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  1. Article ; Online: The Anti-Cancer Activity of Pentamidine and Its Derivatives (WLC-4059) Is through Blocking the Interaction between S100A1 and RAGE V Domain.

    Parveen, Nuzhat / Chiu, Wei-Jung / Shen, Li-Ching / Chou, Ruey-Hwang / Sun, Chung-Ming / Yu, Chin

    Biomolecules

    2022  Volume 13, Issue 1

    Abstract: The S100A1 protein in humans is a calcium-binding protein. Upon ... ...

    Abstract The S100A1 protein in humans is a calcium-binding protein. Upon Ca
    MeSH term(s) Humans ; Calcium/metabolism ; Magnetic Resonance Spectroscopy ; Neoplasms ; Pentamidine/pharmacology ; Protein Binding ; Signal Transduction
    Chemical Substances Calcium (SY7Q814VUP) ; Pentamidine (673LC5J4LQ) ; MOK protein, human (EC 2.7.11.22) ; S100A1 protein
    Language English
    Publishing date 2022-12-30
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom13010081
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Synthesis of Novel Suramin Analogs With Anti-Proliferative Activity

    Parveen, Nuzhat / Lin, Yan-Liang / Chou, Ruey-Hwang / Sun, Chung-Ming / Yu, Chin

    Frontiers in chemistry

    2022  Volume 9, Page(s) 764200

    Abstract: A promising approach in cancer therapy is the inhibition of cell proliferation using small molecules. In this study, we report the synthesis of suramin derivatives and their applications. We used NMR spectroscopy and docking simulations to confirm ... ...

    Abstract A promising approach in cancer therapy is the inhibition of cell proliferation using small molecules. In this study, we report the synthesis of suramin derivatives and their applications. We used NMR spectroscopy and docking simulations to confirm binding sites and three-dimensional models of the ligand-protein complex. The WST-1 assay was used to assess cell viability and cell proliferation
    Language English
    Publishing date 2022-01-03
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2711776-5
    ISSN 2296-2646
    ISSN 2296-2646
    DOI 10.3389/fchem.2021.764200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Synthesis of Novel Suramin Analogs With Anti-Proliferative Activity via FGF1 and FGFRD2 Blockade

    Nuzhat Parveen / Yan-Liang Lin / Ruey-Hwang Chou / Chung-Ming Sun / Chin Yu

    Frontiers in Chemistry, Vol

    2022  Volume 9

    Abstract: A promising approach in cancer therapy is the inhibition of cell proliferation using small molecules. In this study, we report the synthesis of suramin derivatives and their applications. We used NMR spectroscopy and docking simulations to confirm ... ...

    Abstract A promising approach in cancer therapy is the inhibition of cell proliferation using small molecules. In this study, we report the synthesis of suramin derivatives and their applications. We used NMR spectroscopy and docking simulations to confirm binding sites and three-dimensional models of the ligand-protein complex. The WST-1 assay was used to assess cell viability and cell proliferation in vitro to evaluate the inhibition of protein–protein interactions and to investigate the anti-proliferative activities in a breast cancer cell line. All the suramin derivatives showed anti-proliferative activity by blocking FGF1 binding to its receptor FGFRD2. The dissociation constant was measured by fluorescence spectroscopy. The suramin compound derivatives synthesized herein show potential as novel therapeutic agents for their anti-proliferative activity via the inhibition of protein–protein interactions. The cytotoxicity of these suramin derivatives was lower than that of the parent suramin compound, which may be considered a significant advancement in this field. Thus, these novel suramin derivatives may be considered superior anti-metastasis molecules than those of suramin.
    Keywords protein-ligand interaction ; FGF1 ; FGFRD2 ; NMR ; WST1 assay ; cell proliferation ; Chemistry ; QD1-999
    Language English
    Publishing date 2022-01-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: S100A1 blocks the interaction between p53 and mdm2 and decreases cell proliferation activity.

