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Book ; Online ; E-Book: Cardiovascular toxicity and therapeutic modalities targeting cardio-oncology

Qamar, Imteyaz / Maurya, Pawan Kumar

from basic research to advanced study

2022

Author's details	edited by Imteyaz Qamar and Pawan Kumar Maurya
Keywords	Cardiovascular toxicology ; Heart/Effect of drugs on.
Subject code	363.73874
Language	English
Size	1 online resource (278 pages) :, color illustrations
Publisher	Academic press
Publishing place	London, England ; San Diego, California ; Cambridge, Massachusetts
Document type	Book ; Online ; E-Book
Remark	Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
ISBN	0-323-90462-9 ; 9780323904612 ; 978-0-323-90462-9 ; 0323904610
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Book ; Online ; E-Book: Novel therapeutic approaches targeting oxidative stress

Maurya, Pawan Kumar / Qamar, Imteyaz

2022

Author's details	edited by Pawan Kumar Maurya, Imteyaz Qamar
Keywords	Oxidative stress/Diagnosis ; Oxidative stress/Treatment
Subject code	616.39
Language	English
Size	1 online resource (294 pages)
Publisher	Academic Press
Publishing place	London
Document type	Book ; Online ; E-Book
Remark	Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
ISBN	0-323-90906-X ; 9780323909051 ; 978-0-323-90906-8 ; 0323909051
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article: New Insights Into Pyridoxal Kinase Inhibitors and Their Antileukemic Effects.

Banerjee, Pallabi / Singh, Tripti / Qamar, Imteyaz

Cureus

2023 Volume 15, Issue 11, Page(s) e48176

Abstract: Pyridoxal kinase (PDXK) plays a pivotal role as an essential enzyme in cellular processes. It catalyzes the phosphorylation of pyridoxal, pyridoxamine, and pyridoxine to generate pyridoxal 5'-phosphate (PLP), the bioactive form of vitamin B6. An ... ...

Abstract	Pyridoxal kinase (PDXK) plays a pivotal role as an essential enzyme in cellular processes. It catalyzes the phosphorylation of pyridoxal, pyridoxamine, and pyridoxine to generate pyridoxal 5'-phosphate (PLP), the bioactive form of vitamin B6. An intriguing link has emerged between elevated expression levels of PDXK and PLP and various types of carcinomas, including leukemia. Leukemic cells have an increased need for vitamin B6 to sustain their survival and rapid growth, highlighting the potential of targeting PDXK-PLP as a promising therapeutic target in cancer treatment. To discover a novel and promising PDXK inhibitor, we conducted a comprehensive screening of compounds derived from both natural sources and drug-like databases. Our approach involved employing structure-based virtual screening and molecular docking techniques to attenuate the phosphorylation of PLP. Among the top six compounds, ZINC095099376 (referred to as C03) emerged as the most potent inhibitor of PDXK, primarily due to its exceptional binding affinity and remarkable specificity for the target protein. Furthermore, our investigation revealed that compound C03 establishes crucial interactions with key residues within the substrate binding site, indicating that it binds at the same site as the co-crystallized ligand. Remarkably, compound C03 inhibited the endogenous PDXK expression, showed anti-proliferative activity, and triggered an intrinsic pathway for apoptosis via the activation of key apoptotic factors in leukemic cells. In summary, these findings strongly indicate that compound C03 holds promise as a novel inhibitor of PDXK, offering the potential for the development of effective treatments for leukemia.
Language	English
Publishing date	2023-11-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2747273-5
ISSN	2168-8184
ISSN	2168-8184
DOI	10.7759/cureus.48176
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Ligand based-design of potential schistosomiasis inhibitors through QSAR, homology modeling, molecular dynamics, pharmacokinetics, and DFT studies.

Ja'afaru, Saudatu C / Uzairu, Adamu / Chandra, Anshuman / Sallau, Muhammed S / Ndukwe, George I / Ibrahim, Muhammad T / Qamar, Imteyaz

Journal of Taibah University Medical Sciences

2024 Volume 19, Issue 2, Page(s) 429–446

Abstract: Objectives: Schistosomiasis, a neglected tropical disease, is a leading cause of mortality in affected geographic areas. Currently, because no vaccine for schistosomiasis is available, control measures rely on widespread administration of the drug ... ...

