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ADAM22 encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Zusätzlich bieten wir Ihnen ADAM22 Kits (11) und ADAM22 Proteine (9) und viele weitere Produktgruppen zu diesem Protein an.
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Mammalian Monoclonal ADAM22 Primary Antibody für ISt, IHC - ABIN1304515
Zhou, Lee, Jin, Wright, Smith, Anderson: Arrested maturation of excitatory synapses in autosomal dominant lateral temporal lobe epilepsy. in Nature medicine 2009
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Mammalian Monoclonal ADAM22 Primary Antibody für ISt, IHC - ABIN1304516
Ogawa, Oses-Prieto, Kim, Horresh, Peles, Burlingame, Trimmer, Meijer, Rasband: ADAM22, a Kv1 channel-interacting protein, recruits membrane-associated guanylate kinases to juxtaparanodes of myelinated axons. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2010
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LGI1 and ADAM22 form an essential synaptic organizing complex that coordinates the maturation of excitatory synapses by regulating the functional incorporation of PSD-95
Interaction proteomics revealed the interactors of Caspr2, including CNTN2, KCNAs, members of the ADAM family (ADAM22, ADAM23 and ADAM11), members of LGI family and MAGUKs (DLGs and MPPs).
ADAM22 is an axonal component of the Kv1 K+ channel complex that recruits membrane-associated guanylate kinase to juxtaparanodes
ADAM22 is closely involved in the correct functioning of the nervous system.
study identified LGI1 as a specific binding partner of ADAM22 protein from mouse brain, and demonstrated the specific interaction between LGI1 and ADAM22
the LGI1-ADAM22 complex functions as the trans-synaptic machinery for precise synaptic transmission
ADAM22 is critically involved in miR-449a-reduced tamoxifen resistance of estrogen receptor-positive breast cancer cells as a direct target of miR-449a.
these results support the existence of a second mechanism, alternative to inhibition of protein secretion, by which ADLTE-causing LGI1 mutations exert their loss-of-function effect extracellularly, and suggest that interactions of LGI1 with both ADAM22 and ADAM23 play an important role in the molecular mechanisms leading to utosomal dominant lateral temporal epilepsy
Disruption of LGI1-ADAM22 interaction reduces synaptic AMPA receptors in hippocampal neurons.
Data suggest that ADAM22 plays roles in cell differentiation, cell migration, and resistance to endocrine therapy in breast cancer; ADAM22 may serve as biomarker for poor disease-free survival in breast cancer patients. [REVIEW]
findings suggest that SRC-1 switches steroid-responsive tumors to a steroid-resistant state in which the SRC-1 target gene ADAM22 has a critical role
Mutations in disintegrin domain sequence in ADAM22 gene is associted with reduced LGI4-binding abilities resulting in epilepsy.
Transgenic leucine-rich glioma-inactivated 4 (Lgi4) and transgenic Adam22 proteins are both expressed in Schwann cells as well as in sensory neurons; binding of Lgi4 to axonal Adam22 is required on axons to drive myelin formation.
role for the 14-3-3zeta/ADAM 22 association in the regulation of cell adhesion and related signaling events
demonstrated a functional role for ADAM22/14-3-3 in cell adhesion and spreading
ADAM22, a brain-specific cell surface protein, mediates growth inhibition using an integrin dependent pathway. It is expressed in normal brain but not in high-grade gliomas.
This study indicated ADAM22 gene is probably not a major gene for this epilepsy syndrome.
Differential coding potential of ADAM22 mRNAs.
our results suggest that neither ADAM22 nor any of the three Kv1 channel genes are major causative genes for ADLTE.
The pro domains of ADAMs are expressed as two subdomains. The most N-terminal subdomain (ADAM22-P(N)) was found to be susceptible to proteolysis and was required for folding stability of the second subdomain (ADAM22-P(C)).
This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. Unlike other members of the ADAM protein family, the protein encoded by this gene lacks metalloprotease activity since it has no zinc-binding motif. This gene is highly expressed in the brain and may function as an integrin ligand in the brain. In mice, it has been shown to be essential for correct myelination in the peripheral nervous system. Alternative splicing results in several transcript variants.
a disintegrin and metalloprotease domain (ADAM) 22
, disintegrin and metalloproteinase domain-containing protein 22
, a disintegrin and metalloprotease domain 22
, a disintegrin and metalloproteinase domain 22
, metalloproteinase-disintegrin ADAM22-3
, metalloproteinase-like, disintegrin-like, and cysteine-rich protein 2
, ADAM 22
, metalloprotease-disintegrin MDC11b
, metalloprotease/disintegrin xMDC11.2