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Updated: Jan 7, 2026

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

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

T細胞受容体-ペプチド-ヒト白血球抗原共複合および構造分析を行う方法

Demetra S M Chatzileontiadou^1,2,3, Stephanie Gras^4,5,6

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

まとめ

No abstract available in PubMed .

キーワード:

クリスタル構造人間の白血球抗原ペプチド浄化する T細胞受容体 X線写真

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

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

Published on: October 30, 2015

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

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

Published on: February 28, 2019

関連する実験動画

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

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

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

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

Published on: October 30, 2015

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

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

Published on: February 28, 2019