LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 8 of total 8

Search options

  1. Article: Novel Aspects of Renal Magnesium Homeostasis.

    Giménez-Mascarell, Paula / Schirrmacher, Carlotta Else / Martínez-Cruz, Luis Alfonso / Müller, Dominik

    Frontiers in pediatrics

    2018  Volume 6, Page(s) 77

    Abstract: Magnesium ( ... ...

    Abstract Magnesium (Mg
    Language English
    Publishing date 2018-04-09
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2711999-3
    ISSN 2296-2360
    ISSN 2296-2360
    DOI 10.3389/fped.2018.00077
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Current Structural Knowledge on the CNNM Family of Magnesium Transport Mediators.

    Giménez-Mascarell, Paula / González-Recio, Irene / Fernández-Rodríguez, Cármen / Oyenarte, Iker / Müller, Dominik / Martínez-Chantar, María Luz / Martínez-Cruz, Luis Alfonso

    International journal of molecular sciences

    2019  Volume 20, Issue 5

    Abstract: The cyclin and cystathionine β-synthase (CBS) domain magnesium transport mediators, CNNMs, are key players in maintaining the homeostasis of magnesium in different organs. The human family includes four members, whose impaired activity causes diseases ... ...

    Abstract The cyclin and cystathionine β-synthase (CBS) domain magnesium transport mediators, CNNMs, are key players in maintaining the homeostasis of magnesium in different organs. The human family includes four members, whose impaired activity causes diseases such as Jalili Syndrome or Familial Hypomagnesemia, but is also linked to neuropathologic disorders, altered blood pressure, and infertility. Recent findings demonstrated that CNNMs are associated with the highly oncogenic phosphatases of the regenerating liver to promote tumor growth and metastasis, which has attracted renewed focus on their potential exploitation as targets for cancer treatment. However, the exact function of CNNMs remains unclear and is subject to debate, proposed as either direct transporters, sensors, or homeostatic factors. This review gathers the current structural knowledge on the CNNM family, highlighting similarities and differences with the closely related structural partners such as the bacterial Mg
    MeSH term(s) Cation Transport Proteins/chemistry ; Cation Transport Proteins/genetics ; Cation Transport Proteins/metabolism ; Crystallography, X-Ray ; Humans ; Magnesium/metabolism ; Models, Molecular ; Mutation ; Neoplasms/genetics ; Neoplasms/metabolism ; Phosphoric Monoester Hydrolases/metabolism ; Protein Binding
    Chemical Substances Cation Transport Proteins ; Phosphoric Monoester Hydrolases (EC 3.1.3.2) ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2019-03-06
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms20051135
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Crystal structure of cystathionine β-synthase from honeybee Apis mellifera.

    Giménez-Mascarell, Paula / Majtan, Tomas / Oyenarte, Iker / Ereño-Orbea, June / Majtan, Juraj / Klaudiny, Jaroslav / Kraus, Jan P / Martínez-Cruz, Luis Alfonso

    Journal of structural biology

    2017  Volume 202, Issue 1, Page(s) 82–93

    Abstract: Cystathionine β-synthase (CBS), the key enzyme in the transsulfuration pathway, links methionine metabolism to the biosynthesis of cellular redox controlling molecules. CBS catalyzes the pyridoxal-5'-phosphate-dependent condensation of serine and ... ...

    Abstract Cystathionine β-synthase (CBS), the key enzyme in the transsulfuration pathway, links methionine metabolism to the biosynthesis of cellular redox controlling molecules. CBS catalyzes the pyridoxal-5'-phosphate-dependent condensation of serine and homocysteine to form cystathionine, which is subsequently converted into cysteine. Besides maintaining cellular sulfur amino acid homeostasis, CBS also catalyzes multiple hydrogen sulfide-generating reactions using cysteine and homocysteine as substrates. In mammals, CBS is activated by S-adenosylmethionine (AdoMet), where it can adopt two different conformations (basal and activated), but exists as a unique highly active species in fruit fly Drosophila melanogaster. Here we present the crystal structure of CBS from honeybey Apis mellifera, which shows a constitutively active dimeric species and let explain why the enzyme is not allosterically regulated by AdoMet. In addition, comparison of available CBS structures unveils a substrate-induced closure of the catalytic cavity, which in humans is affected by the AdoMet-dependent regulation and likely impaired by the homocystinuria causing mutation T191M.
    MeSH term(s) Amino Acid Sequence ; Animals ; Bees ; Crystallography, X-Ray ; Cystathionine beta-Synthase/chemistry ; Cystathionine beta-Synthase/genetics ; Cystathionine beta-Synthase/metabolism ; Cysteine/metabolism ; Homocysteine/metabolism ; Humans ; Insect Proteins/chemistry ; Insect Proteins/genetics ; Insect Proteins/metabolism ; Models, Molecular ; Protein Conformation ; Protein Multimerization ; S-Adenosylmethionine/metabolism ; Sequence Homology, Amino Acid ; Substrate Specificity
    Chemical Substances Insect Proteins ; Homocysteine (0LVT1QZ0BA) ; S-Adenosylmethionine (7LP2MPO46S) ; Cystathionine beta-Synthase (EC 4.2.1.22) ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2017-12-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1032718-6
    ISSN 1095-8657 ; 1047-8477
    ISSN (online) 1095-8657
    ISSN 1047-8477
    DOI 10.1016/j.jsb.2017.12.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1428: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article: Potential Pharmacological Chaperones for Cystathionine Beta-Synthase-Deficient Homocystinuria.

