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  1. Book ; Online ; E-Book: Chemical biology of the genome

    Roy, Siddhartha / Kundu, Tapas K.

    2021  

    Author's details Siddhartha Roy, Tapas K. Kundu
    Keywords Genomes
    Subject code 572.86
    Language English
    Size 1 online resource (xii, 337 pages) :, illustrations
    Publisher Academic Press, an imprint of Elsevier
    Publishing place London, England
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 0-12-817645-8 ; 0-12-817644-X ; 978-0-12-817644-3 ; 978-0-12-817645-0
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book: Epigenetics

    Kundu, Tapas K.

    development and disease

    (Subcellular biochemistry ; 61)

    2013  

    Author's details Tapas K. Kundu ed
    Series title Subcellular biochemistry ; 61
    Collection
    Keywords Epigenetics ; Gene expression ; Genetic regulation ; Medical genetics
    Subject code 572.865
    Language English
    Size XXVI, 689 S. : Ill., graph. Darst., 24 cm
    Publisher Springer
    Publishing place Dordrecht u.a.
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT017473815
    ISBN 978-94-007-4524-7 ; 94-007-4524-9 ; 9789400745254 ; 9400745257
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2012 A 5946 order for loan Magazin

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  3. Book: Chromatin and disease

    Kundu, Tapas K.

    (Subcellular biochemistry ; 41)

    2007  

    Author's details ed. by Tapas K. Kundu
    Series title Subcellular biochemistry ; 41
    Collection
    Language English
    Size XIII, 433, [22] S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT015022458
    ISBN 1-4020-5465-3 ; 978-1-4020-5465-5
    Database Catalogue ZB MED Medicine, Health

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    Zs A 1068 -41- not available for loan Zeitschriften-Lesesaal

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  4. Article: Metabolic Regulation of Lysine Acetylation: Implications in Cancer.

    Singh, Siddharth / Senapati, Parijat / Kundu, Tapas K

    Sub-cellular biochemistry

    2022  Volume 100, Page(s) 393–426

    Abstract: Lysine acetylation is the second most well-studied post-translational modification after phosphorylation. While phosphorylation regulates signaling cascades, one of the most significant roles of acetylation is regulation of chromatin structure. Acetyl- ... ...

    Abstract Lysine acetylation is the second most well-studied post-translational modification after phosphorylation. While phosphorylation regulates signaling cascades, one of the most significant roles of acetylation is regulation of chromatin structure. Acetyl-coenzyme A (acetyl-CoA) serves as the acetyl group donor for acetylation reactions mediated by lysine acetyltransferases (KATs). On the other hand, NAD+ serves as the cofactor for lysine deacetylases (KDACs). Both acetyl-CoA and NAD+ are metabolites integral to energy metabolism, and therefore, their metabolic flux can regulate the activity of KATs and KDACs impacting the epigenome. In this chapter, we review our current understanding of how metabolic pathways regulate lysine acetylation in normal and cancer cells.
    MeSH term(s) Humans ; Acetylation ; Lysine/metabolism ; Acetyl Coenzyme A/metabolism ; NAD/metabolism ; Protein Processing, Post-Translational ; Neoplasms/genetics
    Chemical Substances Lysine (K3Z4F929H6) ; Acetyl Coenzyme A (72-89-9) ; NAD (0U46U6E8UK)
    Language English
    Publishing date 2022-10-27
    Publishing country United States
    Document type Review ; Journal Article
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-3-031-07634-3_12
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Correction for Batta and Kundu, "Activation of p53 Function by Human Transcriptional Coactivator PC4: Role of Protein-Protein Interaction, DNA Bending, and Posttranslational Modifications".

    Batta, Kiran / Kundu, Tapas K

    Molecular and cellular biology

    2020  Volume 40, Issue 19

    Language English
    Publishing date 2020-09-14
    Publishing country United States
    Document type Journal Article ; Published Erratum
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00364-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1666: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  6. Article ; Online: Lysine Acetyltransferases (KATs) in Disguise: Diseases Implications.

    Srivastava, Swati / Kumar, Sanjay / Bhatt, Rohini / Ramachandran, Ravishankar / Trivedi, Arun K / Kundu, Tapas K

    Journal of biochemistry

    2023  Volume 173, Issue 6, Page(s) 417–433

    Abstract: Acetylation is one of the key post-translational protein modifications catalysed by the protein lysine acetyltransferases (KATs). KATs catalyse the transfer of acetyl groups to the epsilon-amino groups of lysine residues in histones and non-histone ... ...

