[
    {
        "title": "Hepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain.",
        "journal": "Journal of virology",
        "date": "2001",
        "authors": "Taylor DR, Tian B, Romano PR, Hinnebusch AG, Lai MM, Mathews MB",
        "reference": {
            "type": "PubMed",
            "id": "11152499",
            "url": "https://pubmed.ncbi.nlm.nih.gov/11152499"
        },
        "referenced_glycans": [],
        "referenced_proteins": [
            {
                "uniprot_canonical_ac": "O75569-1",
                "protein_name": "Interferon-inducible double-stranded RNA-dependent protein kinase activator A",
                "gene_name": "PRKRA",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q9Y4X5-1",
                "protein_name": "E3 ubiquitin-protein ligase ARIH1",
                "gene_name": "ARIH1",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q15633-1",
                "protein_name": "RISC-loading complex subunit TARBP2",
                "gene_name": "TARBP2",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "O15111-1",
                "protein_name": "Inhibitor of nuclear factor kappa-B kinase subunit alpha",
                "gene_name": "CHUK",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "O14933-1",
                "protein_name": "Ubiquitin/ISG15-conjugating enzyme E2 L6",
                "gene_name": "UBE2L6",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "P68363-1",
                "protein_name": "Tubulin alpha-1B chain",
                "gene_name": "TUBA1B",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q6PEY2-1",
                "protein_name": "Tubulin alpha-3E chain",
                "gene_name": "TUBA3E",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "P68366-1",
                "protein_name": "Tubulin alpha-4A chain",
                "gene_name": "TUBA4A",
                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q71U36-1",
                "protein_name": "Tubulin alpha-1A chain",
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                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "P52564-1",
                "protein_name": "Dual specificity mitogen-activated protein kinase kinase 6",
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                "tax_name": "Human"
            },
            {
                "uniprot_canonical_ac": "Q9BVA1-1",
                "protein_name": "Tubulin beta-2B chain",
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            {
                "uniprot_canonical_ac": "Q12905-1",
                "protein_name": "Interleukin enhancer-binding factor 2",
                "gene_name": "ILF2",
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            {
                "uniprot_canonical_ac": "Q8N2Z9-1",
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                "tax_name": "Human"
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            },
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            {
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                "start_pos": 242,
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    {
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        "title": "Enhanced antiviral and antiproliferative properties of a STAT1 mutant unable to interact with the protein kinase PKR.",
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    {
        "title": "Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop.",
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    {
        "title": "Protein kinase PKR is required for platelet-derived growth factor signaling of c-fos gene expression via Erks and Stat3.",
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    {
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        "title": "Gene-specific regulation by general translation factors.",
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    {
        "title": "Inactivation of the PKR protein kinase and stimulation of mRNA translation by the cellular co-chaperone P58(IPK) does not require J domain function.",
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        "authors": "Yan Wei, Gale Michael J, Tan Seng-Lai, Katze Michael G",
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        "title": "The anti-apoptotic function of Hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein, FANCC.",
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    {
        "title": "Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKR.",
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    {
        "title": "The carboxy-terminal, M3 motifs of PACT and TRBP have opposite effects on PKR activity.",
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    {
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    {
        "title": "The Fanconi anemia proteins functionally interact with the protein kinase regulated by RNA (PKR).",
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        "title": "Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition.",
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    {
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        "journal": "The Journal of biological chemistry",
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        "authors": "Wang S, Raven JF, Baltzis D, Kazemi S, Brunet DV, Hatzoglou M, Tremblay ML, Koromilas AE",
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    {
        "title": "The N-terminus of PKR is responsible for the activation of the NF-kappaB signaling pathway by interacting with the IKK complex.",
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        "title": "Double-stranded RNA-dependent protein kinase phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 mediates apoptosis.",
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    {
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    {
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        "title": "Nck-1 interacts with PKR and modulates its activation by dsRNA.",
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    {
        "title": "PKR, a p53 target gene, plays a crucial role in the tumor-suppressor function of p53.",
