Výsledky vyhledávání - "Agneyo Ganguly"

Plasmid DNA Undergoes Two Compaction Regimes under Macromolecular Crowding

Autor: Suparna Khatun, Anurag Singh, Kumari Shikha, Agneyo Ganguly, Amar Nath Gupta

Publikováno v: ACS Macro Letters. 11:186-192

The laser light scattering experiments were performed to explore the role of dextran (size (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c013eca6ab05f142b00a367ed753c14
https://doi.org/10.1021/acsmacrolett.1c00593

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Residues at the interface between zinc binding and winged helix domains of human RECQ1 play a significant role in DNA strand annealing activity

Autor: Madhuparna Bose, Swagata Mukhopadhyay, Amit Das, Chetan Kumar Jain, Sunandan Mukherjee, Kumari Shikha, Tulika Das, Mayukh Chakraborty, Agneyo Ganguly

Publikováno v: Nucleic Acids Research

RECQ1 is the shortest among the five human RecQ helicases comprising of two RecA like domains, a zinc-binding domain and a RecQ C-terminal domain containing the winged-helix (WH). Mutations or deletions on the tip of a β-hairpin located in the WH do

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https://doi.org/10.1093/nar/gkab968

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The catalytic core of Leishmania donovani RECQ helicase unwinds a wide spectrum of DNA substrates and is stimulated by replication protein A

Autor: Agneyo Ganguly, Suparna Khatun, Debajyoti De, Gugulothu Sriram Bharath, Mayukh Chakraborty, Kumari Shikha, Susmita Ghosh, Swagata Mukhopadhyay, Amar Gupta

Publikováno v: The FEBS journalReferences. 289(2)

RecQ helicases are superfamily 2 (SF2) DNA helicases that unwind a wide spectrum of complex DNA structures in a 3' to 5' direction and are involved in maintaining genome stability. RecQ helicases from protozoan parasites have gained significant inter

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c485d780bcee4e1860fa620f9929184
https://pubmed.ncbi.nlm.nih.gov/34355508

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Repulsive interaction induces fibril formation and their growth

Autor: Agneyo Ganguly, Nisha Pawar, Amar Gupta, Suparna Khatun, Kumari Shikha

Publikováno v: International Journal of Biological Macromolecules. 123:20-25

In a type-II diabetes disease, amylin protein takes an incorrect structure that leads to the formation of the amyloid fibril. The conversion mechanism of amyloid fibril is not well understood. We have observed a repulsive interaction, in terms of sec

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https://doi.org/10.1016/j.ijbiomac.2018.10.205

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Human RecQ helicases in transcription-associated stress management: bridging the gap between DNA and RNA metabolism

Autor: Surasree Pal, Agneyo Ganguly, Tulika Das

Publikováno v: Biological chemistryReferences. 402(5)

RecQ helicases are a highly conserved class of DNA helicases that play crucial role in almost all DNA metabolic processes including replication, repair and recombination. They are able to unwind a wide variety of complex intermediate DNA structures t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9abeb4e69bb531cd2a48c056d7e05d4b
https://pubmed.ncbi.nlm.nih.gov/33567180

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RecQ Family Helicases in Replication Fork Remodeling and Repair: Opening New Avenues towards the Identification of Potential Targets for Cancer Chemotherapy

Autor: Agneyo Ganguly, Chetan Kumar Jain, Swagata Mukhopadhyay

Publikováno v: Anti-cancer agents in medicinal chemistry. 20(11)

Replication fork reversal and restart has gained immense interest as a central response mechanism to replication stress following DNA damage. Although the exact mechanism of fork reversal has not been elucidated precisely, the involvement of diverse

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https://pubmed.ncbi.nlm.nih.gov/32418530

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The latch modulates nucleotide and DNA binding to the helicase-like domain of Thermotoga maritima reverse gyrase and is required for positive DNA supercoiling

Autor: Yoandris del Toro Duany, Dagmar Klostermeier, Agneyo Ganguly, M.G. Rudolph

Publikováno v: Nucleic acids research
Nucleic Acids Research

Reverse gyrase is the only topoisomerase that can introduce positive supercoils into DNA in an ATP-dependent process. It has a modular structure and harnesses a helicase-like domain to support a topoisomerase activity, thereby creating the unique fun

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bccb500896d0cdea68af955369c2d92f
http://doc.rero.ch/record/303980/files/gkq1048.pdf

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Reverse Gyrase Transiently Unwinds Double-Stranded DNA in an ATP-Dependent Reaction

Autor: Agneyo Ganguly, Dagmar Klostermeier, Yoandris del Toro Duany

Publikováno v: Journal of molecular biology

Reverse gyrase is a unique DNA topoisomerase that catalyzes the introduction of positive supercoils into DNA in an ATP-dependent reaction. It consists of a helicase domain that functionally cooperates with a topoisomerase domain. Different models for

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