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  1. Article ; Online: Role and implications of the CXCL12/CXCR4/CXCR7 axis in atherosclerosis: still a debate.

    Murad, Hussam A S / Rafeeq, Misbahuddin M / Alqurashi, Thamer M A

    Annals of medicine

    2021  Volume 53, Issue 1, Page(s) 1598–1612

    Abstract: Atherosclerosis is one of the leading causes of mortality and morbidity worldwide. Chemokines and their receptors are implicated in the pathogenesis of atherosclerosis. CXCL12 is a member of the chemokine family exerting a myriad role in atherosclerosis ... ...

    Abstract Atherosclerosis is one of the leading causes of mortality and morbidity worldwide. Chemokines and their receptors are implicated in the pathogenesis of atherosclerosis. CXCL12 is a member of the chemokine family exerting a myriad role in atherosclerosis through its classical CXCR4 and atypical ACKR3 (CXCR7) receptors. The modulatory and regulatory functional spectrum of CXCL12/CXCR4/ACKR3 axis in atherosclerosis spans from proatherogenic, prothrombotic and proinflammatory to atheroprotective, plaque stabilizer and dyslipidemia rectifier. This diverse continuum is executed in a wide range of biological units including endothelial cells (ECs), progenitor cells, macrophages, monocytes, platelets, lymphocytes, neutrophils and vascular smooth muscle cells (VSMCs) through complex heterogeneous and homogenous coupling of CXCR4 and ACKR3 receptors, employing different downstream signalling pathways, which often cross-talk among themselves and with other signalling interactomes. Hence, a better understanding of this structural and functional heterogeneity and complex phenomenon involving CXCL12/CXCR4/ACKR3 axis in atherosclerosis would not only help in formulation of novel therapeutics, but also in elucidation of the CXCL12 ligand and its receptors, as possible diagnostic and prognostic biomarkers.Key messagesThe role of CXCL12
    MeSH term(s) Atherosclerosis/blood ; Chemokine CXCL12 ; Endothelial Cells ; Humans ; Receptors, CXCR ; Receptors, CXCR4 ; Signal Transduction
    Chemical Substances ACKR3 protein, human ; CXCL12 protein, human ; CXCR4 protein, human ; Chemokine CXCL12 ; Receptors, CXCR ; Receptors, CXCR4
    Language English
    Publishing date 2021-09-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1004226-x
    ISSN 1365-2060 ; 1651-2219 ; 0785-3890 ; 1743-1387
    ISSN (online) 1365-2060 ; 1651-2219
    ISSN 0785-3890 ; 1743-1387
    DOI 10.1080/07853890.2021.1974084
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Correction: Ashraf et al. Inhibition of Microtubule Affinity Regulating Kinase 4 by Metformin: Exploring the Neuroprotective Potential of Antidiabetic Drug through Spectroscopic and Computational Approaches.

    Ashraf, Ghulam Md / DasGupta, Debarati / Alam, Mohammad Zubair / Baeesa, Saleh S / Alghamdi, Badrah S / Anwar, Firoz / Alqurashi, Thamer M A / Sharaf, Sharaf E / Al Abdulmonem, Waleed / Alyousef, Mohammed A / Alhumaydhi, Fahad A / Shamsi, Anas

    Molecules (Basel, Switzerland)

    2023  Volume 28, Issue 2

    Abstract: The updated affiliation information can be seen in the affiliation part of this correction [ ... ]. ...

    Abstract The updated affiliation information can be seen in the affiliation part of this correction [...].
    Language English
    Publishing date 2023-01-06
    Publishing country Switzerland
    Document type Published Erratum
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules28020600
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The role of membrane trafficking and retromer complex in Parkinson's and Alzheimer's disease.

    Abdul-Rahman, Toufik / Ghosh, Shankhaneel / Kalmanovich, Jacob B / Awuah, Andrew Wireko / Zivcevska, Marija / Khalifa, Samar / Bassey, Esther Edet / Ali, Namarig Alnil / Ferreira, Matheus Mendes Dos Santos / Umar, Tungki Pratama / Garg, Neil / Nweze, Victor Nnanna / Inturu, Venkata Sai Sulekhya / Abdelwahab, Maya Magdy / Kurian, Sneha / Alexiou, Athanasios / Alfaleh, Mohammed / Alqurashi, Thamer M A / Ashraf, Ghulam Md

    Journal of neuroscience research

    2024  Volume 102, Issue 1, Page(s) e25261

    Abstract: Membrane trafficking is a physiological process encompassing different pathways involved in transporting cellular products across cell membranes to specific cell locations via encapsulated vesicles. This process is required for cells to mature and ... ...