        "journal": "Proceedings of the National Academy of Sciences of the United States of America",
        "date": "2009-05-12",
        "authors": "Yoon Cheol-Hee, Lee Eun-Soo, Lim Dae-Seog, Bae Yong-Soo",
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    {
        "title": "RNA-specific adenosine deaminase ADAR1 suppresses measles virus-induced apoptosis and activation of protein kinase PKR.",
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    {
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    {
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    {
        "title": "PKR is not a universal target of tumor suppressor p53 in response to genotoxic stress.",
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        "title": "The double-stranded RNA-dependent protein kinase differentially regulates insulin receptor substrates 1 and 2 in HepG2 cells.",
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    {
        "title": "Multiple forms of PKR present in the nuclei of acute leukemia cells represent an active kinase that is responsive to stress.",
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    {
        "title": "The cellular TAR RNA binding protein, TRBP, promotes HIV-1 replication primarily by inhibiting the activation of double-stranded RNA-dependent kinase PKR.",
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    {
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    {
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    {
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        "authors": "Shen Shensi, Niso-Santano Mireia, Adjemian Sandy, Takehara Tetsuo, Malik Shoaib Ahmad, Minoux Herv\u00e9, Souquere Sylvie, Mari\u00f1o Guillermo, Lachkar Sylvie, Senovilla Laura, Galluzzi Lorenzo, Kepp Oliver, Pierron G\u00e9rard, Maiuri Maria Chiara, Hikita Hayato, Kroemer Romano, Kroemer Guido",
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        "title": "Identification of the PKR nuclear interactome reveals roles in ribosome biogenesis, mRNA processing and cell division.",
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        "title": "NF90 exerts antiviral activity through regulation of PKR phosphorylation and stress granules in infected cells.",
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        "authors": "Wen Xi, Huang Xiaofeng, Mok Bobo Wing-Yee, Chen Yixin, Zheng Min, Lau Siu-Ying, Wang Pui, Song Wenjun, Jin Dong-Yan, Yuen Kwok-Yung, Chen Honglin",
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    {
        "title": "IPS-1 plays an essential role in dsRNA-induced stress granule formation by interacting with PKR and promoting its activation.",
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        "date": "2014-06-01",
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                "tax_name": "Human"
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                "uniprot_canonical_ac": "P0DPH8-1",
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                "uniprot_canonical_ac": "Q8NB91-1",
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            {
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                "protein_name": "Signal transducer and activator of transcription 1-alpha/beta",
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            {
                "uniprot_canonical_ac": "Q0VG06-1",
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            {
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            {
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            {
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                "reference_species": "Homo sapiens [9606]"
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                "comment": "Abolishes nuclear location.",
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                "comment": "No effect on nuclear location. No effect on RNA binding.",
                "evidence": [
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                "sequence_org": "I",
                "sequence_mut": "N",
                "comment": "Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with S-719 and N-723.",
                "evidence": [
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                "sequence_org": "IGELVRYLN",
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                "comment": "Disrupts the bi-partite nuclear localization signal and abolishes nuclear location.",
                "evidence": [
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                "sequence_org": "E",
                "sequence_mut": "A",
                "comment": "No effect on nuclear location; when associated with A-721 and A-724.",
                "evidence": [
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                        "url": "https://www.uniprot.org/uniprotkb/P55265"
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                ],
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                "sequence_org": "L",
                "sequence_mut": "S",
                "comment": "Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with N-716 and N-723.",
                "evidence": [
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                "start_pos": 721,
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                "sequence_org": "R",
                "sequence_mut": "A",
                "comment": "No effect on nuclear location; when associated with A-721 and A-724.",
                "evidence": [
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                        "id": "P55265",
                        "url": "https://www.uniprot.org/uniprotkb/P55265"
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                        "id": "24753571",
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                ],
                "uniprot_canonical_ac": "P55265-1"
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                "start_pos": 723,
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                "sequence_org": "L",
                "sequence_mut": "N",
                "comment": "Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with N-716 and S-719.",
