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Related Concept Videos

Phosphoinositides and PIPs01:42

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Phosphodiester Linkages01:01

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Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
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Biosynthesis of Polysaccharides01:26

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Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
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Phosphorylation01:02

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
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Related Experiment Video

Updated: Apr 28, 2026

Absolute Quantitation of Inositol Pyrophosphates by Capillary Electrophoresis Electrospray Ionization Mass Spectrometry
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Elucidating diphosphoinositol polyphosphate function with nonhydrolyzable analogues.

Mingxuan Wu1, Lucy S Chong, Samanta Capolicchio

  • 1Department of Chemistry, Princeton University, Washington Rd, Princeton, NJ 08544 (USA).

Angewandte Chemie (International Ed. in English)
|June 4, 2014
PubMed
Summary
This summary is machine-generated.

New diphosphoinositol polyphosphate (PP-IP) analogues resist degradation, aiding research into cellular signaling. These tools help distinguish PP-IP mechanisms and characterize their roles in biological processes.

Keywords:
diphosphoinositol polyphosphatemechanistic probenonhydrolyzable analoguesphosphorylationsecond messengers

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Preparation of Quality Inositol Pyrophosphates
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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Last Updated: Apr 28, 2026

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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

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Area of Science:

  • Biochemistry
  • Cellular Biology
  • Molecular Signaling

Background:

  • Diphosphoinositol polyphosphates (PP-IPs) are high-energy phosphate messengers regulating diverse cellular functions.
  • PP-IPs are believed to act as allosteric regulators and participate in protein pyrophosphorylation.
  • Understanding PP-IP signaling is limited by the lack of appropriate research tools.

Purpose of the Study:

  • To synthesize novel, stable analogues of PP-IPs for studying their cellular roles.
  • To develop tools that differentiate between PP-IP allosteric regulation and pyrophosphorylation mechanisms.
  • To facilitate structural and biochemical characterization of PP-IP signaling pathways.

Main Methods:

  • Synthesis of PP-IP bisphosphonate analogues (PCP-IPs) designed for chemical and biochemical stability.
  • Assessment of the inhibitory potencies of PCP-IP regioisomers on Akt phosphorylation.
  • Evaluation of the inhibitory effects of PCP-IPs on the phosphatase hDIPP1.
  • Analysis of the ability of PCP analogues to inhibit protein pyrophosphorylation.

Main Results:

  • The synthesized PCP-IP analogues demonstrated resistance to degradation.
  • Both 1PCP-IP5 and 5PCP-IP5 showed similar potency in inhibiting Akt phosphorylation.
  • 1PCP-IP5 was significantly more potent in inhibiting the hDIPP1 phosphatase.
  • PCP analogues were unable to transfer the β-phosphoryl group, thus inhibiting protein pyrophosphorylation.

Conclusions:

  • PCP analogues are valuable tools for dissecting PP-IP signaling mechanisms.
  • These stable analogues enable the distinction between allosteric regulation and pyrophosphorylation by PP-IPs.
  • The developed analogues will advance the structural and biochemical characterization of PP-IP-mediated cellular processes.