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

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

COVID-19 Vaccine Reactogenicity Marks an Innate Inflammatory Response Associated With HLA Variation and Enhanced Protection.

Research square·2026
Same author

γδ T cell-derived IL-4 initiates CD8<sup>+</sup> T cell immunity.

Nature immunology·2026
Same author

Preclinical development of a cross-protective β-SARS-CoV-2 virus-like particle vaccine adjuvanted with MF59.

NPJ vaccines·2026
Same author

An HLA Association With COVID-19 Vaccine Reactogenicity Correlates With Fewer SARS-CoV-2 Infections and Monocyte Activation.

Research square·2026
Same author

Method for Producing Recombinant Soluble T-Cell Receptors.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Method for Determining the Affinity of the T Cell Receptor for the Peptide-Human Leukocyte Antigen Complex.

Methods in molecular biology (Clifton, N.J.)·2026

Video Experimental Relacionado

Updated: Jan 7, 2026

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens
09:53

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

Published on: February 6, 2017

11.8K

Método para realizar la co-complejación y el análisis estructural del receptor-péptido-antígeno leucocitario humano

Demetra S M Chatzileontiadou1,2,3, Stephanie Gras4,5,6

  • 1Infection and Immunity Program, La Trobe Institute for Molecular Science (LIMS), La Trobe University, Bundoora, VIC, Australia.

Methods in molecular biology (Clifton, N.J.)
|January 1, 2026
PubMed
Resumen

No abstract available in PubMed .

Palabras clave:
Estructura de cristalEl antígeno leucocitario humanoEl péptidoPurificaciónReceptor de las células TLas radiografías.

Más Videos Relacionados

Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay
19:05

Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay

Published on: October 30, 2015

12.8K
Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation
12:09

Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation

Published on: February 28, 2019

10.2K

Videos de Experimentos Relacionados

Last Updated: Jan 7, 2026

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens
09:53

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

Published on: February 6, 2017

11.8K
Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay
19:05

Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay

Published on: October 30, 2015

12.8K
Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation
12:09

Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation

Published on: February 28, 2019

10.2K