The Carboxy Terminal Domain of Connexin43

نویسندگان

چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The carboxy-terminal domain initiates trimerization of bacteriophage T4 fibritin.

Bacteriophage T4 fibritin is a triple-stranded, parallel, segmented alpha-helical coiled-coil protein. Earlier we showed that the C-terminal globular domain (foldon) of fibritin is essential for correct trimerization and folding of the protein. We constructed the chimerical fusion protein W31 in which the fibritin foldon sequence is followed by the small globular non-alpha-helical protein gp31 ...

متن کامل

The carboxy-terminal domain of complexin I stimulates liposome fusion.

Regulated exocytosis requires tight coupling of the membrane fusion machinery to a triggering signal and a fast response time. Complexins are part of this regulation and, together with synaptotagmins, control calcium-dependent exocytosis. Stimulatory and inhibitory functions have been reported for complexins. To test if complexins directly affect membrane fusion, we analyzed the 4 known mammali...

متن کامل

Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase

RNA helicases are essential for virtually all cellular processes, however, their regulation is poorly understood. The activities of eight RNA helicases are required for pre-mRNA splicing. Amongst these, Brr2p is unusual in having two helicase modules, of which only the amino-terminal helicase domain appears to be catalytically active. Using genetic and biochemical approaches, we investigated in...

متن کامل

The carboxy terminal domain of connexin43: from molecular regulation of the gap junction channel to supramolecular organization of the intercalated disk.

Cardiac function depends fundamentally on gap junctions, plaques of transmembrane channels constructed from connexin proteins that bridge the plasma membranes of adjacent myocytes. By electrically coupling the entire myocyte population of the heart, these junctions preside over the cell-to-cell passage of the precisely orchestrated patterns of current flow that synchronize, coordinate, and harn...

متن کامل

A colipase fold in the carboxy-terminal domain of the Wnt antagonists – the Dickkopfs

It has recently been shown that a class of secreted proteins — the Dickkopfs — are released by the Spemann organizer of Xenopus and are potent antagonists of Wnt signaling [1]. Although it has been reported that the Dickkopf (Dkk) proteins contain two cysteine-rich domains, no direct functional or structural conclusions have been drawn from their sequences. The role of Wnt signaling in animal d...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Circulation Research

سال: 2007

ISSN: 0009-7330,1524-4571

DOI: 10.1161/circresaha.107.165662