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protein function  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc protein function
    Protein Function, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 2086 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/protein+function/Protein+A/pmc12592524-23-35-40
    Average 96 stars, based on 2086 article reviews
    protein function - by Bioz Stars, 2026-09
    96/100 stars

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    Related Articles

    Sequencing:

    Article Title: Cysteine-rich zinc finger proteins and the nuclear factor kappa-B pathway
    Article Snippet: .. ZFs are signaled via PTMs of the ZF domain, or adjacent motifs in the full-length sequence, which affects overall protein function and cell signaling ( ; ; ). ..

    Modification:

    Article Title: Targeting endoplasmic reticulum stress and nitroso-redox imbalance in neuroendocrine prostate cancer: the therapeutic role of nitric oxide
    Article Snippet: .. Notably, our previous studies have shown that S-nitrosylation, a post-translational modification that involves the covalent attachment of a nitric oxide (NO) group to the side chain of cysteine residues, plays a critical role in regulating protein function and modulating cancer cell signaling [ ]. ..

    Article Title: Inducible Nitric Oxide Synthase (iNOS): More Than an Inducible Enzyme? Rethinking the Classification of NOS Isoforms.
    Article Snippet: .. Cross-talk between iNOS-derived NO and other signaling pathways NO exerts its biological effects primary through two mechanisms: (1) activation of soluble guanylate cyclase (sGC), which increases cyclic guanosine monophosphate (cGMP) levels, leading to activation of protein kinase G (PKG) and downstream phosphorylation of target proteins; and (2) S-nitrosylation, a reversible post-translational modification in which NO covalently modifies cysteine thiols [85] or binds to transition metals [86], thereby modulating protein function [5]. iNOS-derived NO interacts with several major cell signaling pathways, including NF-κB [81, 87, 88], hypoxia-inducible factor-1 (HIF-1) [89, 90], adenosine monophosphate (AMP)activated protein kinase (AMPK) [91], and Janus kinase/signal transducer and activator of transcription (JAK/STAT) [92] (Figure 2). ..

    Article Title: Targeting Endoplasmic Reticulum Stress and Nitroso-Redox Imbalance in Neuroendocrine Prostate Cancer: The Therapeutic Role of Nitric Oxide
    Article Snippet: .. Notably, our previous studies have shown that S-nitrosylation, a post-translational modification that involves the covalent attachment of a nitric oxide (NO) group to cysteine residues, plays a critical role in regulating protein function and modulating cancer cell signaling . ..

    Membrane:

    Article Title: S -acylation of p62 promotes p62 droplet recruitment into autophagosomes in mammalian autophagy
    Article Snippet: .. Protein S -acylation is the covalent attachment of a long-chain fatty acid to specific cysteine residues within a protein; often, this fatty acid is palmitate or stearate., S -acylation significantly increases the hydrophobicity of proteins and contributes to their membrane association, thereby playing critical roles in protein function and cell signaling., , S -acylation is readily reversible due to the lability of the thioester bond between the fatty acyl group and cysteine residue, therefore leading to spatial-temporal control of protein function and subcellular localization., , In the present study, we report that p62 undergoes reversible S -acylation, which is mediated by the zinc-finger Asp-His-His-Cys S -acyltransferase 19 (ZDHHC19) and the acyl protein thioesterase 1 (APT1). ..

    Residue:

    Article Title: S -acylation of p62 promotes p62 droplet recruitment into autophagosomes in mammalian autophagy
    Article Snippet: .. Protein S -acylation is the covalent attachment of a long-chain fatty acid to specific cysteine residues within a protein; often, this fatty acid is palmitate or stearate., S -acylation significantly increases the hydrophobicity of proteins and contributes to their membrane association, thereby playing critical roles in protein function and cell signaling., , S -acylation is readily reversible due to the lability of the thioester bond between the fatty acyl group and cysteine residue, therefore leading to spatial-temporal control of protein function and subcellular localization., , In the present study, we report that p62 undergoes reversible S -acylation, which is mediated by the zinc-finger Asp-His-His-Cys S -acyltransferase 19 (ZDHHC19) and the acyl protein thioesterase 1 (APT1). ..