    Abstract Acetylation is one of the key post-translational protein modifications catalysed by the protein lysine acetyltransferases (KATs). KATs catalyse the transfer of acetyl groups to the epsilon-amino groups of lysine residues in histones and non-histone proteins. Because of its wide range of target proteins, KATs regulate many biological processes, and their aberrant activities may underlie several human diseases, including cancer, asthma, Chronic Obstructive Pulmonary Disease (COPD), and neurological disorders. Unlike most of the histone modifying enzymes, such as lysine methyltransferases, KATs do not possess any conserved domain like SET domain of lysine methyltransferases. However, almost all the major families of KATs are found to be transcriptional coactivators or adaptor proteins, with defined catalytic domains, called canonical KATs. Over the past two decades, a few proteins have been discovered to possess intrinsic KAT activity but are not classical coactivators. We would like to categorize them as non-canonical KATs (NC-KATs). These NC-KATs include general transcription factors TAFII250, mammalian TFIIIC complex, and mitochondrial protein GCN5L1, etc. This review focuses on our understanding, as well as controversies regarding non-canonical KATs, where we compare the structural and functional similarities and dissimilarities of non-canonical KATs with the canonical KATs. This review also highlights the potential role of NC-KATs in health and diseases.
    MeSH term(s) Animals ; Humans ; Lysine Acetyltransferases/chemistry ; Lysine Acetyltransferases/metabolism ; Lysine/metabolism ; Histones/metabolism ; Transcription Factors/metabolism ; Mammals
    Chemical Substances Lysine Acetyltransferases (EC 2.3.1.32) ; Lysine (K3Z4F929H6) ; Histones ; Transcription Factors
    Language English
    Publishing date 2023-03-11
    Publishing country England
    Document type Review ; Journal Article
    ZDB-ID 218073-x
    ISSN 1756-2651 ; 0021-924X
    ISSN (online) 1756-2651
    ISSN 0021-924X
    DOI 10.1093/jb/mvad022
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Autophagy in Cancer: A Metabolic Perspective.

    Sikder, Sweta / Mondal, Atanu / Das, Chandrima / Kundu, Tapas K

    Sub-cellular biochemistry

    2022  Volume 100, Page(s) 143–172

    Abstract: Autophagy is an intracellular catabolic degradative process in which damaged cellular organelles, unwanted proteins and different cytoplasmic components get recycled to maintain cellular homeostasis or metabolic balance. During autophagy, a double ... ...

    Abstract Autophagy is an intracellular catabolic degradative process in which damaged cellular organelles, unwanted proteins and different cytoplasmic components get recycled to maintain cellular homeostasis or metabolic balance. During autophagy, a double membrane vesicle is formed to engulf these cytosolic materials and fuse to lysosomes wherein the entire cargo degrades to be used again. Because of this unique recycling ability of cells, autophagy is a universal stress response mechanism. Dysregulation of autophagy leads to several diseases, including cancer, neurodegeneration and microbial infection. Thus, autophagy machineries have become targets for therapeutics. This chapter provides an overview of the paradoxical role of autophagy in tumorigenesis in the perspective of metabolism.
    MeSH term(s) Humans ; Autophagy ; Cytosol/metabolism ; Homeostasis ; Lysosomes ; Neoplasms/metabolism
    Language English
    Publishing date 2022-10-27
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-3-031-07634-3_5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Visible-light excited polar Dion-Jacobson Rb(Bi

    Panda, Debendra Prasad / Singh, Akash Kumar / Kundu, Tapas K / Sundaresan, A

    Journal of materials chemistry. B

    2022  Volume 10, Issue 6, Page(s) 935–944

    Abstract: Rare-earth ion-activated oxide phosphors are beneficial to overcome problems like photobleaching, reduced lifetime, and the blinking of organic dyes and quantum dots for bioimaging applications. In this work, we report that the phosphors Rb( ... ...

    Abstract Rare-earth ion-activated oxide phosphors are beneficial to overcome problems like photobleaching, reduced lifetime, and the blinking of organic dyes and quantum dots for bioimaging applications. In this work, we report that the phosphors Rb(Bi
    MeSH term(s) Calcium Compounds ; Europium ; HEK293 Cells ; HeLa Cells ; Humans ; Light ; Luminescent Agents ; Oxides ; Titanium
    Chemical Substances Calcium Compounds ; Luminescent Agents ; Oxides ; perovskite (12194-71-7) ; Europium (444W947O8O) ; Titanium (D1JT611TNE)
    Language English
    Publishing date 2022-02-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2702241-9
    ISSN 2050-7518 ; 2050-750X
    ISSN (online) 2050-7518
    ISSN 2050-750X
    DOI 10.1039/d1tb02445k
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: The Largest Subunit of Human TFIIIC Complex, TFIIIC220, a Lysine Acetyltransferase Targets Histone H3K18.

