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Statements

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rdfs:seeAlso: n7:10.1186%2F1471-2407-12-179 n8:22591401 n10:0 n11:0
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bibo:doi: 10.1186%2F1471-2407-12-179
n4:contains: _:vb15978327 _:vb15978301 _:vb15978291

Subject Item: _:vb15978291
rdf:type: n4:Section
dc:title: methods
n4:contains: _:vb15978296 _:vb15978297 _:vb15978298 _:vb15978299 _:vb15978300 _:vb15978292 _:vb15978293 _:vb15978294 _:vb15978295

Subject Item: _:vb15978292
rdf:type: n2:Context
rdf:value: The immortalized human cholangiocyte MMNK-1 cell line [>>21<<,22] was provided by the Department of Surgery of Okayama University School of Medicine.
n2:mentions: n3:14966424

Subject Item: _:vb15978293
rdf:type: n2:Context
rdf:value: The immortalized human cholangiocyte MMNK-1 cell line [21,>>22<<] was provided by the Department of Surgery of Okayama University School of Medicine.
n2:mentions: n3:21571834

Subject Item: _:vb15978294
rdf:type: n2:Context
rdf:value: For long term incubation, EGF was renewed every 15 min [>>23<<]. For recycling inhibition, monensin (Sigma Aldrich) treatment was performed as described previously [24].
n2:mentions: n3:12063263

Subject Item: _:vb15978295
rdf:type: n2:Context
rdf:value: For recycling inhibition, monensin (Sigma Aldrich) treatment was performed as described previously [>>24<<].
n2:mentions: n3:19948031

Subject Item: _:vb15978296
rdf:type: n2:Context
rdf:value: Anti-ubiquitin blotting was done as described previously [>>25<<]. Membranes were submerged in distilled water and autoclaved for 30 min at 121°C before immunoblotting.
n2:mentions: n3:10617627

Subject Item: _:vb15978297
rdf:type: n2:Context
rdf:value: Bourdoncle, Institute Jacques Monod, Service Imagerie, Paris, France) as described previously [>>26<<].
n2:mentions: n3:19289794

Subject Item: _:vb15978298
rdf:type: n2:Context
rdf:value: Live cell immunostaining and flow cytometry were performed as described elsewhere [>>25<<]. All samples were examined by immunostaining in duplicate using anti-EGFR antibody (528) and Mouse IgG2 negative control antibody (Dako, Carpinteria, CA).
n2:mentions: n3:10617627

Subject Item: _:vb15978299
rdf:type: n2:Context
rdf:value: Primers used for human EGFR and β-actin are described elsewhere [>>27<<] and are listed in Table 1.
n2:mentions: n3:18006781

Subject Item: _:vb15978300
rdf:type: n2:Context
rdf:value: Rab11a was depleted with siRNA oligonucleotides as described previously [>>28<<]. siRNA was transfected into RBE cells using Lipofectamine 2000 (Life technologies, Gaithersburg, MD).
n2:mentions: n3:15601896

Subject Item: _:vb15978301
rdf:type: n4:Section
dc:title: discussion
n4:contains: _:vb15978302 _:vb15978303 _:vb15978320 _:vb15978321 _:vb15978322 _:vb15978323 _:vb15978324 _:vb15978325 _:vb15978326 _:vb15978304 _:vb15978305 _:vb15978306 _:vb15978307 _:vb15978308 _:vb15978309 _:vb15978310 _:vb15978311 _:vb15978312 _:vb15978313 _:vb15978314 _:vb15978315 _:vb15978316 _:vb15978317 _:vb15978318 _:vb15978319

Subject Item: _:vb15978302
rdf:type: n2:Context
rdf:value: Since the EGF-EGFR complexes do not dissociate in the early endosome, EGFR remains phosphorylated and associated with Cbl [>>29<<]. Cbl mediates the interaction between EGFR and endosomal sorting complex required for transport (ESCRT) machinery and promotes EGFR sorting in multi-vesicular bodies (MVB) [30]. An early dissociation of the EGF-EGFR complex because of
n2:mentions: n3:11493652