    Control:

    Article Title: S -acylation of p62 promotes p62 droplet recruitment into autophagosomes in mammalian autophagy
    Article Snippet: .. Protein S -acylation is the covalent attachment of a long-chain fatty acid to specific cysteine residues within a protein; often, this fatty acid is palmitate or stearate., S -acylation significantly increases the hydrophobicity of proteins and contributes to their membrane association, thereby playing critical roles in protein function and cell signaling., , S -acylation is readily reversible due to the lability of the thioester bond between the fatty acyl group and cysteine residue, therefore leading to spatial-temporal control of protein function and subcellular localization., , In the present study, we report that p62 undergoes reversible S -acylation, which is mediated by the zinc-finger Asp-His-His-Cys S -acyltransferase 19 (ZDHHC19) and the acyl protein thioesterase 1 (APT1). ..

    Article Title: De novo design of allosterically switchable protein assemblies
    Article Snippet: .. Allosteric modulation of protein function, wherein the binding of an effector to a protein triggers conformational changes at distant functional sites, plays a central part in the control of metabolism and cell signalling – . ..

    Protein-Protein interactions:

    Article Title: Inducible Nitric Oxide Synthase (iNOS): More Than an Inducible Enzyme? Rethinking the Classification of NOS Isoforms.
    Article Snippet: .. Cross-talk between iNOS-derived NO and other signaling pathways NO exerts its biological effects primary through two mechanisms: (1) activation of soluble guanylate cyclase (sGC), which increases cyclic guanosine monophosphate (cGMP) levels, leading to activation of protein kinase G (PKG) and downstream phosphorylation of target proteins; and (2) S-nitrosylation, a reversible post-translational modification in which NO covalently modifies cysteine thiols [85] or binds to transition metals [86], thereby modulating protein function [5]. iNOS-derived NO interacts with several major cell signaling pathways, including NF-κB [81, 87, 88], hypoxia-inducible factor-1 (HIF-1) [89, 90], adenosine monophosphate (AMP)activated protein kinase (AMPK) [91], and Janus kinase/signal transducer and activator of transcription (JAK/STAT) [92] (Figure 2). ..

    Activation Assay:

    Article Title: Inducible Nitric Oxide Synthase (iNOS): More Than an Inducible Enzyme? Rethinking the Classification of NOS Isoforms.
    Article Snippet: .. Cross-talk between iNOS-derived NO and other signaling pathways NO exerts its biological effects primary through two mechanisms: (1) activation of soluble guanylate cyclase (sGC), which increases cyclic guanosine monophosphate (cGMP) levels, leading to activation of protein kinase G (PKG) and downstream phosphorylation of target proteins; and (2) S-nitrosylation, a reversible post-translational modification in which NO covalently modifies cysteine thiols [85] or binds to transition metals [86], thereby modulating protein function [5]. iNOS-derived NO interacts with several major cell signaling pathways, including NF-κB [81, 87, 88], hypoxia-inducible factor-1 (HIF-1) [89, 90], adenosine monophosphate (AMP)activated protein kinase (AMPK) [91], and Janus kinase/signal transducer and activator of transcription (JAK/STAT) [92] (Figure 2). ..

    Phospho-proteomics:

    Article Title: Inducible Nitric Oxide Synthase (iNOS): More Than an Inducible Enzyme? Rethinking the Classification of NOS Isoforms.
    Article Snippet: .. Cross-talk between iNOS-derived NO and other signaling pathways NO exerts its biological effects primary through two mechanisms: (1) activation of soluble guanylate cyclase (sGC), which increases cyclic guanosine monophosphate (cGMP) levels, leading to activation of protein kinase G (PKG) and downstream phosphorylation of target proteins; and (2) S-nitrosylation, a reversible post-translational modification in which NO covalently modifies cysteine thiols [85] or binds to transition metals [86], thereby modulating protein function [5]. iNOS-derived NO interacts with several major cell signaling pathways, including NF-κB [81, 87, 88], hypoxia-inducible factor-1 (HIF-1) [89, 90], adenosine monophosphate (AMP)activated protein kinase (AMPK) [91], and Janus kinase/signal transducer and activator of transcription (JAK/STAT) [92] (Figure 2). ..

    Binding Assay:

    Article Title: De novo design of allosterically switchable protein assemblies
    Article Snippet: .. Allosteric modulation of protein function, wherein the binding of an effector to a protein triggers conformational changes at distant functional sites, plays a central part in the control of metabolism and cell signalling – . ..

    Functional Assay:

    Article Title: De novo design of allosterically switchable protein assemblies
    Article Snippet: .. Allosteric modulation of protein function, wherein the binding of an effector to a protein triggers conformational changes at distant functional sites, plays a central part in the control of metabolism and cell signalling – . ..



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