High-throughput immunoblotting. Ubiquitiin-like protein ISG15 modifies key regulators of signal transduction (Q27863761)

3

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Michael P Malakhov

1

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Ernest C Borden

5

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Dong-Er Zhang

6

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Barbara S Jacobs

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

9 May 2003

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published in

1 reference

Accumulation of an mRNA and protein in interferon-treated Ehrlich ascites tumour cells

PubMed

volume

278

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page(s)

16608-13

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issue

19

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cites work

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Identification of genes differentially regulated by interferon alpha, beta, or gamma using oligonucleotide arrays

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Novel NEMO/IkappaB kinase and NF-kappa B target genes at the pre-B to immature B cell transition

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Immunoregulatory properties of ISG15, an interferon-induced cytokine

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Mechanisms underlying ubiquitination

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Ubiquitin-mediated proteolysis: biological regulation via destruction

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Conjugation of the 15-kDa interferon-induced ubiquitin homolog is distinct from that of ubiquitin

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Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein

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UBP43 (USP18) specifically removes ISG15 from conjugated proteins

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A novel ubiquitin-specific protease, UBP43, cloned from leukemia fusion protein AML1-ETO-expressing mice, functions in hematopoietic cell differentiation

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Cloning and characterization of a novel human ubiquitin-specific protease, a homologue of murine UBP43 (Usp18)

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Molecular responses of macrophages to porcine reproductive and respiratory syndrome virus infection

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RNase-L-dependent destabilization of interferon-induced mRNAs. A role for the 2-5A system in attenuation of the interferon response

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Cloning and characterization of human ubiquitin-processing protease-43 from terminally differentiated human melanoma cells using a rapid subtraction hybridization protocol RaSH.

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Lipopolysaccharide activates the expression of ISG15-specific protease UBP43 via interferon regulatory factor 3.

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Dysregulation of protein modification by ISG15 results in brain cell injury

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Protein ISGylation modulates the JAK-STAT signaling pathway

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Biochemistry. All in the ubiquitin family

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Ubiquitin and its kin: how close are the family ties?

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Serpin 2a is induced in activated macrophages and conjugates to a ubiquitin homolog

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Jaks and STATs: biological implications

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Protein regulation by monoubiquitin

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Structure and functions of the 20S and 26S proteasomes

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Phospholipase C-gamma as a signal-transducing element

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Platelet-derived growth factor-dependent cellular transformation requires either phospholipase Cgamma or phosphatidylinositol 3 kinase

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The protein tyrosine kinase JAK1 complements defects in interferon-alpha/beta and -gamma signal transduction

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Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the Jaks in cytokine-induced biologic responses

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Targeted disruption of the mouse Stat1 gene results in compromised innate immunity to viral disease

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Targeted disruption of the Stat1 gene in mice reveals unexpected physiologic specificity in the JAK-STAT signaling pathway

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Anchorage-dependent ERK signaling--mechanisms and consequences

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Pharmacological inhibitors of MAPK pathways.

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The ubiquitin-activating enzyme E1-like protein in lung cancer cell lines

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Identifiers

DOI

10.1074/JBC.M208435200

1 reference

Consolidated OpenCitations Corpus – April 2017

3866732

3866732

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference