Collagen XII Interacts with Avian Tenascin-X through Its NC3 Domain

نویسندگان
چکیده

برای دانلود رایگان 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

Tenascin-X, collagen, elastin, and the Ehlers-Danlos syndrome.

Tenascin-X is an extracellular matrix protein initially identified because the gene encoding it overlaps with the human CYP21B gene. Because studies of gene and protein function of other tenascins had been poorly predictive of essential functions in vivo, we used a genetic approach that critically relied on an understanding of the genomic locus to uncover an association between inactivating ten...

متن کامل

STAC3 stably interacts through its C1 domain with CaV1.1 in skeletal muscle triads

The adaptor protein STAC3 is essential for skeletal muscle excitation-contraction (EC) coupling and a mutation in the STAC3 gene has been linked to a severe muscle disease, Native American myopathy (NAM). However the function of STAC3, its interaction partner, and the mode of interaction within the EC-coupling complex remained elusive. Here we demonstrate that STAC3 forms a stable interaction w...

متن کامل

Immunolocalization of type XII collagen at the corneoscleral angle of the embryonic avian eye.

A monoclonal antibody specific for the chicken alpha 1 (XII) collagen chain was used to immunolocalize type XII collagen in the corneoscleral of 17-19-day-old chicken embryos. These immunofluorescence studies localized type XII collagen around the scleral cartilages and ossicles. There was also a striking positive staining in the scleral spur and stroma of the corneolimbus beneath the external ...

متن کامل

TEM8 Interacts with the Cleaved C5 Domain of Collagen 3(VI)

Tumor endothelial marker (TEM)8 was uncovered as a gene expressed predominantly in tumor endothelium, and its protein product was recently identified as the receptor for anthrax toxin. Here, we demonstrate that TEM8 protein is preferentially expressed in endothelial cells of neoplastic tissue. We used the extracellular domain of TEM8 to search for ligands and identified the 3 subunit of collage...

متن کامل

The phospholipase PNPLA7 functions as a lysophosphatidylcholine hydrolase and interacts with lipid droplets through its catalytic domain

Mammalian patatin-like phospholipase domain-containing proteins (PNPLAs) are lipid-metabolizing enzymes with essential roles in energy metabolism, skin barrier development, and brain function. A detailed annotation of enzymatic activities and structure-function relationships remains an important prerequisite to understand PNPLA functions in (patho-)physiology, for example, in disorders such as ...

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: Journal of Biological Chemistry

سال: 2006

ISSN: 0021-9258

DOI: 10.1074/jbc.m603147200