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  1. Article ; Online: Structural and functional comparison of magnesium transporters throughout evolution.

    Franken, G A C / Huynen, M A / Martínez-Cruz, L A / Bindels, R J M / de Baaij, J H F

    Cellular and molecular life sciences : CMLS

    2022  Volume 79, Issue 8, Page(s) 418

    Abstract: Magnesium ( ... ...

    Abstract Magnesium (Mg
    MeSH term(s) Biological Transport ; Cations, Divalent/metabolism ; Magnesium/metabolism ; Membrane Transport Proteins/metabolism ; Phosphotransferases/metabolism
    Chemical Substances Cations, Divalent ; Membrane Transport Proteins ; Phosphotransferases (EC 2.7.-) ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2022-07-12
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-022-04442-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 195: Show issues Location:
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  2. Article ; Online: Structural and functional comparison of magnesium transporters throughout evolution

    Franken, G. A. C. / Huynen, M. A. / Martínez-Cruz, L. A. / Bindels, R. J. M. / de Baaij, J. H. F.

    Cell. Mol. Life Sci.. 2022 Aug., v. 79, no. 8 p.418-418

    2022  

    Abstract: Magnesium (Mg²⁺) is the most prevalent divalent intracellular cation. As co-factor in many enzymatic reactions, Mg²⁺ is essential for protein synthesis, energy production, and DNA stability. Disturbances in intracellular Mg²⁺ concentrations, therefore, ... ...

    Abstract Magnesium (Mg²⁺) is the most prevalent divalent intracellular cation. As co-factor in many enzymatic reactions, Mg²⁺ is essential for protein synthesis, energy production, and DNA stability. Disturbances in intracellular Mg²⁺ concentrations, therefore, unequivocally result in delayed cell growth and metabolic defects. To maintain physiological Mg²⁺ levels, all organisms rely on balanced Mg²⁺ influx and efflux via Mg²⁺ channels and transporters. This review compares the structure and the function of prokaryotic Mg²⁺ transporters and their eukaryotic counterparts. In prokaryotes, cellular Mg²⁺ homeostasis is orchestrated via the CorA, MgtA/B, MgtE, and CorB/C Mg²⁺ transporters. For CorA, MgtE, and CorB/C, the motifs that form the selectivity pore are conserved during evolution. These findings suggest that CNNM proteins, the vertebrate orthologues of CorB/C, also have Mg²⁺ transport capacity. Whereas CorA and CorB/C proteins share the gross quaternary structure and functional properties with their respective orthologues, the MgtE channel only shares the selectivity pore with SLC41 Na⁺/Mg²⁺ transporters. In eukaryotes, TRPM6 and TRPM7 Mg²⁺ channels provide an additional Mg²⁺ transport mechanism, consisting of a fusion of channel with a kinase. The unique features these TRP channels allow the integration of hormonal, cellular, and transcriptional regulatory pathways that determine their Mg²⁺ transport capacity. Our review demonstrates that understanding the structure and function of prokaryotic magnesiotropic proteins aids in our basic understanding of Mg²⁺ transport.
    Keywords DNA ; cations ; cell growth ; energy ; eukaryotic cells ; evolution ; homeostasis ; magnesium ; prokaryotic cells ; protein synthesis ; transcription (genetics) ; vertebrates
    Language English
    Dates of publication 2022-08
    Size p. 418.
    Publishing place Springer International Publishing
    Document type Article ; Online
    Note Review
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-022-04442-8
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    In stock of ZB MED Bonn / Germany

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  3. Article: Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability.

    Chi, Y I / Martinez-Cruz, L A / Jancarik, J / Swanson, R V / Robertson, D E / Kim, S H

    FEBS letters

    1999  Volume 445, Issue 2-3, Page(s) 375–383

    Abstract: The glycosyl hydrolases are an important group of enzymes that are responsible for cleaving a range of biologically significant carbohydrate compounds. Structural information on these enzymes has provided useful information on their molecular basis for ... ...

    Abstract The glycosyl hydrolases are an important group of enzymes that are responsible for cleaving a range of biologically significant carbohydrate compounds. Structural information on these enzymes has provided useful information on their molecular basis for the functional variations, while the characterization of the structural features that account for the high thermostability of proteins is of great scientific and biotechnological interest. To these ends we have determined the crystal structure of the beta-glycosidase from a hyperthermophilic archeon Thermosphaera aggregans. The structure is a (beta/alpha)8 barrel (TIM-barrel), as seen in other glycosyl hydrolase family 1 members, and forms a tetramer. Inspection of the active site and the surrounding area reveals two catalytic glutamate residues consistent with the retaining mechanism and the surrounding polar and aromatic residues consistent with a monosaccharide binding site. Comparison of this structure with its mesophilic counterparts implicates a variety of structural features that could contribute to the thermostability. These include an increased number of surface ion pairs, an increased number of internal water molecules and a decreased surface area upon forming an oligomeric quaternary structure.
    MeSH term(s) Amino Acid Sequence ; Base Sequence ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; DNA, Complementary ; Desulfurococcaceae/enzymology ; Enzyme Stability ; Glycoside Hydrolases/chemistry ; Molecular Sequence Data ; Protein Conformation ; Sequence Homology, Amino Acid ; Structure-Activity Relationship
    Chemical Substances DNA, Complementary ; Glycoside Hydrolases (EC 3.2.1.-)
    Language English
    Publishing date 1999-02-26
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/s0014-5793(99)00090-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 282: Show issues Location:
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  4. Article: Pancreatic cancer escape variants that evade immunogene therapy through loss of sensitivity to IFNgamma-induced apoptosis.