    Abstract Membrane trafficking is a physiological process encompassing different pathways involved in transporting cellular products across cell membranes to specific cell locations via encapsulated vesicles. This process is required for cells to mature and function properly, allowing them to adapt to their surroundings. The retromer complex is a complex composed of nexin proteins and peptides that play a vital role in the endosomal pathway of membrane trafficking. In humans, any interference in normal membrane trafficking or retromer complex can cause profound changes such as those seen in neurodegenerative disorders such as Alzheimer's and Parkinson's. Several studies have explored the potential causative mechanisms in developing both disease processes; however, the role of retromer trafficking in their pathogenesis is becoming increasingly significant with promising therapeutic applications. This manuscript describes the processes involved in membrane transport and the roles of the retromer in the onset and progression of Alzheimer's and Parkinson's. Moreover, we will also explore how these aberrant mechanisms may serve as possible avenues for treatment development in both diseases and the prospect of its future application.
    MeSH term(s) Humans ; Alzheimer Disease ; Parkinson Disease ; Cell Membrane ; Biological Transport ; Microtubule-Associated Proteins
    Chemical Substances Microtubule-Associated Proteins
    Language English
    Publishing date 2024-01-29
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 195324-2
    ISSN 1097-4547 ; 0360-4012
    ISSN (online) 1097-4547
    ISSN 0360-4012
    DOI 10.1002/jnr.25261
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Inhibition of Microtubule Affinity Regulating Kinase 4 by Metformin: Exploring the Neuroprotective Potential of Antidiabetic Drug through Spectroscopic and Computational Approaches.

    Ashraf, Ghulam Md / DasGupta, Debarati / Alam, Mohammad Zubair / Baeesa, Saleh S / Alghamdi, Badrah S / Anwar, Firoz / Alqurashi, Thamer M A / Sharaf, Sharaf E / Al Abdulmonem, Waleed / Alyousef, Mohammed A / Alhumaydhi, Fahad A / Shamsi, Anas

    Molecules (Basel, Switzerland)

    2022  Volume 27, Issue 14

    Abstract: Microtubule affinity regulating kinase 4 (MARK4) regulates the mechanism of microtubules by its ability to phosphorylate the microtubule-associated proteins (MAP's). MARK4 is known for its major role in tau phosphorylation via phosphorylating ... ...

    Abstract Microtubule affinity regulating kinase 4 (MARK4) regulates the mechanism of microtubules by its ability to phosphorylate the microtubule-associated proteins (MAP's). MARK4 is known for its major role in tau phosphorylation via phosphorylating Ser
    MeSH term(s) Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Diabetes Mellitus, Type 2/drug therapy ; Diabetes Mellitus, Type 2/metabolism ; Humans ; Hypoglycemic Agents/metabolism ; Hypoglycemic Agents/pharmacology ; Metformin/pharmacology ; Microtubules/metabolism ; Molecular Docking Simulation ; Protein Binding ; Protein Serine-Threonine Kinases
    Chemical Substances Hypoglycemic Agents ; Metformin (9100L32L2N) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2022-07-21
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules27144652
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Unravelling Binding of Human Serum Albumin with Galantamine: Spectroscopic, Calorimetric, and Computational Approaches.

    Ashraf, Ghulam Md / Gupta, Debarati Das / Alam, Mohammad Zubair / Baeesa, Saleh Salem / Alghamdi, Badrah S / Anwar, Firoz / Alqurashi, Thamer M A / Al Abdulmonem, Waleed / Alyousef, Mohammed A / Alhumaydhi, Fahad A / Shamsi, Anas

    ACS omega

    2022  Volume 7, Issue 38, Page(s) 34370–34377

    Abstract: Human serum albumin (HSA), an abundant plasma protein, binds to various ligands, acting as a transporter for numerous endogenous and exogenous substances. Galantamine (GAL), an alkaloid, treats cognitive decline in mild to moderate Alzheimer's disease ... ...

    Abstract Human serum albumin (HSA), an abundant plasma protein, binds to various ligands, acting as a transporter for numerous endogenous and exogenous substances. Galantamine (GAL), an alkaloid, treats cognitive decline in mild to moderate Alzheimer's disease and other memory impairments. A vital step in pharmacological profiling involves the interaction of plasma protein with the drugs, and this serves as an essential platform for pharmaceutical industry advancements. This study is carried out to understand the binding mechanism of GAL with HSA using computational and experimental approaches. Molecular docking revealed that GAL preferentially occupies Sudlow's site I, i.e., binds to subdomain IIIA. The results unveiled that GAL binding does not induce any conformational change in HSA and hence does not compromise the functionality of HSA. Molecular dynamics simulation (250 ns) deciphered the stability of the HSA-GAL complex. We performed the fluorescence binding and isothermal titration calorimetry (ITC) to analyze the actual binding of GAL with HSA. The results suggested that GAL binds to HSA with a significant binding affinity. ITC measurements also delineated thermodynamic parameters associated with the binding of GAL to HSA. Altogether, the present study deciphers the binding mechanism of GAL with HSA.
    Language English
    Publishing date 2022-09-19
    Publishing country United States
    Document type Journal Article
    ISSN 2470-1343
    ISSN (online) 2470-1343
    DOI 10.1021/acsomega.2c04004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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