Subject Item: _:vb15978303
rdf:type: n2:Context
rdf:value: Cbl mediates the interaction between EGFR and endosomal sorting complex required for transport (ESCRT) machinery and promotes EGFR sorting in multi-vesicular bodies (MVB) [>>30<<]. An early dissociation of the EGF-EGFR complex because of abnormally low pH in endosomes or an unstable association between EGF and EGFR-HER2 heterodimers enhances the recycling of unoccupied EGFR [10]. In our study, EGFR was retained in
n2:mentions: n3:18793634

Subject Item: _:vb15978304
rdf:type: n2:Context
rdf:value: An early dissociation of the EGF-EGFR complex because of abnormally low pH in endosomes or an unstable association between EGF and EGFR-HER2 heterodimers enhances the recycling of unoccupied EGFR [>>10<<]. In our study, EGFR was retained in early endosomes and kept phosphorylated at Tyr1068 in RBE cells. Thus, early dissociation of the EGF-EGFR complex was not considered to be the mechanism of impaired degradation and enhanced recycling
n2:mentions: n3:11597398

Subject Item: _:vb15978305
rdf:type: n2:Context
rdf:value: Cbl-mediated ubiquitination is critical for EGFR early endosome exit, lysosome sorting, and degradation [>>18<<,19]. Since low levels of EGFR ubiquitination and poor Cbl association were observed in RBE cells, we considered these factors to be attributed to the dramatically diminished EGFR degradation in RBE cells.
n2:mentions: n3:15210722

Subject Item: _:vb15978306
rdf:type: n2:Context
rdf:value: Cbl-mediated ubiquitination is critical for EGFR early endosome exit, lysosome sorting, and degradation [18,>>19<<]. Since low levels of EGFR ubiquitination and poor Cbl association were observed in RBE cells, we considered these factors to be attributed to the dramatically diminished EGFR degradation in RBE cells.
n2:mentions: n3:18508924

Subject Item: _:vb15978307
rdf:type: n2:Context
rdf:value: Reduced Cbl association and/or impaired EGFR ubiquitination could be linked with a Cbl mutation in the RING Finger domain, especially cysteine 381 (C381), which is the first cysteine of the C3HC4 zinc finger motif [>>31<<], or at the RING finger C-terminal flank, especially valine 431 (V431) and phenylalanine 434 (F434) [20].
n2:mentions: n3:10428778

Subject Item: _:vb15978308
rdf:type: n2:Context
rdf:value: Cbl mutation in the RING Finger domain, especially cysteine 381 (C381), which is the first cysteine of the C3HC4 zinc finger motif [31], or at the RING finger C-terminal flank, especially valine 431 (V431) and phenylalanine 434 (F434) [>>20<<]. Apart from mutations in c-Cbl, the loss of the Cbl docking site on EGFR (pY1068 and pY1045) for numerous reasons, such as EGFR mutations in the tyrosine kinase domain [32,33] or mutations at ubiquitination sites of EGFR [34], could also
n2:mentions: n3:20029031

Subject Item: _:vb15978309
rdf:type: n2:Context
rdf:value: Apart from mutations in c-Cbl, the loss of the Cbl docking site on EGFR (pY1068 and pY1045) for numerous reasons, such as EGFR mutations in the tyrosine kinase domain [>>32<<,33] or mutations at ubiquitination sites of EGFR [34], could also lead to reduced Cbl association and/or impaired EGFR ubiquitination.
n2:mentions: n3:17699773

Subject Item: _:vb15978310
rdf:type: n2:Context
rdf:value: Apart from mutations in c-Cbl, the loss of the Cbl docking site on EGFR (pY1068 and pY1045) for numerous reasons, such as EGFR mutations in the tyrosine kinase domain [32,>>33<<] or mutations at ubiquitination sites of EGFR [34], could also lead to reduced Cbl association and/or impaired EGFR ubiquitination.
n2:mentions: n3:18687633

