Zobrazeno 1 - 10
of 91
pro vyhledávání: '"Irena Ekiel"'
Autor:
Naghmeh S Sarraf, Rong Shi, Laura McDonald, Jason Baardsnes, Linhua Zhang, Miroslaw Cygler, Irena Ekiel
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e100441 (2014)
CbpA is one of the six E. coli DnaJ/Hsp40 homologues of DnaK co-chaperones and the only one that is additionally regulated by a small protein CbpM, conserved in γ-proteobacteria. CbpM inhibits the co-chaperone and DNA binding activities of CbpA. Thi
Externí odkaz:
https://doaj.org/article/9021c492fb554733aff47bf95aa8287c
Publikováno v:
BioTechniques, Vol 26, Iss 1, Pp 142-149 (1999)
Fusion proteins are frequently used in the functional characterization of newly discovered proteins and to identify interacting partners. In our study of hPTP1E, a cytosolic protein tyrosine phosphatase, we used glutathione S-transferase (GST)-fusion
Externí odkaz:
https://doaj.org/article/b8b598660b92428ba52b3d92ed605487
Autor:
Jason Baardsnes, Irena Ekiel, Doreen Harcus, Miroslaw Cygler, Volodymyr Yerko, Traian Sulea, Malcolm Whiteway, Cunle Wu
Publikováno v:
Molecular Biology of the Cell
The Ras-binding domain is conserved among fungal Ste11 MAPKKKs and is critical for mating in fungi. Its interaction with Ras1 is critical for Schizosaccharomyces pombe mating, whereas in Saccharomyces cerevisiae its interaction with the Ste5 PH domai
Autor:
Maureen D. O'Connor-McCourt, Miroslaw Cygler, Irena Ekiel, Jing Cheng, Naghmeh S. Sarraf, Jason Baardsnes
Publikováno v:
Journal of Molecular Biology. 398:111-121
CbpA, one of the Escherichia coli DnaJ homologues, acts as a co-chaperone in the DnaK chaperone system. Despite its extensive similarity in domain structure and function to DnaJ, CbpA has a unique and specific regulatory mechanism mediated through th
Autor:
Olga Vavelyuk, Miroslaw Cygler, Irena Ekiel, Ming-Ni Hung, Ovidiu M. Minailiuc, Shaifali Gandhi
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 66:1004-1007
Autor:
Joseph D. Schrag, Audrey Perreault, Guennadi Kozlov, Kalle Gehring, Irena Ekiel, Morag Park, Miroslaw Cygler
Publikováno v:
Biochemical and Biophysical Research Communications. 321:234-240
PSI domains are cysteine-rich modules found in extracellular fragments of hundreds of signaling proteins, including plexins, semaphorins, integrins, and attractins. Here, we report the solution structure of the PSI domain from the human Met receptor,
Autor:
Gregory De Crescenzo, Kalle Gehring, Avak Kahvejian, Guennadi Kozlov, Nadeem Siddiqui, Nadia S Lim, Nahum Sonenberg, Demetra Elias, Jean-François Trempe, Irena Ekiel, Daniel Fantus, Maureen D. O'Connor-McCourt
Publikováno v:
The EMBO Journal. 23:272-281
The C-terminal domain of poly(A)-binding protein (PABC) is a peptide-binding domain found in poly(A)-binding proteins (PABPs) and a HECT (homologous to E6 -AP C-terminus) family E3 ubiquitin ligase. In protein synthesis, the PABC domain of PABP funct
Autor:
Kalle Gehring, Tara Sprules, Jean-François Trempe, Nadeem Siddiqui, Irena Ekiel, Stephane Coillet-Matillon, Guennadi Kozlov
Publikováno v:
Journal of Biological Chemistry. 277:22822-22828
We have determined the solution structure of the PABC domain from Saccharomyces cerevisiae Pab1p and mapped its peptide-binding site. PABC domains are peptide binding domains found in poly(A)-binding proteins (PABP) and are a subset of HECT-family E3
Publikováno v:
FEBS Letters. 513:147-152
Six charged amino acid residues located in the ectodomain of the full-length type I transforming growth factor (TGF)-β receptor were individually mutated to alanine. Mutation of residues D47, D98, K102 and E104 resulted in functionally impaired rece
Autor:
Irena Ekiel, Miroslaw Cygler, Laura McDonald, Linhua Zhang, Jason Baardsnes, Naghmeh S. Sarraf, Rong Shi
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 6, p e100441 (2014)
PLoS ONE, Vol 9, Iss 6, p e100441 (2014)
CbpA is one of the six E. coli DnaJ/Hsp40 homologues of DnaK co-chaperones and the only one that is additionally regulated by a small protein CbpM, conserved in γ-proteobacteria. CbpM inhibits the co-chaperone and DNA binding activities of CbpA. Thi