Abstract	Objectives: Schistosomiasis, a neglected tropical disease, is a leading cause of mortality in affected geographic areas. Currently, because no vaccine for schistosomiasis is available, control measures rely on widespread administration of the drug praziquantel (PZQ). The mass administration of PZQ has prompted concerns regarding the emergence of drug resistance. Therefore, new therapeutic targets and potential compounds are necessary to combat schistosomiasis. Methods: Twenty-four potent derivatives of PZQ were optimized via density functional theory (DFT) at the B3LYP/6-31G∗ level. Quantitative structureactivity relationship (QSAR) models were generated and statistically validated, and a lead candidate was selected to develop therapeutic options with improved efficacy against schistosomiasis. The biological and binding energies of the designed compounds were evaluated. In addition, molecular dynamics; drug-likeness; absorption, distribution, metabolism, excretion, and toxicity (ADMET); and DFT studies were performed on the newly designed compounds. Results: Five QSAR models were generated, among which model 1 had favorable validation parameters (R Conclusion: The proposed compounds exhibited potential drug characteristics, thus indicating their suitability for further investigation to enhance schistosomiasis treatment options.
Language	English
Publishing date	2024-02-26
Publishing country	Saudi Arabia
Document type	Journal Article
ZDB-ID	2817396-X
ISSN	1658-3612 ; 1658-3612
ISSN (online)	1658-3612
ISSN	1658-3612
DOI	10.1016/j.jtumed.2024.02.003
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Identification of high-affinity pyridoxal kinase inhibitors targeting cancer therapy: an integrated docking and molecular dynamics simulation approach.

Banerjee, Pallabi / Chandra, Anshuman / Mohammad, Taj / Singh, Nagendra / Hassan, Md Imtaiyaz / Qamar, Imteyaz

Journal of biomolecular structure & dynamics

2023 , Page(s) 1–18

Abstract: Pyridoxal kinase (PDXK) is a vitamin B6-dependent transferase enzyme encoded by ... ...

Abstract	Pyridoxal kinase (PDXK) is a vitamin B6-dependent transferase enzyme encoded by the
Language	English
Publishing date	2023-08-14
Publishing country	England
Document type	Journal Article
ZDB-ID	49157-3
ISSN	1538-0254 ; 0739-1102
ISSN (online)	1538-0254
ISSN	0739-1102
DOI	10.1080/07391102.2023.2246580
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Article ; Online: Drugs swapping in coronavirus strains: a structural biology view.

Gurjar, Vaishali / Iqra Kamil, Saiyada / Chandra, Anshuman / Qamar, Imteyaz / Singh, Nagendra

Journal of biomolecular structure & dynamics

2023 Volume 41, Issue 22, Page(s) 13488–13495

Abstract: Coronavirus belongs to the coronaviridae family, having a single-stranded RNA as genetic material of 26-42 kb in size. The first coronavirus infection emerged in 2002, caused by SARS-CoV1. Since then, genome sequences and three-dimensional structures of ... ...

Abstract	Coronavirus belongs to the coronaviridae family, having a single-stranded RNA as genetic material of 26-42 kb in size. The first coronavirus infection emerged in 2002, caused by SARS-CoV1. Since then, genome sequences and three-dimensional structures of crucial proteins and enzymes of the virus have been studied in detail. The novel coronavirus (nCoV) outbreak has caused the COVID19 pandemic, which is responsible for the deaths of millions of people worldwide. The nCoV was later renamed as SARS-CoV2. The details of most of the COV proteins are available at the atomic and molecular levels. The entire genome is made up of 12 open reading frames that code for 27 different proteins. The spike surface glycoprotein, the envelope protein, the nucleocapsid protein, and the membrane protein are the four structural proteins which are required for virus attachment, entrance, assembly, and pathogenicity. The remaining proteins encoded are called non-structural (NSPs) and support the survival of the virus. Several non-structural proteins are also validated targets for drug development against coronavirus and are being used for drug design purposes. To perform a comparative study, sequences and three-dimensional structures of four crucial viral enzymes, Mpro, PLpro, RdRp, and EndoU from SARS-CoV1 and SARS-CoV2 variants were analyzed. The key structural elements and ligands recognizing amino acid residues were found to be similar in enzymes from both strains. The significant sequences and structural resemblance also suggest that a drug developed either for SARS-CoV1 or SARS-CoV2 using these enzymes may also have the potential to cross-react.Communicated by Ramaswamy H. Sarma.
MeSH term(s)	Humans ; RNA, Viral ; SARS-CoV-2/genetics ; COVID-19 ; Nucleocapsid Proteins/chemistry ; Nucleocapsid Proteins/genetics ; Biology
Chemical Substances	RNA, Viral ; Nucleocapsid Proteins
Language	English
Publishing date	2023-02-06
Publishing country	England
Document type	Journal Article
ZDB-ID	49157-3
ISSN	1538-0254 ; 0739-1102
ISSN (online)	1538-0254
ISSN	0739-1102
DOI	10.1080/07391102.2023.2175037
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Article: Expression of Regucalcin, a calcium-binding protein is regulated by hypoxia-inducible factor-1α

Singh, Tripti / Banerjee, Pallabi / Uditi / Kumari, Sarita / Chopra, Anita / Singh, Nagendra / Qamar, Imteyaz

Life sciences. 2022 Mar. 01, v. 292

2022

Abstract: Regucalcin (RGN) regulates intracellular Ca²⁺ homeostasis and the activity of several proteins involved in intracellular signaling pathways, which highlights its importance in cell biology. Regucalcin has cytoprotective effects reducing intracellular ... ...