Subject Item: _:vb15978311
rdf:type: n2:Context
rdf:value: Apart from mutations in c-Cbl, the loss of the Cbl docking site on EGFR (pY1068 and pY1045) for numerous reasons, such as EGFR mutations in the tyrosine kinase domain [32,33] or mutations at ubiquitination sites of EGFR [>>34<<], could also lead to reduced Cbl association and/or impaired EGFR ubiquitination.
n2:mentions: n3:16543144

Subject Item: _:vb15978312
rdf:type: n2:Context
rdf:value: In RBE cells, no mutations at C381, V431 or F434 of Cbl, the tyrosine kinase domain or Tyr1068 or 1045 residues of EGFR, or of the extracellular domain that binds to ligands (exon 2 ~ 16) [>>35<<] were identified.
n2:mentions: n3:14732694

Subject Item: _:vb15978313
rdf:type: n2:Context
rdf:value: Tokuzou Arao [>>36<<], was transfected into RBE cells and revealed that Myc-tagged wtEGFR was retained in early endosomes and was not sorted into late endosomes/lysosomes (data not shown).
n2:mentions: n3:19154417

Subject Item: _:vb15978314
rdf:type: n2:Context
rdf:value: However, unlike Tyr1068 that could be phosphorylated normally, Tyr1045 could not be phosphorylated following EGF stimulation. Combining this with the data from Grøvdal et al. [>>37<<], who described that a direct association of c-Cbl with EGFR pY1045 was important for MVB sorting of EGFR, we surmised that aberrant EGFR sorting into lysosomes in RBE cells was caused by an impaired association between c-Cbl and EGFR
n2:mentions: n3:15475003

Subject Item: _:vb15978315
rdf:type: n2:Context
rdf:value: Hypophosphorylation of Tyr1045 has been reported in non-small cell lung cancers (NSCLCs) bearing EGFR mutations in the tyrosine kinase domain [>>33<<] and in an EGFRvIII variant bearing an internal in-frame deletion in the extracellular domain [38].
n2:mentions: n3:18687633

Subject Item: _:vb15978316
rdf:type: n2:Context
rdf:value: of Tyr1045 has been reported in non-small cell lung cancers (NSCLCs) bearing EGFR mutations in the tyrosine kinase domain [33] and in an EGFRvIII variant bearing an internal in-frame deletion in the extracellular domain [>>38<<]. However, no EGFR mutation was identified in our RBE cells, nor was Tyr1045 of the transfected wtEGFR seen to be phosphorylated (data not shown).
n2:mentions: n3:16969069

Subject Item: _:vb15978317
rdf:type: n2:Context
rdf:value: Willmarth et al. [>>39<<] reported similar findings caused by stimulation with one member of the EGF family, Amphiregulin (AR), in SUM149 human breast cancer cells.
n2:mentions: n3:18951974

Subject Item: _:vb15978318
rdf:type: n2:Context
rdf:value: study, AR activation of EGFR resulted in increased steady-state levels of the receptor that accumulated at the cell surface as a result of decreased phosphorylation of Tyr1045 on EGFR (wild type) and a resultant failure to ubiquitinate [>>39<<]. However, the mechanism of Tyr1045 hypophosporylation without mutation as in RBE cells remains unclear.
n2:mentions: n3:18951974

Subject Item: _:vb15978319
rdf:type: n2:Context
rdf:value: an abnormality of EGFR or its ligand, a diminished EGF-EGFR interaction affinity and reduced receptor-associated tyrosine kinase activity caused by phosphorylation of EGFR threonine residues through protein kinase C (PKC)-dependent [>>40<<] or independent pathways [41] may be speculated as the mechanism of Tyr1045 hypophosphorylation in RBE cells.
n2:mentions: n3:3379075

Subject Item: _:vb15978320
rdf:type: n2:Context
rdf:value: its ligand, a diminished EGF-EGFR interaction affinity and reduced receptor-associated tyrosine kinase activity caused by phosphorylation of EGFR threonine residues through protein kinase C (PKC)-dependent [40] or independent pathways [>>41<<] may be speculated as the mechanism of Tyr1045 hypophosphorylation in RBE cells.
n2:mentions: n3:3106361

