GDNF–Induced Activation of the Ret Protein Tyrosine Kinase Is Mediated by GDNFR-α, a Novel Receptor for GDNF
Shuqian Jing,Duanzhi Wen,Yanbin Yu,Paige Holst,Yi Luo,Mei Fang,Rami Tamir,Laarni Antonio,Zheng Hu,Rod Cupples,Jean-Claude Louis,Sylvia Hu,Bruce W. Altrock,Gary M. Fox +13 more
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TLDR
In this paper, the expression cloning and characterization of GDNFR-α, a novel glycosylphosphatidylinositol-linked cell surface receptor for glial cell line-derived neurotrophic factor (GDNF), was reported.About:
This article is published in Cell.The article was published on 1996-06-28 and is currently open access. It has received 1164 citations till now. The article focuses on the topics: Glial cell line-derived neurotrophic factor & GDNF family of ligands.read more
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Patent
Polypeptide derivatives of parathyroid hormone (pth)
TL;DR: Novel parathyroid hormone (PTH) polypeptide derivatives are disclosed in this article, as well as pharmaceutical compositions containing said poly-peptides, and synthetic and recombinant methods for producing them.
Journal ArticleDOI
A new germline RET mutation apparently devoid of transforming activity serendipitously discovered in a patient with atrophic autoimmune thyroiditis and primary ovarian failure
G Orgiana,G. Pinna,Andrea Camedda,De Falco,Massimo Santoro,Rm Melillo,Rossella Elisei,Cristina Romei,S. Lai,Carlo Carcassi,Stefano Mariotti +10 more
TL;DR: A new RET point mutation (R694Q (CGG→CAG) was found in a 23-yr-old woman with hypothyroidism due to atrophic Hashimoto's thyroiditis and primary ovarian failure, without altered calcitonin secretion as discussed by the authors.
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Glial cell line-derived neurotrophic factor-like immunoreactivity in the cerebella of normal subjects and patients with multiple system atrophy.
TL;DR: Examination of the cerebella of eight control cases and eight patients with multiple system atrophy immunohistochemically suggests that GDNF may be mainly produced and localized in the Purkinje cells of the human cerebellum, even in patients with MSA, and that the functional impairment of the Purkine cells of MSA patients might cause a focal accumulation of GDNF in the dendrites of some of the surviving Purkin Je cells.
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Glial cell line-derived neurotrophic factor induces cell proliferation in the mouse urogenital sinus.
Hyun Jung Park,Eric C. Bolton +1 more
TL;DR: It is determined that exogenous GDNF increases proliferation of UrM and UrE cells, altering UGS morphology, thus implicating GDNF signaling in prostate development and growth.
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How familial cancer genes and environmentally induced oncogenes have changed the endocrine landscape.
TL;DR: The gene responsible for MEN-2, the ret proto-ocogene, has elucidated mechanisms of endocrine tumorigenesis, leading to a better understanding of papillary thyroid carcinoma and provides a novel immunohistochemical marker that widens the diagnostic armamentarium.
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Antibodies: A Laboratory Manual
Ed Harlow,David P. Lane +1 more
TL;DR: A second edition of Antibodies: A Laboratory Manual is being published in September 2013, Revised, extended and updated by Edward Greenfield of the Dana-Farber Cancer Center, the material has been recast with extensive new information and new chapters have been added.
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Improved tools for biological sequence comparison.
TL;DR: Three computer programs for comparisons of protein and DNA sequences can be used to search sequence data bases, evaluate similarity scores, and identify periodic structures based on local sequence similarity.
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Signal transduction by receptors with tyrosine kinase activity
Axel Ullrich,Joseph Schlessinger +1 more
TL;DR: Cet article synthese montre comment des recepteurs membranaires a activite tyrosine kinase peuvent etre impliques dans la transduction and notamment jouent le role de signal de the transduction.
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An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs
TL;DR: 5'-Noncoding sequences have been compiled from 699 vertebrate mRNAs and GCCA/GCCATGG emerges as the consensus sequence for initiation of translation in vertebrates.
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A new method for predicting signal sequence cleavage sites.
TL;DR: A new method for identifying secretory signal sequences and for predicting the site of cleavage between a signal sequence and the mature exported protein is described.
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