About: Hedgehog patterning activity: role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain

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About: Hedgehog patterning activity: role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain Goto Sponge NotDistinct Permalink

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scientific journal article

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description	artículu científicu espublizáu en 1996 (ast) vědecký článek publikovaný v roce 1996 (cs) 1996 թուականի Յուլիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в липні 1996 (uk) 1996 թվականի հուլիսին հրատարակված գիտական հոդված (hy) vedecký článok (publikovaný 1996/07/12) (sk) مقالة علمية (نشرت في 12-7-1996) (ar) wetenschappelijk artikel (gepubliceerd op 1996/07/12) (nl) article scientifique publié en 1996 (fr) scientific journal article (en) im Juli 1996 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28609824-E843ABF0-12F1-46B7-B303-05FB3F8D33BF
publication date	1996-07-12 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28609824-06630958-3538-4C65-81B0-CB8073058BCD
language of work or name	English
cites work	wds:Q28609824-0F98017B-D86B-4B34-80D5-0DF22FE643AA wds:Q28609824-12003FF6-7E62-4F1A-8BB2-A823AD8AEB44 wds:Q28609824-1DAA37B3-D5DB-49D0-9136-43B3982B98DF wds:Q28609824-2B5D4C2F-9B0B-48F7-B0A9-B59FDD2240A8 wds:Q28609824-2CD21FEB-76EB-458F-A9AD-6FF147F51EE7 wds:Q28609824-304504F9-6DCA-4DFC-906F-1EA5C83B93BE wds:Q28609824-3263D50F-B1D9-4BDE-9A78-E29131F4D60C wds:Q28609824-3C033126-8BF0-411A-877C-DD20DB7A8AF3 wds:Q28609824-4BFCDBA0-3F91-4857-9928-CE9671B889EE wds:Q28609824-522C1792-3539-4D13-986E-BD698C1F84FD wds:Q28609824-592DF1D1-81FB-4253-9DC9-5A08A20412AC wds:Q28609824-645B1095-3462-448F-923F-5AD864CE0DA5 wds:Q28609824-698906B7-C035-4BD2-93AE-EE17197CFCAE wds:Q28609824-6F270C3E-850B-46DD-989E-9FE2DF3D5B39 wds:Q28609824-75606F54-ED27-47D5-905E-856602A13879 wds:Q28609824-76D70333-AEAB-495A-B446-70167462620A wds:Q28609824-77C6493C-7014-4373-BDCB-747B074736F3 wds:Q28609824-869529FF-15CD-44EF-A99C-EA41C0ACAEC2 wds:Q28609824-86F39AE5-EB83-40FF-9E77-CBD2C6289E1B wds:Q28609824-9A2FF934-2A7E-4F7D-AD0C-0999FA50157D wds:Q28609824-AD8300BE-D3F7-4146-897C-64D4DE5F7940 wds:Q28609824-BA3C87EC-5707-46F8-9846-1C6068910B2C wds:Q28609824-CD8C69AA-A430-45DF-B4D2-1ACF145B54A9 wds:Q28609824-D24A389A-91AB-4AF3-A9EC-433155CF200B wds:Q28609824-D8D76237-BCE1-4123-AFB1-BDCFB041D445 wds:Q28609824-DEEA8C15-E506-4D42-B097-9029AA3DB52B wds:Q28609824-F16B84E9-B052-4AFD-858F-746B7C131688 wds:Q28609824-F6F7336E-011F-40FB-A2BE-BAE0F43BB67D wds:Q28609824-FCFF97D0-5BAD-4E37-96BD-D7161351728A
cites work	Proteolytic processing yields two secreted forms of sonic hedgehog Hedgehog is a signaling protein with a key role in patterning Drosophila imaginal discs Contrasting distributions of patched and hedgehog proteins in the Drosophila embryo. Drosophila hedgehog acts as a morphogen in cellular patterning. A potential catalytic site revealed by the 1.7-A crystal structure of the amino-terminal signalling domain of Sonic hedgehog A protein splice-junction motif in hedgehog family proteins A protein catalytic framework with an N-terminal nucleophile is capable of self-activation Floor plate and motor neuron induction by different concentrations of the amino-terminal cleavage product of sonic hedgehog autoproteolysis Protein lipidation in cell signaling A new method for predicting signal sequence cleavage sites An enzyme with ubiquitin carboxy-terminal esterase activity from reticulocytes Pyruvoyl-dependent enzymes Autoproteolysis in hedgehog protein biogenesis The product of hedgehog autoproteolytic cleavage active in local and long-range signalling. Secretion of the amino-terminal fragment of the hedgehog protein is necessary and sufficient for hedgehog signalling in Drosophila. Polarity of epithelial and neuronal cells Protein splicing: self-splicing of genetically mobile elements at the protein level. The ubiquitin system for protein degradation Polyethylene membrane as a sample support for direct matrix-assisted laser desorption/ionization mass spectrometric analysis of high mass proteins Membrane proteins with soluble counterparts: role of proteolysis in the release of transmembrane proteins The membrane form of variant surface glycoproteins of Trypanosoma brucei Localized hedgehog activity controls spatial limits of wingless transcription in the Drosophila embryo. Characterization of a solvent system for separation of water-insoluble poliovirus proteins by reversed-phase high-performance liquid chromatography Synthesis of proteins by native chemical ligation Protein sequence comparison at genome scale How glycosylphosphatidylinositol-anchored membrane proteins are made The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors Ancient conserved regions in new gene sequences and the protein databases. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions
author name string	wds:Q28609824-04D45800-B2C5-4239-89D4-0269651A66A9 wds:Q28609824-442DE02A-C8C3-49D0-A604-350DEB74B387 wds:Q28609824-49A68549-3062-4492-A226-8DB5431C6096 wds:Q28609824-8DAE9254-6AC0-436D-BA11-7697775294FD wds:Q28609824-C6C15CB5-7FC2-4257-AF5C-1CB484F11774 wds:Q28609824-CFFBB142-4B59-4CC8-93DD-F4D081461748 wds:Q28609824-E53C1F9F-22ED-42B5-82A9-20A1649EECAE wds:Q28609824-EE09BFEF-B2F7-410B-BCAB-9FE498EF6630 wds:Q28609824-F3000D6D-422E-48B0-934B-76796E7F5E90 wds:Q28609824-F738582C-F67C-46F3-AD74-7330CB29846A
OpenCitations bibliographic resource ID	wds:Q28609824-DCA199C2-AC03-49AF-9509-F6B72DB1C7BA
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/4683763
author name string	Y. Ma C. H. Chen A. S. Woods D. P. von Kessler J. A. Porter K. E. Young P. A. Beachy R. J. Cotter S. C. Ekker W. J. Park
OpenCitations bibliographic resource ID	4683763
rdfs:label	Hedgehog patterning activity: role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain (en) Hedgehog patterning activity: role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain (nl) Hedgehog patterning activity: role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain (ast)

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