Zobrazeno 1 - 10
of 113
pro vyhledávání: '"Marvin L. Tanzer"'
Publikováno v:
Archives of Oral Biology. 48:263-271
A number of studies have implicated the fibrin-coagulation-fibrinolysis system in human tumour progression. Interleukin-8 (IL-8) mediates most of the angiogenic activity induced by human oral squamous cell carcinoma (OSCC) cells. We have recently dem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79a18fa469fe4f4847f483ec8b0f8a4a
https://doi.org/10.1016/s0003-9969(03)00005-0
https://doi.org/10.1016/s0003-9969(03)00005-0
Autor:
Peiyin Y. Wang, Nina W. Flay, Seung S. Gwon, Wei Luo, Marvin L. Tanzer, Barbara M. Vertel, Tung-Ling L. Chen, Jing Zheng, Chunxia Guo
Publikováno v:
Experimental Cell Research. 263:224-235
In this article, we report the misdirected targeting of expressed aggrecan domains. Aggrecan, the chondroitin sulfate (CS) proteoglycan of cartilage, normally progresses through the exocytic pathway. Proteins expressed from constructs containing the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecf9dc9e30f334756470eaed6b859f42
https://doi.org/10.1006/excr.2000.5093
https://doi.org/10.1006/excr.2000.5093
Publikováno v:
Journal of Biological Chemistry. 271:16447-16450
The proteoglycan, aggrecan has a globular domain, G1, at the N terminus and a different globular domain, G3, at the C terminus. Aggrecan produced by mutant nanomelic chickens is truncated due to a premature stop codon and consequently lacks G3 and a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5093c18697ba6406be4e4ed9b08ee243
https://doi.org/10.1074/jbc.271.28.16447
https://doi.org/10.1074/jbc.271.28.16447
Publikováno v:
Journal of Biological Chemistry. 271:7891-7894
Several lines of evidence indicate that calreticulin has lectin-like properties. As a molecular chaperone, calreticulin binds preferentially to nascent glycoproteins via their immature carbohydrates; this property closely resembles that seen for caln
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26117f83e249ab015bef7bdc9567bcf8
https://doi.org/10.1074/jbc.271.14.7891
https://doi.org/10.1074/jbc.271.14.7891
Publikováno v:
Journal of Cellular Biochemistry. 58:527-534
The dystrophin-glycoprotein complex plays an important role in muscle function. One of the components of the complex, a 156-kDa cell surface glycoprotein (alpha-dystroglycan) binds to laminin, thereby connecting the basal lamina and muscle cells. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3acc3aab94b58532036bb56b0c1a162a
https://doi.org/10.1002/jcb.240580416
https://doi.org/10.1002/jcb.240580416
Publikováno v:
Biology of the Cell. 83:39-47
Snail muscles were extracted by a solution of EDTA and electron microscopy showed that the extract contained dispersed, depolymerized collagen fibrils and cross-shaped laminin-like structures. The extracts were purified by ultracentrifugation followe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80bcd9628e74db9dec2acfab5f98a8e8
https://doi.org/10.1016/0248-4900(96)89930-8
https://doi.org/10.1016/0248-4900(96)89930-8
Publikováno v:
Journal of Biological Chemistry. 269:3367-3373
The spreading of murine melanoma cells on unglycosylated laminin is initiated by soluble glycosylated laminins containing oligomannosides, or by mannan, and is inhibited by mannose (Chandrasekaran, S., Tanzer, M. L., and Giniger, M. S. (1994) J. Biol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5b573bccf247a0a0f66a33ebf9041810
https://doi.org/10.1016/s0021-9258(17)41871-0
https://doi.org/10.1016/s0021-9258(17)41871-0
Publikováno v:
Journal of Biological Chemistry. 269:3356-3366
Murine melanoma cells readily bind and spread on murine laminin. Uncoupling of spreading from adhesion occurs when unglycosylated laminin is used as the cellular substratum; spreading is restored by soluble glycosylated laminin or soluble glycopeptid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::54e6979126025be69c37891759fce596
https://doi.org/10.1016/s0021-9258(17)41870-9
https://doi.org/10.1016/s0021-9258(17)41870-9
Publikováno v:
Experientia. 49:384-392
The large aggregating chondroitin sulfate proteoglycan of cartilage, aggrecan, has served as a prototype of proteoglycan structure. Molecular cloning has elucidated its primary structure and revealed both known and unknown domains. To date the comple
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a6fe5abe1cee334ebe9b14792ddb70b
https://doi.org/10.1007/bf01923583
https://doi.org/10.1007/bf01923583
Publikováno v:
Kidney International. 43(1):66-72
Role of laminin carbohydrates on cellular interactions. Laminins, a family of large multidomain glycoproteins of the basal lamina, have been implicated in the development and maintenance of cellular and tissue organization. Considerable interest has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14fb507540b27e318aa9689b75763353