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    GUCY1B1 guanylate cyclase 1 soluble subunit beta 1 [ Homo sapiens (human) ]

    Gene ID: 2983, updated on 11-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Inflammation in the Human Periodontium Induces Downregulation of the alpha1- and beta1-Subunits of the sGC in Cementoclasts.

    Inflammation in the Human Periodontium Induces Downregulation of the α(1)- and β(1)-Subunits of the sGC in Cementoclasts.
    Korkmaz Y, Puladi B, Galler K, Kämmerer PW, Schröder A, Gölz L, Sparwasser T, Bloch W, Friebe A, Deschner J., Free PMC Article

    04/3/2021
    Results suggest mechanistic insights into the molecular pathway for soluble guanylyl cyclase (sGC) activation.

    Synergistic mutations in soluble guanylyl cyclase (sGC) reveal a key role for interfacial regions in the sGC activation mechanism.
    Childers KC, Yao XQ, Giannakoulias S, Amason J, Hamelberg D, Garcin ED., Free PMC Article

    06/27/2020
    Our observations revealed that rs7638A/C polymorphism of GUCY1B3 and the longer telomere length inclined toward adaptation to high altitude.

    Elevated Vasodilatory Cyclases and Shorter Telomere Length Contribute to High-Altitude Pulmonary Edema.
    Rain M, Chaudhary H, Kukreti R, Thinlas T, Mohammad G, Pasha Q.

    12/22/2018
    Human Red Blood Cells carry catalytically active alpha1beta1-soluble guanylate cyclase (isoform 1). Red cell soluble guanylate cyclase activity is fully preserved in patients with stable coronary artery disease.

    Identification of a soluble guanylate cyclase in RBCs: preserved activity in patients with coronary artery disease.
    Cortese-Krott MM, Mergia E, Kramer CM, Lückstädt W, Yang J, Wolff G, Panknin C, Bracht T, Sitek B, Pernow J, Stasch JP, Feelisch M, Koesling D, Kelm M., Free PMC Article

    07/14/2018
    Inhibition of HDAC3 with targeted therapy could benefit treatment of the diseases associated with sGCbeta1 down-regulation and/or deficiency such as cancer and several vascular-related diseases.

    Epigenetic regulation of soluble guanylate cyclase (sGC) β1 in breast cancer cells.
    Sotolongo A, Mónica FZ, Kots A, Xiao H, Liu J, Seto E, Bian K, Murad F.

    08/26/2017
    The kinetics of heme loss from oxidized sGC was monitored by a new method based on the heme group de-quenching the fluorescence of FlAsH-EDT2.

    The molecular mechanism of heme loss from oxidized soluble guanylate cyclase induced by conformational change.
    Pan J, Zhang X, Yuan H, Xu Q, Zhang H, Zhou Y, Huang ZX, Tan X.

    06/28/2016
    Dynamic interplay between hsp90, apo-sGC-beta1, and sGC-alpha1 in response to NO is unprecedented and represent new steps by which cells can modulate the heme content and activity of sGC for signaling cascades.

    Nitric oxide and heat shock protein 90 activate soluble guanylate cyclase by driving rapid change in its subunit interactions and heme content.
    Ghosh A, Stasch JP, Papapetropoulos A, Stuehr DJ., Free PMC Article

    10/11/2014
    Gene expression in dendritic cells of CCL5 and CXCL5 as well as TIMP1 and GUCY1B3 showed a significant increase within the first 4 days after trauma.

    Subsequent gene expression pattern in dendritic cells following multiple trauma.
    Geiger EV, Maier M, Schiessling S, Wutzler S, Lehnert M, Marzi I, Henrich D.

    08/31/2013
    The G-protein regulator LGN modulates the activity of the NO receptor soluble guanylate cyclase

    The G-protein regulator LGN modulates the activity of the NO receptor soluble guanylate cyclase.
    Chauhan S, Jelen F, Sharina I, Martin E., Free PMC Article

    11/17/2012
    The results indicate that in comparison with the alpha-1 beta-1 isoform, the brain alpha-2 beta-1 isoform exhibits a distinctly different CO/NO affinity and binding rate in favor of NO signaling.

    Structural and functional insights into the heme-binding domain of the human soluble guanylate cyclase α2 subunit and heterodimeric α2β1.
    Wang H, Zhong F, Pan J, Li W, Su J, Huang ZX, Tan X.

    09/22/2012
    We concluded that the alpha-subunit and the beta(1)(191-619) domain exert structural strains on the heme domain.

    Quaternary structure controls ligand dynamics in soluble guanylate cyclase.
    Yoo BK, Lamarre I, Martin JL, Negrerie M., Free PMC Article

    04/28/2012
    Data show that show that it is possible to directly monitor the sGC haem oxidation state in intact cells. By inserting the TC motif into the coding sequence of the beta1 subunit of sGC in transiently transfected Chinese hamster ovary cells.

    Fluorescence dequenching makes haem-free soluble guanylate cyclase detectable in living cells.
    Hoffmann LS, Schmidt PM, Keim Y, Hoffmann C, Schmidt HH, Stasch JP., Free PMC Article

    02/18/2012
    recombinant soluble guanylate cyclase (sGC) beta1 subunit and truncated N-terminal fragments expressed in E. coli; studied interaction between NO and sGC and schematic mechanism was proposed; study provides insights into structure and NO-binding of sGC

    Efficient expression of human soluble guanylate cyclase in Escherichia coli and its signaling-related interaction with nitric oxide.
    Zhong F, Wang H, Ying T, Huang ZX, Tan X.

    10/23/2010
    Results show that NOGCbeta1 and GC-A interact and that NOGCbeta1 regulates atrial natriuretic peptide signaling in HK-2 cells.

    Evidence for cross-talk between atrial natriuretic peptide and nitric oxide receptors.
    Kotlo KU, Rasenick MM, Danziger RS., Free PMC Article

    10/23/2010
    The mutant analysis indicated an importance for not only certain dimerization residue positions, but also an important role for other faces of the coiled coil dimer which might perhaps interact with adjacent domains

    Crystal structure of the signaling helix coiled-coil domain of the beta1 subunit of the soluble guanylyl cyclase.
    Ma X, Beuve A, van den Akker F., Free PMC Article

    05/10/2010
    Although soluble guanylate cyclase(sGC) beta1-subunit expression was increased in mononuclear cells from patients with erectile dysfunction, the sGC activity was reduced

    Soluble guanylate cyclase beta1-subunit expression is increased in mononuclear cells from patients with erectile dysfunction.
    Mateos-Cáceres PJ, Garcia-Cardoso J, Lapuente L, Zamorano-León JJ, Sacristán D, de Prada TP, Calahorra J, Macaya C, Vela-Navarrete R, López-Farré AJ.

    01/21/2010
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