Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain (Q64008501)

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English	Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain	scholarly article

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instance of

scholarly article

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title

Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain (English)

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main subject

erythropoietin

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based on heuristic

inferred from title

author

Harvey Lodish

series ordinal

6

object named as

H F Lodish

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author name string

S N Constantinescu

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1

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T Keren

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2

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M Socolovsky

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3

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H Nam

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4

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Y I Henis

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5

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language of work or name

English

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publication date

10 April 2001

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published in

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

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volume

98

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issue

8

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page(s)

4379-84

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cites work

Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Substitution of the insulin receptor transmembrane domain with that of glycophorin A inhibits insulin action.

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

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inferred from PubMed ID database lookup

The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely oriented, hydrophobic motif

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

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inferred from PubMed ID database lookup

Erythropoietin receptor. Subunit structure and activation

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Point mutation in the exoplasmic domain of the erythropoietin receptor resulting in hormone-independent activation and tumorigenicity

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Sequence specificity in the dimerization of transmembrane alpha-helices

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

based on heuristic

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Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The types II and III transforming growth factor-beta receptors form homo-oligomers

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

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inferred from PubMed ID database lookup

Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

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inferred from PubMed ID database lookup

Small peptides as potent mimetics of the protein hormone erythropoietin

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

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Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 A

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

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Activation of the erythropoietin (EPO) receptor by bivalent anti-EPO receptor antibodies

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Cytokine receptor signal transduction and the control of hematopoietic cell development

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

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12 December 2020

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inferred from PubMed ID database lookup

Homodimerization of erythropoietin receptor by a bivalent monoclonal antibody triggers cell proliferation and differentiation of erythroid precursors.

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A transmembrane helix dimer: structure and implications

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The prolactin receptor and severely truncated erythropoietin receptors support differentiation of erythroid progenitors

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Oligomeric Structure of Type I and Type II Transforming Growth Factor β Receptors: Homodimers Form in the ER and Persist at the Plasma Membrane

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Efficiency of signalling through cytokine receptors depends critically on receptor orientation

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Erythropoietin receptor activation by a ligand-induced conformation change

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Transforming growth factor-beta induces formation of a dithiothreitol-resistant type I/Type II receptor complex in live cells.

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Activation of the erythropoietin receptor by the gp55-P viral envelope protein is determined by a single amino acid in its transmembrane domain

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Generation of mammalian cells stably expressing multiple genes at predetermined levels.

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/11296286

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.081069198

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ADS bibcode

2001PNAS...98.4379C

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PMC publication ID

31843

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PubMed publication ID

11296286

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