    Basu, Moumita / Bhatt, Rohini / Sharma, Anjali / Boopathi, Ramachandran / Das, Sadhan / Kundu, Tapas K

    Journal of biochemistry

    2023  Volume 175, Issue 2, Page(s) 205–213

    Abstract: TFIIIC is a multi-subunit complex required for tRNA transcription by RNA polymerase III. Human TFIIIC holo-complex possesses lysine acetyltransferase activity that aids in relieving chromatin-mediated repression for RNA polymerase III-mediated ... ...

    Abstract TFIIIC is a multi-subunit complex required for tRNA transcription by RNA polymerase III. Human TFIIIC holo-complex possesses lysine acetyltransferase activity that aids in relieving chromatin-mediated repression for RNA polymerase III-mediated transcription and chromatin assembly. Here we have characterized the acetyltransferase activity of the largest and DNA-binding subunit of TFIIIC complex, TFIIIC220. Purified recombinant human TFIIIC220 acetylated core histones H3, H4 and H2A in vitro. Moreover, we have identified the putative catalytic domain of TFIIIC220 that efficiently acetylates core histones in vitro. Mutating critical residues of the putative acetyl-CoA binding 'P loop' drastically reduced the catalytic activity of the acetyltransferase domain. Further analysis showed that the knockdown of TFIIIC220 in mammalian cell lines dramatically reduces global H3K18 acetylation level, which was rescued by overexpression of the putative acetyltransferase domain of human TFIIIC220. Our findings indicated a possibility of a crucial role for TFIIIC220 in maintaining acetylation homeostasis in the cell.
    MeSH term(s) Animals ; Humans ; Histones/metabolism ; Lysine Acetyltransferases/metabolism ; RNA Polymerase III/metabolism ; Histone Acetyltransferases/genetics ; Histone Acetyltransferases/metabolism ; Acetylation ; Mammals ; Transcription Factors, TFIII
    Chemical Substances Histones ; transcription factor TFIIIC ; Lysine Acetyltransferases (EC 2.3.1.32) ; RNA Polymerase III (EC 2.7.7.6) ; Histone Acetyltransferases (EC 2.3.1.48) ; Transcription Factors, TFIII
    Language English
    Publishing date 2023-11-14
    Publishing country England
    Document type Journal Article
    ZDB-ID 218073-x
    ISSN 1756-2651 ; 0021-924X
    ISSN (online) 1756-2651
    ISSN 0021-924X
    DOI 10.1093/jb/mvad088
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Disrupting the interaction between a p53 gain-of-function mutant and the transcriptional co-activator PC4 reverses drug resistance in cancer cells.

    Mondal, Priya / Roy, Kumar Singha / Bhagat, Supriya Varsha / Singh, Siddharth / Chattopadhyay, Anupa / Ghosh, Damayanti Das / Kundu, Tapas K / Roychoudhury, Susanta / Roy, Siddhartha

    FEBS letters

    2024  

    Abstract: PC4 is a chromatin-associated protein and transcriptional coactivator whose role in gene regulation by wild-type p53 is now well known. Little is known about the roles of PC4 in tumor cells bearing mutant p53 genes. We show that PC4 associates with one ... ...

    Abstract PC4 is a chromatin-associated protein and transcriptional coactivator whose role in gene regulation by wild-type p53 is now well known. Little is known about the roles of PC4 in tumor cells bearing mutant p53 genes. We show that PC4 associates with one of the tumor-associated gain-of-function p53 mutants, R273H. This association drives its recruitment to two promoters, UBE2C and MDR1, known to be responsible for imparting aggressive growth and resistance to many drugs. Here, we introduced a peptide that disrupts the PC4-R273Hp53 interaction to tumor cells bearing the R273HTP53 gene, which led to a lowering of MDR1 expression and abrogation of drug resistance in a mutant-specific manner. The results suggest that the PC4-R273Hp53 interaction may be a promising target for reducing proliferation and drug resistance in tumors.
    Language English
    Publishing date 2024-04-25
    Publishing country England
    Document type Journal Article
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14890
    Database MEDical Literature Analysis and Retrieval System OnLINE

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