    Deepu Dowarha / Ruey-Hwang Chou / Chin Yu

    PLoS ONE, Vol 15, Iss 6, p e

    2020  Volume 0234152

    Abstract: About 50% of human cancers across the globe arise due to a mutation in the p53 gene which gives rise to its functional inactive form, and in the rest of the cancer the efficacy of active p53 (wild-type) is hindered by MDM2-mediated degradation. Breakdown ...

    Abstract About 50% of human cancers across the globe arise due to a mutation in the p53 gene which gives rise to its functional inactive form, and in the rest of the cancer the efficacy of active p53 (wild-type) is hindered by MDM2-mediated degradation. Breakdown of the p53-MDM2 association may constitute an effective strategy to stimulate or reinstate the activity of wild type p53, thereby reviving the p53 tumor suppressor capability. S100A1 has been revealed to associate with the N-terminal domain of MDM2 and p53 protein. We utilized NMR spectroscopy to study the interface amongst the S100A1 and N-terminal domain of MDM2. Additionally, the S100A1-MDM2 complex generated through the HADDOCK program was then superimposed with the p53 (peptide) -MDM2 complex reported earlier. The overlay indicated that a segment of S100A1 could block the interaction of p53 (peptide) -MDM2 complex significantly. To further justify our assumption, we performed HSQC-NMR titration for the S100A1 and p53 N-terminal domain (p53-TAD). The data obtained indicated that the S100A1 segment comprising nearly 17 residues have some common residues that interact with both MDM2 and p53-TAD. Further, we synthesized the 17-residue peptide derived from the S100A1 protein and attached it to the cell-penetrating HIV-TAT peptide. The HSQC-NMR competitive binding experiment revealed that Peptide 1 could successfully interfere with the p53-MDM2 interaction. Furthermore, functional effects of the peptide was validated in cancer cells. The results showed that Peptide 1 effectively inhibited cell proliferation, and increased the protein levels of p53 and its downstream p21 in MCF-7 cells. Treatment of Peptide 1 resulted in cell cycle arrest at G2/M phase, and also induced apoptotic cell death at higher concentration. Taken together, the results suggest that disruption of the interaction of p53 and MDM2 by Peptide 1 could activate normal p53 functions, leading to cell cycle arrest and apoptotic cell death in cancer cells. We proposed here that S100A1 could influence ...
    Keywords Medicine ; R ; Science ; Q
    Subject code 572
    Language English
    Publishing date 2020-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Pentamidine inhibit S100A4 - p53 interaction and decreases cell proliferation activity.

    Katte, Revansiddha H / Chou, Ruey-Hwang / Yu, Chin

    Archives of biochemistry and biophysics

    2020  Volume 691, Page(s) 108442

    Abstract: Metastasis-associated S100A4 protein is a small calcium-binding protein typically overexpressed in several tumor forms, and it is widely accepted that S100A4 plays a significant role in the metastasis of cancer. Tumor suppressor p53 is one of the S100A4' ... ...

    Abstract Metastasis-associated S100A4 protein is a small calcium-binding protein typically overexpressed in several tumor forms, and it is widely accepted that S100A4 plays a significant role in the metastasis of cancer. Tumor suppressor p53 is one of the S100A4's main targets. Previous reports show that through p53, S100A4 regulates collagen expression and cell proliferation. When S100A4 interacts with p53, the S100A4 destabilizes wild type p53. In the current study, based on
    MeSH term(s) Antineoplastic Agents/metabolism ; Antineoplastic Agents/pharmacology ; Binding Sites ; Cell Proliferation/drug effects ; Drug Screening Assays, Antitumor ; Humans ; MCF-7 Cells ; Pentamidine/metabolism ; Pentamidine/pharmacology ; Protein Binding ; Protein Multimerization/drug effects ; S100 Calcium-Binding Protein A4/chemistry ; S100 Calcium-Binding Protein A4/metabolism ; Tumor Suppressor Protein p53/chemistry ; Tumor Suppressor Protein p53/metabolism
    Chemical Substances Antineoplastic Agents ; S100 Calcium-Binding Protein A4 ; TP53 protein, human ; Tumor Suppressor Protein p53 ; S100A4 protein, human (142662-27-9) ; Pentamidine (673LC5J4LQ)
    Language English
    Publishing date 2020-07-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2020.108442
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.237: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: S100P Interacts with p53 while Pentamidine Inhibits This Interaction.

