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(1985) Correction: High-Affinity-Receptor-Mediated Uptake and Degradation of Glucose-Modified Proteins: A Potential Mechanism for the Removal of Senescent Macro-Molecules. Proceedings of the National Academy of Sciences, 82 (23) 8274 doi:10.1073/pnas.82.23.8274-b

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Reference TypeJournal (article/letter/editorial)
TitleCorrection: High-Affinity-Receptor-Mediated Uptake and Degradation of Glucose-Modified Proteins: A Potential Mechanism for the Removal of Senescent Macro-Molecules
JournalProceedings of the National Academy of Sciences
Year1985 (December 1)Volume82
Issue23
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.82.23.8274-bSearch in ResearchGate
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Mindat Ref. ID1446175Long-form Identifiermindat:1:5:1446175:2
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Full Reference(1985) Correction: High-Affinity-Receptor-Mediated Uptake and Degradation of Glucose-Modified Proteins: A Potential Mechanism for the Removal of Senescent Macro-Molecules. Proceedings of the National Academy of Sciences, 82 (23) 8274 doi:10.1073/pnas.82.23.8274-b
Plain Text(1985) Correction: High-Affinity-Receptor-Mediated Uptake and Degradation of Glucose-Modified Proteins: A Potential Mechanism for the Removal of Senescent Macro-Molecules. Proceedings of the National Academy of Sciences, 82 (23) 8274 doi:10.1073/pnas.82.23.8274-b
In(1985, December) Proceedings of the National Academy of Sciences Vol. 82 (23) Proceedings of the National Academy of Sciences

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Vlassara, H., Brownlee, M., Cerami, A. (1985) High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules. Proceedings of the National Academy of Sciences, 82 (17) 5588-5592 doi:10.1073/pnas.82.17.5588
(1985) Correction: Induction of Omithine Decarboxylase Activity by Insulin and Growth Factors is Mediated by Amino Acids. Proceedings of the National Academy of Sciences, 82 (23) 8274 doi:10.1073/pnas.82.23.8274
(1985) Correction: DNA Polymorphic loci Mapped to Human Chromosomes 3, 5, 9, 11, 17, 18, and 22. Proceedings of the National Academy of Sciences, 82 (23) 8274 doi:10.1073/pnas.82.23.8274-a
(1985) Correction: Accurate Transcription of Cloned Neurospora RNA Polymerase II-Dependent Genes in vitro by Homologous Soluble Extracts. Proceedings of the National Academy of Sciences, 82 (23) 8274 doi:10.1073/pnas.82.23.8274-c
Inman, W. H., Colowick, S. P. (1985) Stimulation of glucose uptake by transforming growth factor beta: evidence for the requirement of epidermal growth factor-receptor activation. Proceedings of the National Academy of Sciences, 82 (5) 1346-1349 doi:10.1073/pnas.82.5.1346
(1985) Correction: Exon-Shuffling. Proceedings of the National Academy of Sciences, 82 (15) 5236 doi:10.1073/pnas.82.15.5236-b
Kay, M. M. (1985) Glucose transport protein is structurally and immunologically related to band 3 and senescent cell antigen. Proceedings of the National Academy of Sciences, 82 (6) 1731-1735 doi:10.1073/pnas.82.6.1731
(2009) Correction for Stewart-Jones et al., Rational development of high-affinity T-cell receptor-like antibodies. Proceedings of the National Academy of Sciences, 106 (26) 10872 doi:10.1073/pnas.0905399106
Mason, J. C., Tager, H. S. (1985) Identification of distinct receptor complexes that account for high-and low-affinity glucagon binding to hepatic plasma membranes. Proceedings of the National Academy of Sciences, 82 (20) 6835-6839 doi:10.1073/pnas.82.20.6835
Pribluda, V. S., Pribluda, C., Metzger, H. (1994) Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation. Proceedings of the National Academy of Sciences, 91 (23) 11246-11250 doi:10.1073/pnas.91.23.11246
Cresswell, P. (1985) Intracellular class II HLA antigens are accessible to transferrin-neuraminidase conjugates internalized by receptor-mediated endocytosis. Proceedings of the National Academy of Sciences, 82 (23) 8188-8192 doi:10.1073/pnas.82.23.8188
 
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