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Related Concept Videos

Protein Networks02:26

Protein Networks

4.4K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Protein Networks02:26

Protein Networks

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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Updated: Dec 21, 2025

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
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Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

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RESTful API for iPTMnet: a resource for protein post-translational modification network discovery.

Sachin Gavali1, Julie Cowart1, Chuming Chen1,2

  • 1Center for Bioinformatics and Computational Biology, 205 Delaware Biotechnology Institute, 15 Innovation Way, Newark, DE 19711, USA.

Database : the Journal of Biological Databases and Curation
|May 13, 2020
PubMed
Summary

iPTMnet now offers a RESTful API for seamless integration of protein post-translational modification (PTM) data into bioinformatics workflows. This enables automated data access and enhances scientific discovery, connecting PTM sites to signaling pathways.

Keywords:
CloudDockerPhosphoproteomicsPost-Translational ModificationRESTful APIRustWeb ServiceiPTMnet

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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Molecular Biology

Background:

  • iPTMnet is a valuable resource for protein post-translational modification (PTM) data.
  • Current iPTMnet website lacks automated data integration capabilities.
  • Need for streamlined access to PTM data in research pipelines.

Purpose of the Study:

  • Develop a RESTful API for iPTMnet to enable automated data integration.
  • Facilitate the incorporation of iPTMnet data into existing bioinformatics tools and pipelines.
  • Enhance scientific discovery through easier access to PTM information.

Main Methods:

  • Developed a RESTful API using cloud technologies.
  • Packaged the iPTMnet API software in Docker containers for redistribution on DockerHub.
  • Created Python and R packages for user-friendly integration.

Main Results:

  • Successfully implemented a RESTful API for iPTMnet.
  • API is readily available via Docker containers and language-specific packages.
  • Demonstrated a use case connecting PTM sites to kinase signaling pathways.

Conclusions:

  • The new iPTMnet API significantly improves data accessibility and integration.
  • Facilitates automated PTM data retrieval for bioinformatics research.
  • Empowers researchers to conduct more advanced scientific discovery and analysis.