    Katte, Revansiddha H / Dowarha, Deepu / Chou, Ruey-Hwang / Yu, Chin

    Biomolecules

    2021  Volume 11, Issue 5

    Abstract: S100P, a small calcium-binding protein, associates with the p53 protein with micromolar affinity. It has been hypothesized that the oncogenic function of S100P may involve binding-induced inactivation of p53. We ... ...

    Abstract S100P, a small calcium-binding protein, associates with the p53 protein with micromolar affinity. It has been hypothesized that the oncogenic function of S100P may involve binding-induced inactivation of p53. We used
    MeSH term(s) Binding Sites ; Calcium-Binding Proteins/chemistry ; Calcium-Binding Proteins/metabolism ; Calcium-Binding Proteins/physiology ; Cell Line, Tumor ; Cell Proliferation ; Humans ; Models, Molecular ; Neoplasm Proteins/chemistry ; Neoplasm Proteins/metabolism ; Neoplasm Proteins/physiology ; Pentamidine/chemistry ; Pentamidine/metabolism ; Protein Binding ; Protein Domains ; Protein Interaction Mapping/methods ; S100 Proteins/chemistry ; S100 Proteins/metabolism ; Tumor Suppressor Protein p53/chemistry ; Tumor Suppressor Protein p53/metabolism ; Tumor Suppressor Protein p53/physiology
    Chemical Substances Calcium-Binding Proteins ; Neoplasm Proteins ; S100 Proteins ; S100P protein, human ; TP53 protein, human ; Tumor Suppressor Protein p53 ; Pentamidine (673LC5J4LQ)
    Language English
    Publishing date 2021-04-24
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom11050634
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: S100A1 blocks the interaction between p53 and mdm2 and decreases cell proliferation activity.

    Dowarha, Deepu / Chou, Ruey-Hwang / Yu, Chin

    PloS one

    2020  Volume 15, Issue 6, Page(s) e0234152

    Abstract: About 50% of human cancers across the globe arise due to a mutation in the p53 gene which gives rise to its functional inactive form, and in the rest of the cancer the efficacy of active p53 (wild-type) is hindered by MDM2-mediated degradation. Breakdown ...

    Abstract About 50% of human cancers across the globe arise due to a mutation in the p53 gene which gives rise to its functional inactive form, and in the rest of the cancer the efficacy of active p53 (wild-type) is hindered by MDM2-mediated degradation. Breakdown of the p53-MDM2 association may constitute an effective strategy to stimulate or reinstate the activity of wild type p53, thereby reviving the p53 tumor suppressor capability. S100A1 has been revealed to associate with the N-terminal domain of MDM2 and p53 protein. We utilized NMR spectroscopy to study the interface amongst the S100A1 and N-terminal domain of MDM2. Additionally, the S100A1-MDM2 complex generated through the HADDOCK program was then superimposed with the p53 (peptide) -MDM2 complex reported earlier. The overlay indicated that a segment of S100A1 could block the interaction of p53 (peptide) -MDM2 complex significantly. To further justify our assumption, we performed HSQC-NMR titration for the S100A1 and p53 N-terminal domain (p53-TAD). The data obtained indicated that the S100A1 segment comprising nearly 17 residues have some common residues that interact with both MDM2 and p53-TAD. Further, we synthesized the 17-residue peptide derived from the S100A1 protein and attached it to the cell-penetrating HIV-TAT peptide. The HSQC-NMR competitive binding experiment revealed that Peptide 1 could successfully interfere with the p53-MDM2 interaction. Furthermore, functional effects of the peptide was validated in cancer cells. The results showed that Peptide 1 effectively inhibited cell proliferation, and increased the protein levels of p53 and its downstream p21 in MCF-7 cells. Treatment of Peptide 1 resulted in cell cycle arrest at G2/M phase, and also induced apoptotic cell death at higher concentration. Taken together, the results suggest that disruption of the interaction of p53 and MDM2 by Peptide 1 could activate normal p53 functions, leading to cell cycle arrest and apoptotic cell death in cancer cells. We proposed here that S100A1 could influence the p53-MDM2 interaction credibly and possibly reactivates the wild type p53 pathway.
    MeSH term(s) Amino Acid Sequence ; Cell Proliferation ; Humans ; MCF-7 Cells ; Molecular Docking Simulation ; Protein Binding ; Protein Domains ; Proto-Oncogene Proteins c-mdm2/chemistry ; Proto-Oncogene Proteins c-mdm2/metabolism ; S100 Proteins/chemistry ; S100 Proteins/metabolism ; Tumor Suppressor Protein p53/chemistry ; Tumor Suppressor Protein p53/metabolism
    Chemical Substances S100 Proteins ; S100A1 protein ; Tumor Suppressor Protein p53 ; MDM2 protein, human (EC 2.3.2.27) ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27)
    Language English
    Publishing date 2020-06-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0234152
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Pentamidine inhibit S100A4 - p53 interaction and decreases cell proliferation activity