    Majtan, Tomas / Pey, Angel L / Gimenez-Mascarell, Paula / Martínez-Cruz, Luis Alfonso / Szabo, Csaba / Kožich, Viktor / Kraus, Jan P

    Handbook of experimental pharmacology

    2017  Volume 245, Page(s) 345–383

    Abstract: Classical homocystinuria (HCU) is the most common loss-of-function inborn error of sulfur amino acid metabolism. HCU is caused by a deficiency in enzymatic degradation of homocysteine, a toxic intermediate of methionine transformation to cysteine, ... ...

    Abstract Classical homocystinuria (HCU) is the most common loss-of-function inborn error of sulfur amino acid metabolism. HCU is caused by a deficiency in enzymatic degradation of homocysteine, a toxic intermediate of methionine transformation to cysteine, chiefly due to missense mutations in the cystathionine beta-synthase (CBS) gene. As with many other inherited disorders, the pathogenic mutations do not target key catalytic residues, but rather introduce structural perturbations leading to an enhanced tendency of the mutant CBS to misfold and either to form nonfunctional aggregates or to undergo proteasome-dependent degradation. Correction of CBS misfolding would represent an alternative therapeutic approach for HCU. In this review, we summarize the complex nature of CBS, its multi-domain architecture, the interplay between the three cofactors required for CBS function [heme, pyridoxal-5'-phosphate (PLP), and S-adenosylmethionine (SAM)], as well as the intricate allosteric regulatory mechanism only recently understood, thanks to advances in CBS crystallography. While roughly half of the patients respond to treatment with a PLP precursor pyridoxine, many studies suggested usefulness of small chemicals, such as chemical and pharmacological chaperones or proteasome inhibitors, rescuing mutant CBS activity in cellular and animal models of HCU. Non-specific chemical chaperones and proteasome inhibitors assist in mutant CBS folding process and/or prevent its rapid degradation, thus resulting in increased steady-state levels of the enzyme and CBS activity. Recent interest in the field and available structural information will hopefully yield CBS-specific compounds, by using high-throughput screening and computational modeling of novel ligands, improving folding, stability, and activity of CBS mutants.
    MeSH term(s) Animals ; Cystathionine beta-Synthase/chemistry ; Cystathionine beta-Synthase/deficiency ; Cystathionine beta-Synthase/physiology ; Enzyme Stability ; High-Throughput Screening Assays ; Homocystinuria/drug therapy ; Humans ; Molecular Chaperones/therapeutic use ; Protein Folding ; Protein Processing, Post-Translational
    Chemical Substances Molecular Chaperones ; Cystathionine beta-Synthase (EC 4.2.1.22)
    Language English
    Publishing date 2017-11-08
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 0171-2004
    ISSN 0171-2004
    DOI 10.1007/164_2017_72
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Sign. bis Bd. 125 (1997): 1982 A 2146: Show issues
     danach: Sign. bei den Einzelbänden: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: Current Structural Knowledge on the CNNM Family of Magnesium Transport Mediators

    Paula Giménez-Mascarell / Irene González-Recio / Cármen Fernández-Rodríguez / Iker Oyenarte / Dominik Müller / María Luz Martínez-Chantar / Luis Alfonso Martínez-Cruz

    International Journal of Molecular Sciences, Vol 20, Iss 5, p

    2019  Volume 1135

    Abstract: The cyclin and cystathionine β-synthase (CBS) domain magnesium transport mediators, CNNMs, are key players in maintaining the homeostasis of magnesium in different organs. The human family includes four members, whose impaired activity causes diseases ... ...