Subject Item: _:vb15978321
rdf:type: n2:Context
rdf:value: Lastly, we employed two methods to verify the role of EGFR recycling in cell membrane EGFR over-expression: monensin treatment [>>24<<,42] and Rab11a protein depletion [43]. Rab proteins regulate various steps in recycling:
n2:mentions: n3:19948031

Subject Item: _:vb15978322
rdf:type: n2:Context
rdf:value: Lastly, we employed two methods to verify the role of EGFR recycling in cell membrane EGFR over-expression: monensin treatment [24,>>42<<] and Rab11a protein depletion [43]. Rab proteins regulate various steps in recycling:
n2:mentions: n3:20616078

Subject Item: _:vb15978323
rdf:type: n2:Context
rdf:value: Lastly, we employed two methods to verify the role of EGFR recycling in cell membrane EGFR over-expression: monensin treatment [24,42] and Rab11a protein depletion [>>43<<]. Rab proteins regulate various steps in recycling: Rab4 regulates fast/direct recycling from the early endosome to the cell membrane [44], and Rab11a regulates recycling from the deeper perinuclear recycling compartment [43].
n2:mentions: n3:9600939

Subject Item: _:vb15978324
rdf:type: n2:Context
rdf:value: Rab proteins regulate various steps in recycling: Rab4 regulates fast/direct recycling from the early endosome to the cell membrane [>>44<<], and Rab11a regulates recycling from the deeper perinuclear recycling compartment [43].
n2:mentions: n3:15040445

Subject Item: _:vb15978325
rdf:type: n2:Context
rdf:value: Rab proteins regulate various steps in recycling: Rab4 regulates fast/direct recycling from the early endosome to the cell membrane [44], and Rab11a regulates recycling from the deeper perinuclear recycling compartment [>>43<<]. Monensin treatment blocks recycling from both the early endosome and perinuclear recycling compartment [24]. Suppressed cell surface EGFR expression by monensin treatment or Rab11a depletion indicated that enhanced recycling occurred at
n2:mentions: n3:9600939

Subject Item: _:vb15978326
rdf:type: n2:Context
rdf:value: Monensin treatment blocks recycling from both the early endosome and perinuclear recycling compartment [>>24<<]. Suppressed cell surface EGFR expression by monensin treatment or Rab11a depletion indicated that enhanced recycling occurred at least in the perinuclear recycling compartment in RBE cells with EGF stimulation. Furthermore, early
n2:mentions: n3:19948031

Subject Item: _:vb15978327
rdf:type: n4:Section
dc:title: background
n4:contains: _:vb15978344 _:vb15978345 _:vb15978346 _:vb15978347 _:vb15978336 _:vb15978337 _:vb15978338 _:vb15978339 _:vb15978340 _:vb15978341 _:vb15978342 _:vb15978343 _:vb15978328 _:vb15978329 _:vb15978330 _:vb15978331 _:vb15978332 _:vb15978333 _:vb15978334 _:vb15978335

Subject Item: _:vb15978328
rdf:type: n2:Context
rdf:value: Cholangiocarcinoma is the second most common primary malignancy of the liver whose only therapeutic option is radical surgical resection or hepatectomy [>>1<<]. As the 5-year overall survival rate with curative resection (R0 resection) is reported to be 30.4% for intrahepatic cholangiocarcinoma [2], effective adjuvant therapy is needed to improve disease prognosis.
n2:mentions: n3:21491796

Subject Item: _:vb15978329
rdf:type: n2:Context
rdf:value: As the 5-year overall survival rate with curative resection (R0 resection) is reported to be 30.4% for intrahepatic cholangiocarcinoma [>>2<<], effective adjuvant therapy is needed to improve disease prognosis.
n2:mentions: n3:19212186

Subject Item: _:vb15978330
rdf:type: n2:Context
rdf:value: Molecular-targeted treatment is superior to traditional chemotherapy through its ability to selectively suppress cancer cells. Overexpression [>>3<<], gene amplification [4], and mutation [5] of epidermal growth factor receptor (EGFR) have all been associated with the tumorigenesis and progression of cholangiocarcinoma, and thus EGFR and its molecular transducers are thought to be
n2:mentions: n3:18087285