    Katte, Revansiddha H / Chou, Ruey-Hwang / Yu, Chin

    Archives of biochemistry and biophysics. 2020 Sept. 30, v. 691

    2020  

    Abstract: Metastasis-associated S100A4 protein is a small calcium-binding protein typically overexpressed in several tumor forms, and it is widely accepted that S100A4 plays a significant role in the metastasis of cancer. Tumor suppressor p53 is one of the S100A4' ... ...

    Abstract Metastasis-associated S100A4 protein is a small calcium-binding protein typically overexpressed in several tumor forms, and it is widely accepted that S100A4 plays a significant role in the metastasis of cancer. Tumor suppressor p53 is one of the S100A4's main targets. Previous reports show that through p53, S100A4 regulates collagen expression and cell proliferation. When S100A4 interacts with p53, the S100A4 destabilizes wild type p53. In the current study, based on ¹H–¹⁵N HSQC NMR experiments and HADDOCK results, S100A4 interacts with the intrinsically unstructured transactivation domain (TAD) of the protein p53 and the pentamidine molecules in the presence of calcium ions. Our results suggest that the p53 TAD and pentamidine molecules share similar binding sites on the S100A4 protein. This observation indicates that a competitive binding mechanism can interfere with the binding of S100A4-p53 and increase the level of p53. Also, we compare different aspects of p53 activity in the WST-1 test using MCF 7 cells. We found that the presence of a pentamidine molecule results in higher p53 activity, which is also reflected in less cell proliferation. Collectively, our results indicate that disrupting the S100A4-p53 interaction would prevent cancer progression, and thus S100A4-p53 inhibitors provide a new avenue for cancer therapy.
    Keywords biophysics ; calcium ; calcium-binding proteins ; cancer therapy ; cell proliferation ; collagen ; metastasis ; neoplasm progression ; neoplasms ; transcriptional activation
    Language English
    Dates of publication 2020-0930
    Publishing place Elsevier Inc.
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2020.108442
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    In stock of ZB MED Bonn / Germany

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  9. Article ; Online: S100B as an Antagonist To Interfere with the Interface Area Flanked by S100A11 and RAGE V Domain.

    Dowarha, Deepu / Chou, Ruey-Hwang / Yu, Chin

    ACS omega

    2018  Volume 3, Issue 8, Page(s) 9689–9698

    Abstract: ... The ... ...

    Abstract The Ca
    Language English
    Publishing date 2018-08-22
    Publishing country United States
    Document type Journal Article
    ISSN 2470-1343
    ISSN (online) 2470-1343
    DOI 10.1021/acsomega.8b00922
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  10. Article ; Online: S100B as an Antagonist To Interfere with the Interface Area Flanked by S100A11 and RAGE V Domain

    Deepu Dowarha / Ruey-Hwang Chou / Chin Yu

    ACS Omega, Vol 3, Iss 8, Pp 9689-

    2018  Volume 9698

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2018-08-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
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