Abstract	Regucalcin (RGN) regulates intracellular Ca²⁺ homeostasis and the activity of several proteins involved in intracellular signaling pathways, which highlights its importance in cell biology. Regucalcin has cytoprotective effects reducing intracellular levels of oxidative stress, also playing a crucial role in the control of cell survival and apoptosis. In an effort to assess its gene regulation, we initially identified the expression of Regucalcin in rat lungs treated with hypoxia at various time points. Previously, HIF-1α expression was also reported to be upregulated in hypoxia. Interestingly hypoxic induced Regucalcin expression in a fashion similar to that of HIF-1α expression in rat lungs. Sequence analysis of the Regucalcin promoter region revealed the presence of putative HRE binding motifs. Further analysis of the 1 kb Regucalcin promoter region with 5′ deletion and point mutants of HRE binding motif showed that the HRE binding site was critical for high promoter activity. In addition, HIF-1α protein binds directly to the HRE binding motifs within the Regucalcin promoter in-vivo, and regulates Regucalcin gene expression. All together, these findings suggest that Regucalcin is the novel target gene of HIF-1α and that Regucalcin gene expression in hypoxia may be regulated by the control of HIF-1α expression.
Keywords	apoptosis ; calcium ; calcium-binding proteins ; cell viability ; gene expression ; genes ; homeostasis ; hypoxia ; oxidative stress ; promoter regions ; rats ; sequence analysis
Language	English
Dates of publication	2022-0301
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	3378-9
ISSN	1879-0631 ; 0024-3205
ISSN (online)	1879-0631
ISSN	0024-3205
DOI	10.1016/j.lfs.2021.120278
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Identification of a novel and potent small molecule inhibitor of SRPK1: mechanism of dual inhibition of SRPK1 for the inhibition of cancer progression.

Chandra, Anshuman / Ananda, Hanumappa / Singh, Nagendra / Qamar, Imteyaz

Aging

2020 Volume 13, Issue 1, Page(s) 163–180

Abstract: Protein kinases are the family of attractive enzyme targets for drug design with relevance to cancer biology. Serine arginine protein kinase 1 (SRPK1) is responsible for the phosphorylation of serine/arginine (SR)-rich proteins. Alternative Splicing ... ...

Abstract	Protein kinases are the family of attractive enzyme targets for drug design with relevance to cancer biology. Serine arginine protein kinase 1 (SRPK1) is responsible for the phosphorylation of serine/arginine (SR)-rich proteins. Alternative Splicing Factor/Splicing Factor 2 (ASF/SF2) involved in mRNA editing. ASF/SF2 is over expressed in many cancers and plays crucial roles in the cell survival. Phosphorylation of ASF/SF2 is decisive for its functions in cancer. In search of potential anticancer therapeutic agents for attenuating phosphorylation of ASF/SF2, we have explored specific and potential inhibitors of SRPK1 from natural and drug like compounds databases using
MeSH term(s)	A549 Cells ; Apoptosis/drug effects ; Cell Death/drug effects ; Cell Proliferation/drug effects ; Cell Survival/drug effects ; Drug Design ; Drug Screening Assays, Antitumor ; HeLa Cells ; Humans ; Inhibitory Concentration 50 ; Jurkat Cells ; K562 Cells ; Molecular Docking Simulation ; Phosphorylation ; Protein Kinase Inhibitors/pharmacology ; Protein-Serine-Threonine Kinases/antagonists & inhibitors ; Protein-Serine-Threonine Kinases/metabolism ; RNA, Messenger/metabolism ; Serine-Arginine Splicing Factors/metabolism
Chemical Substances	Protein Kinase Inhibitors ; RNA, Messenger ; SRSF1 protein, human ; Serine-Arginine Splicing Factors (170974-22-8) ; SRPK1 protein, human (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2020-12-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1945-4589
ISSN (online)	1945-4589
DOI	10.18632/aging.202301
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Article ; Online: Identification of potential inhibitors of SARS-COV-2 endoribonuclease (EndoU) from FDA approved drugs: a drug repurposing approach to find therapeutics for COVID-19.

