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TMPRSS2 encodes a protein that belongs to the serine protease family. Zusätzlich bieten wir Ihnen TMPRSS2 Antikörper (72) und TMPRSS2 Kits (26) und viele weitere Produktgruppen zu diesem Protein an.
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Our findings indicate that TGF-beta (zeige TGFB1 Proteine) signaling is a major determinant of EMT (zeige ITK Proteine) in T/E overexpressing LNCaP cells.
A potential novel function of TMPRSS2-ERG (zeige ERG Proteine) as a major regulator of IGF1R (zeige IGF1R Proteine) gene expression.
Study shows that T2E fusion transcripts are associated with higher levels of AMACR (zeige AMACR Proteine) mRNA in patients with atypical small acinar proliferation (ASAP (zeige MAP9 Proteine)) which represents an indicator of risk for prostate cancer in patients with ASAP (zeige MAP9 Proteine).
TMPRSS2-ERG (zeige ERG Proteine) may have a role in progression of prostate neoplasms and in alteration of the metabolic profile
Meta-analysis showed the prevalence of TMPRSS2:ERG (zeige ERG Proteine) fusions in prostate cancer to be highest in men of European descent (49%), followed by Asians (27%) and then African (25%) descent.
Data show that tumors displaying TMPRSS2-ERG (zeige ERG Proteine) fusions that retained interstitial genes were less likely to be associated with biochemical recurrence
We demonstrate a role for inflammation-induced oxidative stress in the formation of DNA breaks leading to recurrent TMPRSS2-ERG (zeige ERG Proteine) gene fusions. The transcriptional status and epigenetic features of the target genes influence this effect.
NOTCH (zeige NOTCH1 Proteine) pathway inhibition antagonizes the growth and invasion of transmembrane protease serine 2 (TMPRSS2)-transforming protein ERG (ERG) (T2E) -positive prostate cancer cells.
The TMPRSS2-ERG (zeige ERG Proteine) gene fusion is the most frequently observed genetic aberration in prostate cancer.
Study provide evidence that PTEN deletion and TMPRSS2-ERG (zeige ERG Proteine) gene fusion were mutually exclusive in patients with prostate neoplasm. TMPRSS2-ERG (zeige ERG Proteine) gene fusion was rare compared to peripheral zone tumors and to PTEN inactivation in T1a (zeige PDPN Proteine) transition zone tumors.
Study shows that Influenza A (IAV) possessing a monobasic cleavage site in the haemagglutinin (HA) replicates poorly in TMPRSS2 knockout mice due to insufficient HA cleavage. On the contrary, IBV successfully underwent HA cleavage in TMPRSS2 knockout mice, and that the mouse-adapted strain was fully pathogenic. These data demonstrate a clear difference between IAV and IBV in their molecular mechanisms for spreading.
DPP4 (zeige DPP4 Proteine):CD9 (zeige CD9 Proteine):TTSP (zeige TMPRSS11E Proteine) as the protein complexes are necessary for early efficient MERS-coronavirus entry.
Genetic inhibition of TMPRSS2-ERG (zeige ERG Proteine) junction oncogene (zeige RAB1A Proteine) in prostate cancer by means of siRNA has strong antineoplastic effect in a mouse model and in vitro.
The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis
TMPRSS2 as a host cell factor essential for viral spread and pathogenesis of mono-basic H1N1 and H3N2 influenza A viruses.
These results demonstrate that TMPRSS2 expression is essential for influenza A virus replication in vivo.
These data demonstrate that TMPRSS2 is a host factor that is essential for pneumotropism and pathogenicity of H7N9 and H1N1 influenza virus in mice.
Loss of TMPRSS2 serine protease (zeige F2 Proteine) activity does not influence fertility, reduce survival, result in prostate hyperplasia or carcinoma, or alter prostatic luminal epithelial cell regrowth following castration and androgen replacement.
This gene encodes a protein that belongs to the serine protease family. The encoded protein contains a type II transmembrane domain, a receptor class A domain, a scavenger receptor cysteine-rich domain and a protease domain. Serine proteases are known to be involved in many physiological and pathological processes. This gene was demonstrated to be up-regulated by androgenic hormones in prostate cancer cells and down-regulated in androgen-independent prostate cancer tissue. The protease domain of this protein is thought to be cleaved and secreted into cell media after autocleavage. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, serine protease 10
, transmembrane protease serine 2
, plasmic transmembrane protein X