Purification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor (Q36263355)

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English	Purification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor	scientific article

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scholarly article

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Europe PubMed Central

PMC publication ID

345319

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13 August 2017

title

Purification and NH2-terminal amino acid sequencing of the beta subunit of a human T-cell antigen receptor (English)

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Europe PubMed Central

PMC publication ID

345319

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13 August 2017

author

Marina Fabbi

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M Fabbi

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2

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O Acuto

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1

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Europe PubMed Central

PMC publication ID

345319

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13 August 2017

J Smart

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3

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Europe PubMed Central

PMC publication ID

345319

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13 August 2017

C B Poole

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4

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Europe PubMed Central

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345319

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13 August 2017

J Protentis

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5

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Europe PubMed Central

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345319

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13 August 2017

H D Royer

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6

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Europe PubMed Central

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345319

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13 August 2017

S F Schlossman

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7

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345319

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13 August 2017

E L Reinherz

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8

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345319

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13 August 2017

language of work or name

English

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publication date

1 June 1984

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Europe PubMed Central

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345319

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13 August 2017

number of pages

5

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Proceedings of the National Academy of Sciences of the United States of America

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345319

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13 August 2017

volume

81

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Europe PubMed Central

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345319

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13 August 2017

issue

12

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Europe PubMed Central

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345319

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13 August 2017

page(s)

3851-3855

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345319

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13 August 2017

cites work

THE PREPARATION OF I-131-LABELLED HUMAN GROWTH HORMONE OF HIGH SPECIFIC RADIOACTIVITY

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Comparison of T3-associated 49- and 43-kilodalton cell surface molecules on individual human T-cell clones: evidence for peptide variability in T-cell receptor structures

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The major histocompatibility complex-restricted antigen receptor on T cells. I. Isolation with a monoclonal antibody

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Primary structure of a human IgA1 immunoglobulin. V. Amino acid sequence of a human IgA lambda light chain (Bur)

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Peptide variability exists within alpha and beta subunits of the T cell receptor for antigen

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Clonotypic structures involved in antigen-specific human T cell function. Relationship to the T3 molecular complex

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The mouse T cell receptor: structural heterogeneity of molecules of normal T cells defined by xenoantiserum

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A one-step purification of membrane proteins using a high efficiency immunomatrix

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Evidence for the T3-associated 90K heterodimer as the T-cell antigen receptor

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The major histocompatibility complex-restricted antigen receptor on T cells in mouse and man: Identification of constant and variable peptides

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Isolation of cDNA clones encoding T cell-specific membrane-associated proteins

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PubMed

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Pressure homogenization of mammalian tissues

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Isolation and characterization of lymphocyte plasma membranes

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/6427776

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.81.12.3851

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stated in

Europe PubMed Central

PMC publication ID

345319

retrieved

13 August 2017

ADS bibcode

1984PNAS...81.3851A

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PMC publication ID

345319

1 reference

stated in

Europe PubMed Central

PMC publication ID

345319

retrieved

13 August 2017

PubMed publication ID

6427776

1 reference

stated in

Europe PubMed Central

PMC publication ID

345319

retrieved

13 August 2017

ResearchGate publication ID

16768081

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