Subject Item: _:vb15978331
rdf:type: n2:Context
rdf:value: Molecular-targeted treatment is superior to traditional chemotherapy through its ability to selectively suppress cancer cells. Overexpression [3], gene amplification [>>4<<], and mutation [5] of epidermal growth factor receptor (EGFR) have all been associated with the tumorigenesis and progression of cholangiocarcinoma, and thus EGFR and its molecular transducers are thought to be ideal therapeutic targets
n2:mentions: n3:15892172

Subject Item: _:vb15978332
rdf:type: n2:Context
rdf:value: Molecular-targeted treatment is superior to traditional chemotherapy through its ability to selectively suppress cancer cells. Overexpression [3], gene amplification [4], and mutation [>>5<<] of epidermal growth factor receptor (EGFR) have all been associated with the tumorigenesis and progression of cholangiocarcinoma, and thus EGFR and its molecular transducers are thought to be ideal therapeutic targets for
n2:mentions: n3:16032426

Subject Item: _:vb15978333
rdf:type: n2:Context
rdf:value: factor receptor (EGFR) have all been associated with the tumorigenesis and progression of cholangiocarcinoma, and thus EGFR and its molecular transducers are thought to be ideal therapeutic targets for cholangiocarcinoma treatment [>>6<<,7]. However, further understanding of the mechanism of aberrant EGFR signaling is needed to refine molecular targeted therapy due to the limited response rate of cholangiocarcinoma to EGFR-targeted therapy in clinical trial [8].
n2:mentions: n3:20164661

Subject Item: _:vb15978334
rdf:type: n2:Context
rdf:value: factor receptor (EGFR) have all been associated with the tumorigenesis and progression of cholangiocarcinoma, and thus EGFR and its molecular transducers are thought to be ideal therapeutic targets for cholangiocarcinoma treatment [6,>>7<<]. However, further understanding of the mechanism of aberrant EGFR signaling is needed to refine molecular targeted therapy due to the limited response rate of cholangiocarcinoma to EGFR-targeted therapy in clinical trial [8].
n2:mentions: n3:19414361

Subject Item: _:vb15978335
rdf:type: n2:Context
rdf:value: However, further understanding of the mechanism of aberrant EGFR signaling is needed to refine molecular targeted therapy due to the limited response rate of cholangiocarcinoma to EGFR-targeted therapy in clinical trial [>>8<<].
n2:mentions: n3:18025804

Subject Item: _:vb15978336
rdf:type: n2:Context
rdf:value: EGFR has important functions in cell proliferation, survival, migration, and differentiation via the activation by several distinct ligands, which include EGF, transforming growth factor-alpha and heparin-binding EGF [>>9<<]. The receptor stimulates numerous signal transduction cascades, such as those for mitogen-activated protein kinase (MAPK), phosphoinositol kinase, the anti-apoptotic kinase Akt, and several transcriptional regulators [10].
n2:mentions: n3:10404636

Subject Item: _:vb15978337
rdf:type: n2:Context
rdf:value: The receptor stimulates numerous signal transduction cascades, such as those for mitogen-activated protein kinase (MAPK), phosphoinositol kinase, the anti-apoptotic kinase Akt, and several transcriptional regulators [>>10<<]. Aberrant EGFR activity has been shown to play a key role in the development and growth of various types of cancer cells [11,12]. To date, several mechanisms involving abnormal activation of EGFR have been reported, including increased
n2:mentions: n3:11597398

Subject Item: _:vb15978338
rdf:type: n2:Context
rdf:value: Aberrant EGFR activity has been shown to play a key role in the development and growth of various types of cancer cells [>>11<<,12]. To date, several mechanisms involving abnormal activation of EGFR have been reported, including increased production of ligands, increased levels of EGFR protein, EGFR mutations giving rise to constitutively active variants,
n2:mentions: n3:17234795