    Mazzolini, G / Narvaiza, I / Martinez-Cruz, L A / Arina, A / Barajas, M / Galofré, J C / Qian, C / Mato, J M / Prieto, J / Melero, I

    Gene therapy

    2003  Volume 10, Issue 13, Page(s) 1067–1078

    Abstract: Combined injections into experimental tumor nodules of adenovirus encoding IL-12 and certain chemokines are capable to induce immune-mediated complete regressions. In this study, we found that the combination of two adenoviruses, one encoding IL-12 and ... ...

    Abstract Combined injections into experimental tumor nodules of adenovirus encoding IL-12 and certain chemokines are capable to induce immune-mediated complete regressions. In this study, we found that the combination of two adenoviruses, one encoding IL-12 and other MIP3alpha (AdCMVIL-12+AdCMVMIP3alpha) was very successful in treating CT-26-derived colon carcinomas. However, in experimental tumors generated from the pancreatic carcinoma cell line Panc02 such combined treatment induces 50% of macroscopic complete regressions, although local relapses within 1 week are almost constant. We derived cell lines from such relapsing tumors and found that experimental malignancies derived from their inoculum were not amenable to treatment in any case with AdCMVIL-12+AdCMVMIP-3alpha. Importantly, relapsing cell lines were insensitive to in vitro induction of apoptosis by IFNgamma, in clear contrast with the original Panc02 cells. Comparative analyses by cDNA arrays of relapsing cell lines versus wild-type Panc02 were performed revealing an important number of genes (383) whose expression levels were modified more than two-fold. These changes grouped in certain gene ontology categories should harbor the mechanistic explanations of the acquired selective resistance to IFNgamma.
    MeSH term(s) Adenoviridae/genetics ; Animals ; Apoptosis ; Chemokine CCL20 ; Chemokines, CC/genetics ; Colonic Neoplasms/therapy ; Female ; Genetic Therapy/methods ; Genetic Vectors/administration & dosage ; Immunotherapy/methods ; Interferon-gamma/therapeutic use ; Interleukin-12/genetics ; Macrophage Inflammatory Proteins/genetics ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Neoplasms, Experimental/genetics ; Neoplasms, Experimental/immunology ; Neoplasms, Experimental/therapy ; Oligonucleotide Array Sequence Analysis ; Pancreatic Neoplasms/genetics ; Pancreatic Neoplasms/immunology ; Pancreatic Neoplasms/therapy ; Receptors, CCR6 ; Receptors, Chemokine ; Receptors, Interferon/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Transduction, Genetic ; Tumor Cells, Cultured ; Tumor Escape/genetics
    Chemical Substances CCL20 protein, human ; CCR6 protein, human ; Chemokine CCL20 ; Chemokines, CC ; Macrophage Inflammatory Proteins ; Receptors, CCR6 ; Receptors, Chemokine ; Receptors, Interferon ; Interleukin-12 (187348-17-0) ; Interferon-gamma (82115-62-6)
    Language English
    Publishing date 2003-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1191036-7
    ISSN 1476-5462 ; 0969-7128
    ISSN (online) 1476-5462
    ISSN 0969-7128
    DOI 10.1038/sj.gt.3301957
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3991: Show issues Location:
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  5. Article: S-Adenosylmethionine revisited: its essential role in the regulation of liver function.

    Avila, Matiías A / García-Trevijano, Elena R / Martínez-Chantar, María L / Latasa, M Ujue / Pérez-Mato, Isabel / Martínez-Cruz, L A / del Pino, Manuel M / Corrales, Fernando J / Mato, José M

    Alcohol (Fayetteville, N.Y.)

    2002  Volume 27, Issue 3, Page(s) 163–167

    Abstract: Dietary methionine is mainly metabolized in the liver where it is converted into S-adenosylmethionine (AdoMet), the main biologic methyl donor. This reaction is catalyzed by methionine adenosyltransferase I/III (MAT I/III), the product of MAT1A gene, ... ...

    Abstract Dietary methionine is mainly metabolized in the liver where it is converted into S-adenosylmethionine (AdoMet), the main biologic methyl donor. This reaction is catalyzed by methionine adenosyltransferase I/III (MAT I/III), the product of MAT1A gene, which is exclusively expressed in this organ. It was first observed that serum methionine levels were elevated in experimental models of liver damage and in liver cirrhosis in human beings. Results of further studies showed that this pathological alteration was due to reduced MAT1A gene expression and MAT I/III enzyme inactivation associated with liver injury. Synthesis of AdoMet is essential to all cells in the organism, but it is in the liver where most of the methylation reactions take place. The central role played by AdoMet in cellular function, together with the observation that AdoMet administration reduces liver damage caused by different agents and improves survival of alcohol-dependent patients with cirrhosis, led us to propose that alterations in methionine metabolism could play a role in the onset of liver disease and not just be a consequence of it. In the present work, we review the recent findings that support this hypothesis and highlight the mechanisms behind the hepatoprotective role of AdoMet.
    MeSH term(s) Animals ; Humans ; Liver/physiology ; Liver Diseases, Alcoholic/drug therapy ; Liver Diseases, Alcoholic/physiopathology ; S-Adenosylmethionine/physiology ; S-Adenosylmethionine/therapeutic use
    Chemical Substances S-Adenosylmethionine (7LP2MPO46S)
    Language English
    Publishing date 2002-05-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 605912-0
    ISSN 0741-8329
    ISSN 0741-8329
    DOI 10.1016/s0741-8329(02)00228-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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