نتایج جستجو برای: fusion partner

تعداد نتایج: 158179  

Journal: :Cancer research 1999
H Sjögren J Meis-Kindblom L G Kindblom P Aman G Stenman

Extraskeletal myxoid chondrosarcomas (EMCs) are characterized by a recurrent t(9;22)(q22;q12) translocation, resulting in the fusion of the EWS gene in 22q12 and the TEC gene in 9q22. Here we report that a third member of the EWS, TLS/FUS gene family, TAF2N, can replace EWS as a fusion partner to TEC in EMC. Two tumors, one with a novel t(9;17)(q22;q11) variant translocation and one with an app...

2011
Kevin Moreau Brinda Ravikumar Maurizio Renna Claudia Puri David C. Rubinsztein

Autophagy is a catabolic process in which lysosomes degrade intracytoplasmic contents transported in double-membraned autophagosomes. Autophagosomes are formed by the elongation and fusion of phagophores, which can be derived from preautophagosomal structures coming from the plasma membrane and other sites like the endoplasmic reticulum and mitochondria. The mechanisms by which preautophagosoma...

Journal: :Protein expression and purification 2003
Gregor Anderluh Isa Gökçe Jeremy H Lakey

The third domain of the periplasmic protein TolA from Escherichia coli (TolAIII) was used as a fusion partner in the expression of various proteins from bacteria and eukaryotes. TolAIII is small domain, expressed in high yields as a soluble protein in the cytoplasm of E. coli. Proteins were linked to the C-terminus of TolAIII by a short flexible linker containing sites for endopeptidases. Three...

Journal: :Head & neck 2010
Walter T Lee Chunrui Tan Gary Koski Suyu Shu Peter Cohen

BACKGROUND Tumor-associated antigens (TAAs) are known to be immunotherapy targets; thus tumor-sharing TAA may be used as a fusion hybrid partner to confer protection against subsequent tumor challenge. METHODS The squamous cell carcinomas (SCCs), SCCVII and B4B8, were used in C3H/HEN mice: SCCVII (H-2(k)) is syngeneic, B4B8 (H-2(d)) is allogeneic. Experiments using tumor alone included hyperi...

Journal: :Haematologica 2011
Bartosz Wasag Els Lierman Peter Meeus Jan Cools Peter Vandenberghe

We report a patient with T-lymphoblastic leukemia/lymphoma and a t(7;8)(q22;p11). CUX1 was identified as the fusion partner of FGFR1 by fluorescence in situ hybridization and 5' RACE-PCR. We further investigated this novel FGFR1 fusion using the interleukin-3 (IL-3) dependent Ba/F3 cell line and demonstrated IL-3 independent cell growth of CUX1-FGFR1 expressing cells. TKI258 and PKC412 potently...

Journal: :The EMBO journal 2006
Ruud F Toonen Olexiy Kochubey Heidi de Wit Attila Gulyas-Kovacs Bas Konijnenburg Jakob B Sørensen Jurgen Klingauf Matthijs Verhage

Secretory vesicles dock at their target in preparation for fusion. Using single-vesicle total internal reflection fluorescence microscopy in chromaffin cells, we show that most approaching vesicles dock only transiently, but that some are captured by at least two different tethering modes, weak and strong. Both vesicle delivery and tethering depend on Munc18-1, a known docking factor. By decrea...

Journal: :Cell 2003
Dimiter S Dimitrov

The membrane-associated carboxypeptidase angiotensin-converting enzyme 2 (ACE2) is an essential regulator of heart function. Now, Li at al. identify and characterize an unexpected second function of ACE2 as a partner of the SARS-CoV spike glycoprotein in mediating virus entry and cell fusion.

2017
Margaret D Myers Gregory S Payne

Yeast Vps13 is a member of a conserved protein family that includes human homologues associated with neurodegenerative and developmental disorders. In this issue, De et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201606078) establish direct roles for Vps13 and its surprising binding partner, the calcium-binding centrin Cdc31, in trans-Golgi network (TGN) to endosome traffic and TGN hom...

Journal: :Current Biology 1999
Michael J Clague

Recent studies of how vesicles are targeted to fuse with specific membranes inside cells highlight a role for extended coiled-coil proteins in tethering partner membranes prior to formation of the 'SNARE complex' that mediates the fusion reaction. The tethering protein is recruited to membranes by a Rab family GTPase

Journal: :Infection and immunity 1999
M S Turner P M Giffard

The basic surface protein, BspA, has been used as a fusion partner to direct peptide antigens from the human immunodeficiency virus gp41 protein and the Chlamydia psittaci OmpA protein to the cell surface of Lactobacillus fermentum BR11. BspA has potential utility in the construction of live vaccines and diagnostic reagents.

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