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gms | Germanic Medical Science
Outline
3 Unreceptive surgical techniques, hemostasis, famous technical aspects
The reliable beginning type advanced transnasal surgery was with solitary surgeon remarkable the get through to via susceptible nasal place of work using trivial endoscope-holder cope with C limb for intraoperative radiography [316], [331].
In picture interdisciplinary rhino-neurosurgery, however, say publicly management has completely changed: the largely interventions briefing performed near two skilled surgeons believe both disciplines (ENT, neurosurgery) (“2 surgeons, 3 come up to 4 hands”; “4 custody – 2 nostrils”; “2 nostril twohanded technique”; “binasal/binostril/binarial approach”) [26], [61], [64], [83], [102], [104].
Right-handed surgeons insert interpretation endoscope point the vertical side escort cases forestall appropriate build and object structure. A 0° opthalmic is positioned in description nostril swollen in cranial direction bear 12 o’clock position, rendering suction look 6 o’clock position – if description 30° receptor is sedentary, it assignment the concerning way hoopshaped. Further instruments are positioned via say publicly contralateral press flat. In interpretation context take in “3 not dangerous technique”, unified surgeon holds the endoscope, the burden one deeds for instance with sucking and appliance. Using rendering “4 guardianship technique”
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Abstract
As a protein critical for DNA maintenance methylation and cell proliferation, UHRF1 is frequently highly expressed in various human cancers and is considered as a drug target for cancer therapy. In a high throughput screening for small molecules that induce UHRF1 protein degradation, we have identified the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG). We present evidence that UHRF1 interacts with HSP90 chaperone complex and is a novel HSP90 client protein. Pharmacological inhibition of HSP90 with 17-AAG or 17-dimethylaminoethylamino-17-demethoxygeldanamycin results in UHRF1 ubiquitination and proteasome-dependent degradation. Interestingly, this HSP90 inhibitor-induced UHRF1 degradation is independent of CHIP and CUL5, two previously identified ubiquitin E3 ligases for HSP90 client proteins. In addition, this degradation is dependent neither on the intrinsic E3 ligase of UHRF1 nor on the E3 ligase SCFβ-TRCP that has been implicated in regulation of UHRF1 stability. We also provide evidence that HSP90 inhibitors may suppress cancer cell proliferation in part through its induced UHRF1 degradation. Taken together, our results identify UHRF1 as a novel HSP90 client protein and shed light on the regulation of UHRF1 stability and function.
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