Definitions
from Wiktionary, Creative Commons Attribution/Share-Alike License.
- adjective biology
Adjacent to amembrane on one side of it.
Etymologies
from Wiktionary, Creative Commons Attribution/Share-Alike License
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Examples
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SP, signal peptide; LRR, leucine rich repeats; TM, transmembrane domain; JM, juxtamembrane domain; Myc-XA21CP; cleavage product of Myc-XA21.
PLoS ONE Alerts: New Articles Chang-Jin Park et al. 2010
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Extended kinase domain was taken as it has been reported that for kinase activity and stabilization, additional residues of juxtamembrane region are required.
PLoS ONE Alerts: New Articles Gunjan Arora et al. 2010
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Liu GZ, Chen X, Tinjuangjun P, et al. (2006) The autophosphorylated Ser686, Thr688, and Ser689 residues in the intracellular juxtamembrane domain of XA21 are implicated in stability control of rice receptor-like kinase.
PLoS ONE Alerts: New Articles Chang-Jin Park et al. 2010
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Liu GZ, Chen X, Tinjuangjun P, et al. (2006) The autophosphorylated Ser686, Thr688, and Ser689 residues in the intracellular juxtamembrane domain of XA21 are implicated in stability control of rice receptor-like kinase.
PLoS ONE Alerts: New Articles Chang-Jin Park et al. 2010
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Williams O, Palomero T, Tosello V, Pallikuppam S, et al. (2008) Notch1 extracellular juxtamembrane expansion mutations in T-ALL.
PLoS ONE Alerts: New Articles Miguel Aste-Amézaga et al. 2010
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SP, signal peptide; LRR, leucine rich repeats; TM, transmembrane domain; JM, juxtamembrane domain; Myc-XA21CP; cleavage product of Myc-XA21.
PLoS ONE Alerts: New Articles Chang-Jin Park et al. 2010
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Exactly how receptor auto-phosphorylation alters receptor affinity is not yet known, although both linkage and cooperativity require the presence of the intracellular juxtamembrane domain as deletion of this region eliminates both binding phenomena.
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Exactly how receptor auto-phosphorylation alters receptor affinity is not yet known, although both linkage and cooperativity require the presence of the intracellular juxtamembrane domain as deletion of this region eliminates both binding phenomena.
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The juxtamembrane domain has previously been shown to be required for activation of the EGF receptor tyrosine kinase, and now its duties have expanded to include allosteric Comparison of binding isotherms of wild-type and K721A kinase-dead EGF receptors reveals opposite shifts in direction as receptor number increases; the right to left shift in K721A suggests positive linkage.
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The juxtamembrane domain has previously been shown to be required for activation of the EGF receptor tyrosine kinase, and now its duties have expanded to include allosteric Comparison of binding isotherms of wild-type and K721A kinase-dead EGF receptors reveals opposite shifts in direction as receptor number increases; the right to left shift in K721A suggests positive linkage.
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