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Related Concept Videos

Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

Factors Affecting Protein-Drug Binding: Protein-Related Factors

Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be bound by...
Factors Affecting Protein-Drug Binding: Drug-Related Factors01:18

Factors Affecting Protein-Drug Binding: Drug-Related Factors

Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In contrast,...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Drug Distribution: Plasma Protein Binding01:29

Drug Distribution: Plasma Protein Binding

Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

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Updated: May 14, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Poly(A) binding proteins: are they all created equal?

Dixie J Goss1, Frida Esther Kleiman

  • 1Chemistry Department, Hunter College CUNY, New York, NY, USA. dgoss@hunter.cuny.edu

Wiley Interdisciplinary Reviews. RNA
|February 21, 2013
PubMed
Summary
This summary is machine-generated.

Poly(A)-binding proteins (PABPs) are crucial for mRNA metabolism, acting beyond just shielding the poly(A) tail. Their complex interactions regulate diverse mRNA pathways, including translation and degradation, impacting development and viral infections.

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Area of Science:

  • Molecular Biology
  • RNA Biology
  • Gene Regulation

Background:

  • Poly(A)-binding proteins (PABPs) were initially considered simple mRNA poly(A) tail protectors.
  • Recent research reveals PABPs interact with both the poly(A) tail and specific mRNA sequences.
  • PABP functions are intricate, involving interactions with numerous cellular factors.

Purpose of the Study:

  • To review and update current knowledge on PABP roles in mRNA metabolism.
  • To highlight emerging data on specific interactions of PABP homologs.
  • To explore the complex regulatory network of PABP functions.

Main Methods:

  • Literature review of PABP research.
  • Analysis of PABP interactions with mRNA and cellular factors.
  • Synthesis of data on PABP involvement in various mRNA pathways.

Main Results:

  • PABPs play both general and specific roles in mRNA metabolism.
  • PABPs are involved in polyadenylation/deadenylation, export, surveillance, translation, degradation, and microRNA regulation.
  • Individual PABPC family members have specific roles in development and viral infections.

Conclusions:

  • PABP functions are complex, extending to multiple mRNA metabolic pathways.
  • Emerging evidence points to nuclear-cytoplasmic shuttling and post-translational modifications fine-tuning PABP activity.
  • PABPs are central regulators of gene expression with significant implications in cellular processes and disease.