| scholarly article | Q13442814 |
| P819 | ADS bibcode | 1991PNAS...88.1918S |
| P356 | DOI | 10.1073/PNAS.88.5.1918 |
| P932 | PMC publication ID | 51137 |
| P698 | PubMed publication ID | 2000396 |
| P5875 | ResearchGate publication ID | 21156407 |
| P50 | author | Jack L. Strominger | Q1398103 |
| P2093 | author name string | R L Dunbrack | |
| J Shin | |||
| S Lee | |||
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| The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus type 2 consists of three separate amino acid segments at the carboxy terminus | Q41716713 | ||
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| The isolation and nucleotide sequence of a cDNA encoding the T cell surface protein T4: a new member of the immunoglobulin gene family | Q48376775 | ||
| Identification by anti-idiotype antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal | Q56766292 | ||
| Structural nature of the interaction between T lymphocyte surface molecule CD4 and the intracellular protein tyrosine kinase lck | Q67275646 | ||
| Failure to synthesize the T cell CD3-zeta chain: structure and function of a partial T cell receptor complex | Q68128126 | ||
| Assembly of the human T cell receptor-CD3 complex takes place in the endoplasmic reticulum and involves intermediary complexes between the CD3-gamma.delta.epsilon core and single T cell receptor alpha or beta chains | Q70046916 | ||
| P433 | issue | 5 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | endoplasmic reticulum | Q79927 |
| transmembrane protein | Q424204 | ||
| P1104 | number of pages | 5 | |
| P304 | page(s) | 1918-1922 | |
| P577 | publication date | 1991-03-01 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Signals for retention of transmembrane proteins in the endoplasmic reticulum studied with CD4 truncation mutants | |
| P478 | volume | 88 |
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| Q45016131 | Coexpression of the membrane glycoproteins G1 and G2 of Hantaan virus is required for targeting to the Golgi complex |
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