Chandra, Anshuman / Gurjar, Vaishali / Qamar, Imteyaz / Singh, Nagendra

Journal of biomolecular structure & dynamics

2020 Volume 39, Issue 12, Page(s) 4201–4211

Abstract: SARS-CoV-2 is causative agent of COVID-19, which is responsible for severe social and economic disruption globally. Lack of vaccine or antiviral drug with clinical efficacy suggested that drug repurposing approach may provide a quick therapeutic solution ...

Abstract	SARS-CoV-2 is causative agent of COVID-19, which is responsible for severe social and economic disruption globally. Lack of vaccine or antiviral drug with clinical efficacy suggested that drug repurposing approach may provide a quick therapeutic solution to COVID-19. Nonstructural protein-15 (NSP15) encodes for an uridylate-specific endoribonuclease (EndoU) enzyme, essential for virus life cycle and an attractive target for drug development. We have performed
MeSH term(s)	Antiviral Agents ; COVID-19 ; Drug Repositioning ; Endoribonucleases ; Humans ; Molecular Docking Simulation ; Pharmaceutical Preparations ; SARS-CoV-2
Chemical Substances	Antiviral Agents ; Pharmaceutical Preparations ; Endoribonucleases (EC 3.1.-)
Keywords	covid19
Language	English
Publishing date	2020-06-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	49157-3
ISSN	1538-0254 ; 0739-1102
ISSN (online)	1538-0254
ISSN	0739-1102
DOI	10.1080/07391102.2020.1775127
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Article ; Online: Identification of hot spot residues on serine-arginine protein kinase-1 by molecular dynamics simulation studies.

Chandra, Anshuman / Goyal, Nainee / Qamar, Imteyaz / Singh, Nagendra

Journal of biomolecular structure & dynamics

2020 Volume 39, Issue 5, Page(s) 1579–1587

Abstract: Serine-arginine protein kinase-1 (SRPK1) is a highly specific kinase that recognizes serine-arginine dipeptide repeats and phosphorylates SR rich splicing factor ASF/SF2 in a cell-cycle regulated manner. SRPK1 processively phosphorylates serine residues ... ...

Abstract	Serine-arginine protein kinase-1 (SRPK1) is a highly specific kinase that recognizes serine-arginine dipeptide repeats and phosphorylates SR rich splicing factor ASF/SF2 in a cell-cycle regulated manner. SRPK1 processively phosphorylates serine residues on its substrate ASF/SF2. Elevated expression pattern of both SRPK1 and ASF/SF2 and their association with various carcinomas have established SRPK1 as a potent target for drug design against cancers. In order to develop specific inhibitors the binding of ASF/SF2 to SRPK1 is desired to be selectively interrupted. We have performed molecular dynamics simulation studies on crystal structure of SRPK1 complex with ASF/SF2. The ASF/SF2 acquired a stable binding on the surface of SRPK1 with strong attractive forces. Analysis revealed that there was no major position shifting of the core β-sheet region within the catalytic site of SRPK1 when present in the state of ASF/SF2 bound in comparison to apo form. Global motions of SRPK1 indicated that major stable structural changes occurred after the substrate binding. The interactions between SRPK1 and ASF/SF2 were examined and calculated during molecular dynamics simulation of 1 µs. Molecular dynamics study indicated Arg84, Lys85, Leu86, Lys174, Tyr227 and Leu479 residues of SRPK1 as essential hot spots involved in the stable binding with substrate. Structural analysis of the binding affinity and hot spot investigation provided significant information on ASF/SF2 binding which may also be considered for designing of the novel specific inhibitors of SRPK1 for the applications in cancer therapy.Communicated by Ramaswamy H. Sarma.
MeSH term(s)	Arginine ; Arginine Kinase ; Molecular Dynamics Simulation ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Kinases ; Protein-Serine-Threonine Kinases/metabolism ; RNA-Binding Proteins ; Serine ; Serine-Arginine Splicing Factors/genetics
Chemical Substances	Nuclear Proteins ; RNA-Binding Proteins ; Serine-Arginine Splicing Factors (170974-22-8) ; Serine (452VLY9402) ; Arginine (94ZLA3W45F) ; Protein Kinases (EC 2.7.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Arginine Kinase (EC 2.7.3.3)
Language	English
Publishing date	2020-03-04
Publishing country	England
Document type	Journal Article
ZDB-ID	49157-3
ISSN	1538-0254 ; 0739-1102
ISSN (online)	1538-0254
ISSN	0739-1102
DOI	10.1080/07391102.2020.1734487
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