                "evidence": [
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                "sequence_org": "N",
                "sequence_mut": "A",
                "comment": "No effect on nuclear location; when associated with A-718 and A-721.",
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                "comment": "Disrupts nuclear localization signal. No effect on RNA binding.",
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                "comment": "Strongly impaired RNA binding. No effect on nuclear location.",
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        "abstract": "",
        "glycosylation": [],
        "snv": [],
        "phosphorylation": [],
        "glycation": [],
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        "title": "p53-derived host restriction of HIV-1 replication by protein kinase R-mediated Tat phosphorylation and inactivation.",
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        "title": "The Regulatory and Kinase Domains but Not the Interdomain Linker Determine Human Double-stranded RNA-activated Kinase (PKR) Sensitivity to Inhibition by Viral Non-coding RNAs.",
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    {
        "title": "Activated PKR inhibits pancreatic \u03b2-cell proliferation through sumoylation-dependent stabilization of P53.",
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    {
        "title": "Regulation of PKR by RNA: formation of active and inactive dimers.",
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    {
        "title": "Essential role of protein kinase R antagonism by TRS1 in human cytomegalovirus replication.",
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    {
        "title": "Activation of PKR by short stem-loop RNAs containing single-stranded arms.",
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        "title": "Human noncoding RNA 886 (nc886) adopts two structurally distinct conformers that are functionally opposing regulators of PKR.",
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        "authors": "Calderon Brenda M, Conn Graeme L",
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        "title": "ADAR1 and PACT contribute to efficient translation of transcripts containing HIV-1 trans-activating response (TAR) element.",
        "journal": "The Biochemical journal",
        "date": "2017",
        "authors": "Chukwurah E, Handy I, Patel RC",
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    {
        "title": "Auto-phosphorylation Represses Protein Kinase R Activity.",
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        "authors": "Wang Die, de Weerd Nicole A, Willard Belinda, Polekhina Galina, Williams Bryan R G, Sadler Anthony J",
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    {
        "title": "Non-coding RNA 886 promotes renal cell carcinoma growth and metastasis through the Janus kinase 2/signal transducer and activator of transcription 3 signaling pathway.",
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    {
        "title": "Inhibition of the inflammatory response to stress by targeting interaction between PKR and its cellular activator PACT.",
        "journal": "Scientific reports",
        "date": "2017-11-23",
        "authors": "Dabo Stephanie, Maillard Patrick, Collados Rodriguez Milagros, Hansen Marianne Dor\u00e9, Mazouz Sabrina, Bigot Donna-Joe, Tible Marion, Janvier Genevi\u00e8ve, Helynck Olivier, Cassonnet Patricia, Jacob Yves, Bellalou Jacques, Gatignol Anne, Patel Rekha C, Hugon Jacques, Munier-Lehmann H\u00e9l\u00e8ne, Meurs Eliane F",
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        "title": "Contribution of the two dsRBM motifs to the double-stranded RNA binding and protein interactions of PACT.",
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    {
        "title": "Stress-induced TRBP phosphorylation enhances its interaction with PKR to regulate cellular survival.",
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        "authors": "Chukwurah E, Patel RC",
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    {
        "title": "Nc886 is epigenetically repressed in prostate cancer and acts as a tumor suppressor through the inhibition of cell growth.",
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        "date": "2018-02-02",
        "authors": "Fort Rafael Sebasti\u00e1n, Math\u00f3 Cecilia, Geraldo Murilo Vieira, Ottati Mar\u00eda Carolina, Yamashita Alex Shimura, Saito Kelly Cristina, Leite Katia Ramos Moreira, M\u00e9ndez Manuel, Maedo Noem\u00ed, M\u00e9ndez Laura, Garat Beatriz, Kimura Edna Teruko, Sotelo-Silveira Jos\u00e9 Roberto, Duhagon Mar\u00eda Ana",
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    {
        "title": "Human ADAR1 Prevents Endogenous RNA from Triggering Translational Shutdown.",
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        "authors": "Chung Hachung, Calis Jorg J A, Wu Xianfang, Sun Tony, Yu Yingpu, Sarbanes Stephanie L, Dao Thi Viet Loan, Shilvock Abigail R, Hoffmann H-Heinrich, Rosenberg Brad R, Rice Charles M",
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    {
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    {
        "title": "Inflammation kinase PKR phosphorylates \u03b1-synuclein and causes \u03b1-synuclein-dependent cell death.",
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        "authors": "Reimer Lasse, Vesterager Louise Buur, Betzer Cristine, Zheng Jin, Nielsen L\u00e6rke Dalsgaard, Kofoed Rikke Hahn, Lassen Louise Berkhoudt, B\u00f8lcho Ulrik, Paludan S\u00f8ren Riis, Fog Karina, Jensen Poul Henning",
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    {
        "title": "PKR Senses Nuclear and Mitochondrial Signals by Interacting with Endogenous Double-Stranded RNAs.",
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    {
        "title": "The search for a PKR code-differential regulation of protein kinase R activity by diverse RNA and protein regulators.",
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        "date": "2019",
        "authors": "Bou-Nader C, Gordon JM, Henderson FE, Zhang J",
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