000119641 001__ 119641
000119641 005__ 20240228134946.0
000119641 0247_ $$2doi$$a10.1016/j.bbrc.2013.11.063
000119641 0247_ $$2pmid$$apmid:24269589
000119641 0247_ $$2ISSN$$a0006-291X
000119641 0247_ $$2ISSN$$a1090-2104
000119641 037__ $$aDKFZ-2017-00272
000119641 041__ $$aeng
000119641 082__ $$a570
000119641 1001_ $$aBerbís, M Álvaro$$b0
000119641 245__ $$aPeptides derived from human galectin-3 N-terminal tail interact with its carbohydrate recognition domain in a phosphorylation-dependent manner.
000119641 260__ $$aOrlando, Fla.$$bAcademic Press$$c2014
000119641 3367_ $$2DRIVER$$aarticle
000119641 3367_ $$2DataCite$$aOutput Types/Journal article
000119641 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1520586996_4496
000119641 3367_ $$2BibTeX$$aARTICLE
000119641 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000119641 3367_ $$00$$2EndNote$$aJournal Article
000119641 520__ $$aGalectin-3 (Gal-3) is a multi-functional effector protein that functions in the cytoplasm and the nucleus, as well as extracellularly following non-classical secretion. Structurally, Gal-3 is unique among galectins with its carbohydrate recognition domain (CRD) attached to a rather long N-terminal tail composed mostly of collagen-like repeats (nine in the human protein) and terminating in a short non-collagenous terminal peptide sequence unique in this lectin family and not yet fully explored. Although several Ser and Tyr sites within the N-terminal tail can be phosphorylated, the physiological significance of this post-translational modification remains unclear. Here, we used a series of synthetic (phospho)peptides derived from the tail to assess phosphorylation-mediated interactions with (15)N-labeled Gal-3 CRD. HSQC-derived chemical shift perturbations revealed selective interactions at the backface of the CRD that were attenuated by phosphorylation of Tyr 107 and Tyr 118, while phosphorylation of Ser 6 and Ser 12 was essential. Controls with sequence scrambling underscored inherent specificity. Our studies shed light on how phosphorylation of the N-terminal tail may impact on Gal-3 function and prompt further studies using phosphorylated full-length protein.
000119641 536__ $$0G:(DE-HGF)POF3-312$$a312 - Functional and structural genomics (POF3-312)$$cPOF3-312$$fPOF III$$x0
000119641 588__ $$aDataset connected to CrossRef, PubMed,
000119641 650_7 $$2NLM Chemicals$$aCarbohydrates
000119641 650_7 $$2NLM Chemicals$$aGalectin 3
000119641 650_7 $$2NLM Chemicals$$aPeptides
000119641 650_7 $$2NLM Chemicals$$aRecombinant Proteins
000119641 650_7 $$042HK56048U$$2NLM Chemicals$$aTyrosine
000119641 7001_ $$aAndré, Sabine$$b1
000119641 7001_ $$aCañada, F Javier$$b2
000119641 7001_ $$0P:(DE-HGF)0$$aPipkorn, Rüdiger$$b3
000119641 7001_ $$aIppel, Hans$$b4
000119641 7001_ $$aMayo, Kevin H$$b5
000119641 7001_ $$0P:(DE-HGF)0$$aKübler, Dieter$$b6
000119641 7001_ $$aGabius, Hans-Joachim$$b7
000119641 7001_ $$aJiménez-Barbero, Jesús$$b8
000119641 773__ $$0PERI:(DE-600)1461396-7$$a10.1016/j.bbrc.2013.11.063$$gVol. 443, no. 1, p. 126 - 131$$n1$$p126 - 131$$tBiochemical and biophysical research communications$$v443$$x0006-291X$$y2014
000119641 909CO $$ooai:inrepo02.dkfz.de:119641$$pVDB
000119641 9101_ $$0I:(DE-588b)2036810-0$$6P:(DE-HGF)0$$aDeutsches Krebsforschungszentrum$$b3$$kDKFZ
000119641 9101_ $$0I:(DE-588b)2036810-0$$6P:(DE-HGF)0$$aDeutsches Krebsforschungszentrum$$b6$$kDKFZ
000119641 9131_ $$0G:(DE-HGF)POF3-312$$1G:(DE-HGF)POF3-310$$2G:(DE-HGF)POF3-300$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bGesundheit$$lKrebsforschung$$vFunctional and structural genomics$$x0
000119641 9141_ $$y2014
000119641 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz
000119641 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000119641 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000119641 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000119641 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bBIOCHEM BIOPH RES CO : 2015
000119641 915__ $$0StatID:(DE-HGF)0600$$2StatID$$aDBCoverage$$bEbsco Academic Search
000119641 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer Review$$bASC
000119641 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000119641 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000119641 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000119641 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000119641 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000119641 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000119641 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5
000119641 9201_ $$0I:(DE-He78)D015-20160331$$kD015$$lTranslationale Immunologie$$x0
000119641 9201_ $$0I:(DE-He78)A060-20160331$$kA060$$lMechanismen biomolekularer Wechselwirkungen$$x1
000119641 980__ $$ajournal
000119641 980__ $$aVDB
000119641 980__ $$aI:(DE-He78)D015-20160331
000119641 980__ $$aI:(DE-He78)A060-20160331
000119641 980__ $$aUNRESTRICTED