Subject Item: _:vb15978339
rdf:type: n2:Context
rdf:value: Aberrant EGFR activity has been shown to play a key role in the development and growth of various types of cancer cells [11,>>12<<]. To date, several mechanisms involving abnormal activation of EGFR have been reported, including increased production of ligands, increased levels of EGFR protein, EGFR mutations giving rise to constitutively active variants, defective
n2:mentions: n3:21665310

Subject Item: _:vb15978340
rdf:type: n2:Context
rdf:value: reported, including increased production of ligands, increased levels of EGFR protein, EGFR mutations giving rise to constitutively active variants, defective down-regulation of EGFR, and cross-talk with heterologous receptor systems [>>13<<].
n2:mentions: n3:17681753

Subject Item: _:vb15978341
rdf:type: n2:Context
rdf:value: Down-regulation of EGFR by endocytosis and degradation is the major negative regulatory mechanism of attenuating EGFR signaling activation [>>14<<]. Upon ligand binding, cell surface EGFR is endocytosed into the cytosol and sequestered in a sorting/early endosome for either recycling or degradation [15].
n2:mentions: n3:19696798

Subject Item: _:vb15978342
rdf:type: n2:Context
rdf:value: Upon ligand binding, cell surface EGFR is endocytosed into the cytosol and sequestered in a sorting/early endosome for either recycling or degradation [>>15<<]. Ubiquitination mediated by the E3 ubiquitin ligase Cbl is a key post-translational protein modification in EGFR endocytosis in porcine aortic endothelial (PAE), Hela, and laryngeal carcinoma cell line Hep2 cells [16,17], as well as in
n2:mentions: n3:11864992

Subject Item: _:vb15978343
rdf:type: n2:Context
rdf:value: Ubiquitination mediated by the E3 ubiquitin ligase Cbl is a key post-translational protein modification in EGFR endocytosis in porcine aortic endothelial (PAE), Hela, and laryngeal carcinoma cell line Hep2 cells [>>16<<,17], as well as in EGFR degradation in Chinese hamster ovary (CHO) and human embryonic kidney (HEK) cell line 293 T cells [18,19].
n2:mentions: n3:12631709

Subject Item: _:vb15978344
rdf:type: n2:Context
rdf:value: Ubiquitination mediated by the E3 ubiquitin ligase Cbl is a key post-translational protein modification in EGFR endocytosis in porcine aortic endothelial (PAE), Hela, and laryngeal carcinoma cell line Hep2 cells [16,>>17<<], as well as in EGFR degradation in Chinese hamster ovary (CHO) and human embryonic kidney (HEK) cell line 293 T cells [18,19].
n2:mentions: n3:15194809

Subject Item: _:vb15978345
rdf:type: n2:Context
rdf:value: in EGFR endocytosis in porcine aortic endothelial (PAE), Hela, and laryngeal carcinoma cell line Hep2 cells [16,17], as well as in EGFR degradation in Chinese hamster ovary (CHO) and human embryonic kidney (HEK) cell line 293 T cells [>>18<<,19]. In a related report, Cbl mutation and reduced EGFR ubiquitination inhibited early endosome fusion and EGFR degradation in HEK 293 cells [20].
n2:mentions: n3:15210722

Subject Item: _:vb15978346
rdf:type: n2:Context
rdf:value: EGFR endocytosis in porcine aortic endothelial (PAE), Hela, and laryngeal carcinoma cell line Hep2 cells [16,17], as well as in EGFR degradation in Chinese hamster ovary (CHO) and human embryonic kidney (HEK) cell line 293 T cells [18,>>19<<]. In a related report, Cbl mutation and reduced EGFR ubiquitination inhibited early endosome fusion and EGFR degradation in HEK 293 cells [20].
n2:mentions: n3:18508924

Subject Item: _:vb15978347
rdf:type: n2:Context
rdf:value: In a related report, Cbl mutation and reduced EGFR ubiquitination inhibited early endosome fusion and EGFR degradation in HEK 293 cells [>>20<<].
n2:mentions: n3:20029031

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