vikas Gautam, Sonal Mahajan

Publikováno v: Biochemistry and Biophysics Reports, Vol 26, Iss, Pp 101028-(2021)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd509ae8324a9f652f92fb97d948f42e
http://www.sciencedirect.com/science/article/pii/S2405580821001229

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Effect of naturally occurring variations of the F-type lectin sequence motif on glycan binding: studies on F-type lectin domains with typical and atypical sequence motifs

Autor: T.N.C. Ramya, Shailza Sharma, Aasawari Khairnar, Ritika Bishnoi

Publikováno v: IUBMB Life. 71:385-397

The typical F-type lectin domain (FLD) has an L-fucose-binding motif [HX(26)RXDX(4)R/K] with conserved basic residues that mediate hydrogen bonding with alpha-L-fucose. About one-third of the nonredundant FLD sequences in the publicly available datab

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::36382bf31dfed08b0b3f781dc7f5e9e2
https://doi.org/10.1002/iub.1994

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Amino acid residues important for D-galactose recognition by the F-type lectin, Ranaspumin-4

Autor: T.N.C. Ramya, Shailza Sharma, Sonali Sunsunwal, Aasawari Khairnar, Sonal Mahajan

Publikováno v: Biochemical and biophysical research communications. 532(1)

F-type lectins are typically L-fucose binding proteins with characteristic L-fucose-binding and calcium-binding sequence motifs, and an F-type lectin fold. An exception is Ranaspumin-4, an F-type lectin of the Tungra frog, Engystomops pustulosus. Ran

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dda0d76bf9be12651135652dcf1023e5
https://pubmed.ncbi.nlm.nih.gov/32819714

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