    Abstract The cyclin and cystathionine β-synthase (CBS) domain magnesium transport mediators, CNNMs, are key players in maintaining the homeostasis of magnesium in different organs. The human family includes four members, whose impaired activity causes diseases such as Jalili Syndrome or Familial Hypomagnesemia, but is also linked to neuropathologic disorders, altered blood pressure, and infertility. Recent findings demonstrated that CNNMs are associated with the highly oncogenic phosphatases of the regenerating liver to promote tumor growth and metastasis, which has attracted renewed focus on their potential exploitation as targets for cancer treatment. However, the exact function of CNNMs remains unclear and is subject to debate, proposed as either direct transporters, sensors, or homeostatic factors. This review gathers the current structural knowledge on the CNNM family, highlighting similarities and differences with the closely related structural partners such as the bacterial Mg2+/Co2+ efflux protein CorC and the Mg2+ channel MgtE.
    Keywords CNNM ; ACDP ; magnesium homeostasis ; magnesium transport ; CBS domain ; cNMP domain ; CNBH domain ; Jalili syndrome ; hypomagnesemia ; cancer ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 572
    Language English
    Publishing date 2019-03-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

    More links

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  6. Article ; Online: Structural Insights into the Intracellular Region of the Human Magnesium Transport Mediator CNNM4.

    Giménez-Mascarell, Paula / Oyenarte, Iker / González-Recio, Irene / Fernández-Rodríguez, Carmen / Corral-Rodríguez, María Ángeles / Campos-Zarraga, Igone / Simón, Jorge / Kostantin, Elie / Hardy, Serge / Díaz Quintana, Antonio / Zubillaga Lizeaga, Mara / Merino, Nekane / Diercks, Tammo / Blanco, Francisco J / Díaz Moreno, Irene / Martínez-Chantar, María Luz / Tremblay, Michel L / Müller, Dominik / Siliqi, Dritan /
    Martínez-Cruz, Luis Alfonso

    International journal of molecular sciences

    2019  Volume 20, Issue 24

    Abstract: The four member family of "Cyclin and Cystathionine β-synthase (CBS) domain divalent metal cation transport mediators", CNNMs, are the least-studied mammalian magnesium transport mediators. CNNM4 is abundant in the brain and the intestinal tract, and its ...

    Abstract The four member family of "Cyclin and Cystathionine β-synthase (CBS) domain divalent metal cation transport mediators", CNNMs, are the least-studied mammalian magnesium transport mediators. CNNM4 is abundant in the brain and the intestinal tract, and its abnormal activity causes Jalili Syndrome. Recent findings show that suppression of CNNM4 in mice promotes malignant progression of intestinal polyps and is linked to infertility. The association of CNNM4 with phosphatases of the regenerating liver, PRLs, abrogates its Mg
    MeSH term(s) Adenosine Triphosphate/chemistry ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Binding Sites ; Biological Transport ; Cation Transport Proteins/chemistry ; Cation Transport Proteins/metabolism ; Humans ; Magnesium/chemistry ; Magnesium/metabolism ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Conformation ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Structure-Activity Relationship
    Chemical Substances CNNM4 protein, human ; Cation Transport Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2019-12-12
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms20246279
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: Structural Basis of the Oncogenic Interaction of Phosphatase PRL-1 with the Magnesium Transporter CNNM2.

    Giménez-Mascarell, Paula / Oyenarte, Iker / Hardy, Serge / Breiderhoff, Tilman / Stuiver, Marchel / Kostantin, Elie / Diercks, Tammo / Pey, Angel L / Ereño-Orbea, June / Martínez-Chantar, María Luz / Khalaf-Nazzal, Reham / Claverie-Martin, Felix / Müller, Dominik / Tremblay, Michel L / Martínez-Cruz, Luis Alfonso

    The Journal of biological chemistry

    2016  Volume 292, Issue 3, Page(s) 786–801

    Abstract: Phosphatases of regenerating liver (PRLs), the most oncogenic of all protein-tyrosine phosphatases (PTPs), play a critical role in metastatic progression of cancers. Recent findings established a new paradigm by uncovering that their association with ... ...

