Jove
Visualize
Contáctanos
JoVE
x logofacebook logolinkedin logoyoutube logo
ACERCA DE JoVE
Visión GeneralLiderazgoBlogCentro de Ayuda JoVE
AUTORES
Proceso de PublicaciónConsejo EditorialAlcance y PolíticasRevisión por ParesPreguntas FrecuentesEnviar
BIBLIOTECARIOS
TestimoniosSuscripcionesAccesoRecursosConsejo Asesor de BibliotecasPreguntas Frecuentes
INVESTIGACIÓN
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchivo
EDUCACIÓN
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualCentro de Recursos para ProfesoresSitio de Profesores
Términos y Condiciones de Uso
Política de Privacidad
Políticas

Videos de Conceptos Relacionados

Phosphorylation01:02

Phosphorylation

44.6K
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.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
44.6K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

12.1K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
12.1K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.2K
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....
8.2K
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

15.4K
Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
15.4K

También podría leer

Artículos Relacionados

Artículos vinculados a este trabajo por autores compartidos, revista y gráfico de citas.

Ordenar por
Same author

Reflection on "Site-specific PEGylation of proteins by a Staudinger-phosphite reaction": from protein modification to ADCs in the clinic.

Chemical science·2026
Same author

Upcoming Treatments in Celiac Disease: From Luminal Enzymes to Oral Immune Tolerance.

United European gastroenterology journal·2026
Same author

A cell-permeable nanobody to restore F508del cystic fibrosis transmembrane conductance regulator activity.

Nature chemical biology·2026
Same author

Polyfluoroalkyl-Tagged Cell-Penetrating Peptide-Additives Enhance Intracellular Protein Delivery via Sustained Monomeric Lipid Interaction.

Angewandte Chemie (International ed. in English)·2026
Same author

European Society for the Study of Coeliac Disease (ESsCD) 2025 Updated Guidelines on the Diagnosis and Management of Coeliac Disease in Adults. Part 2: Management, Follow-Up, and Complex Disease Courses.

United European gastroenterology journal·2026
Same author

Modular Vinyl Phosphonamidates for Cysteine-Directed Protein Targeting.

Journal of the American Chemical Society·2026

Video Experimental Relacionado

Updated: Apr 24, 2026

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
08:48

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Published on: November 29, 2014

13.4K

Los péptidos de lisina fosforilados específicamente para el sitio.

Jordi Bertran-Vicente1, Remigiusz A Serwa, Michael Schümann

  • 1Leibniz-Institut für Molekulare Pharmakologie (FMP) , Robert-Rössle Str. 10, 13125 Berlin, Germany.

Journal of the American Chemical Society
|September 9, 2014
PubMed
Resumen

Los investigadores desarrollaron un nuevo método para sintetizar péptidos de fosfolisina, lo que permite el estudio de la fosforilación de la lisina. Este avance facilita la detección y la evaluación de la relevancia biológica de esta modificación crucial después de la traducción.

Más Videos Relacionados

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

7.8K
Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

8.1K

Videos de Experimentos Relacionados

Last Updated: Apr 24, 2026

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
08:48

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Published on: November 29, 2014

13.4K
Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

7.8K
Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

8.1K

Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Biología Molecular Biología Molecular
  • La proteómica es la proteómica.

Sus antecedentes:

  • La fosforilación de proteínas es vital para los procesos celulares, y el papel de la fosforilación de lisina es en gran parte inexplorado.
  • Los métodos existentes están limitados por la inestabilidad de la fosfolisina durante la síntesis de péptidos.

Objetivo del estudio:

  • Desarrollar una nueva ruta sintética para péptidos específicos del sitio que contienen fosfolisina (pLys).
  • Para permitir el estudio de la importancia biológica de la fosforilación de lisina.

Principales métodos:

  • Utilizó la reacción Staudinger-fosfito para la síntesis quimioselectiva.
  • Empleado la síntesis de péptidos en fase sólida (SPPS) con péptidos de azido lisina.
  • Los fosforamidatos convertidos en pLys a través de la irradiación UV o la desprotección básica.

Principales resultados:

  • Se han sintetizado con éxito péptidos específicos del sitio que contienen pLys.
  • Espectrometría de masas en tándem de disociación por transferencia de electrones demostrada para la asignación de pLys en péptidos histónicos.
  • Mostró la detección de estos péptidos en lisatos celulares utilizando proteómica de abajo hacia arriba.

Conclusiones:

  • El nuevo método sintético supera las limitaciones anteriores en el estudio de la fosforilación de la lisina.
  • Este enfoque es crucial para investigar la relevancia biológica de la fosforilación de la lisina.
  • Se espera que la técnica desarrollada sea una herramienta esencial en el campo.