    Abstract Phosphatases of regenerating liver (PRLs), the most oncogenic of all protein-tyrosine phosphatases (PTPs), play a critical role in metastatic progression of cancers. Recent findings established a new paradigm by uncovering that their association with magnesium transporters of the cyclin M (CNNM) family causes a rise in intracellular magnesium levels that promote oncogenic transformation. Recently, however, essential roles for regulation of the circadian rhythm and reproduction of the CNNM family have been highlighted. Here, we describe the crystal structure of PRL-1 in complex with the Bateman module of CNNM2 (CNNM2
    MeSH term(s) Animals ; Cation Transport Proteins/chemistry ; Cation Transport Proteins/genetics ; Cation Transport Proteins/metabolism ; Immediate-Early Proteins/chemistry ; Immediate-Early Proteins/genetics ; Immediate-Early Proteins/metabolism ; Magnesium/chemistry ; Magnesium/metabolism ; Mice ; Neoplasm Metastasis ; Neoplasms/genetics ; Neoplasms/metabolism ; Neoplasms/pathology ; Oncogene Proteins/chemistry ; Oncogene Proteins/genetics ; Oncogene Proteins/metabolism ; Protein Binding ; Protein Domains ; Protein Structure, Secondary ; Protein Tyrosine Phosphatases/chemistry ; Protein Tyrosine Phosphatases/genetics ; Protein Tyrosine Phosphatases/metabolism
    Chemical Substances Cation Transport Proteins ; Cnnm2 protein, mouse ; Immediate-Early Proteins ; Oncogene Proteins ; Protein Tyrosine Phosphatases (EC 3.1.3.48) ; Ptp4a1 protein, mouse (EC 3.1.3.48) ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2016-11-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M116.759944
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article ; Online: Magnesium accumulation upon cyclin M4 silencing activates microsomal triglyceride transfer protein improving NASH.

    Simón, Jorge / Goikoetxea-Usandizaga, Naroa / Serrano-Maciá, Marina / Fernández-Ramos, David / Sáenz de Urturi, Diego / Gruskos, Jessica J / Fernández-Tussy, Pablo / Lachiondo-Ortega, Sofía / González-Recio, Irene / Rodríguez-Agudo, Rubén / Gutiérrez-de-Juan, Virginia / Rodríguez-Iruretagoyena, Begoña / Varela-Rey, Marta / Gimenez-Mascarell, Paula / Mercado-Gomez, María / Gómez-Santos, Beatriz / Fernandez-Rodriguez, Carmen / Lopitz-Otsoa, Fernando / Bizkarguenaga, Maider /
    Dames, Sibylle / Schaeper, Ute / Martin, Franz / Sabio, Guadalupe / Iruzubieta, Paula / Crespo, Javier / Aspichueta, Patricia / Chu, Kevan H-Y / Buccella, Daniela / Martín, César / Delgado, Teresa Cardoso / Martínez-Cruz, Luis Alfonso / Martínez-Chantar, María Luz

    Journal of hepatology

    2021  Volume 75, Issue 1, Page(s) 34–45

    Abstract: Background & aims: Perturbations of intracellular magnesium (Mg: Methods: Serum Mg: Results: Patients with NASH showed hepatic CNNM4 overexpression and dysregulated Mg: Conclusions: CNNM4 is overexpressed in patients with NASH and is ... ...

    Abstract Background & aims: Perturbations of intracellular magnesium (Mg
    Methods: Serum Mg
    Results: Patients with NASH showed hepatic CNNM4 overexpression and dysregulated Mg
    Conclusions: CNNM4 is overexpressed in patients with NASH and is responsible for dysregulated Mg
    Lay summary: Cyclin M4 (CNNM4) is overexpressed in non-alcoholic steatohepatitis (NASH) and promotes the export of magnesium from the liver. The liver-specific silencing of Cnnm4 ameliorates NASH by reducing endoplasmic reticulum stress and promoting the activity of microsomal triglyceride transfer protein.
    MeSH term(s) Animals ; Biological Transport/drug effects ; Carrier Proteins/metabolism ; Cation Transport Proteins/metabolism ; Cells, Cultured ; Disease Models, Animal ; Drug Discovery ; Endoplasmic Reticulum Stress/drug effects ; Gene Expression Regulation ; Hepatocytes/metabolism ; Humans ; Magnesium/blood ; Magnesium/metabolism ; Mice ; Non-alcoholic Fatty Liver Disease/metabolism ; Non-alcoholic Fatty Liver Disease/pathology
    Chemical Substances CNNM4 protein, human ; Carrier Proteins ; Cation Transport Proteins ; Cnnm4 protein, mouse ; microsomal triglyceride transfer protein ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2021-02-09
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 605953-3
    ISSN 1600-0641 ; 0168-8278
    ISSN (online) 1600-0641
    ISSN 0168-8278
    DOI 10.1016/j.jhep.2021.01.043
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 2027: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top