000			01900 a2200517 4500
005			20250513205031.0
264		0	_c20000502
008			200005s 0 0 eng d
022			_a1072-8368
024	7		_a10.1038/74101 _2doi
040			_aNLM _beng _cNLM
100	1		_aVarani, L
245	0	0	_aThe NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein. _h[electronic resource]
260			_bNature structural biology _cApr 2000
300			_a329-35 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650	0	4	_a3' Untranslated Regions _xchemistry
650	0	4	_aAllosteric Regulation
650	0	4	_aAmino Acid Sequence
650	0	4	_aBase Sequence
650	0	4	_aBinding Sites
650	0	4	_aHumans
650	0	4	_aModels, Molecular
650	0	4	_aMolecular Sequence Data
650	0	4	_aMolecular Weight
650	0	4	_aNuclear Magnetic Resonance, Biomolecular
650	0	4	_aNucleic Acid Conformation
650	0	4	_aPoly A _xmetabolism
650	0	4	_aPolynucleotide Adenylyltransferase _xantagonists & inhibitors
650	0	4	_aProtein Binding
650	0	4	_aProtein Structure, Secondary
650	0	4	_aRNA Processing, Post-Transcriptional _xgenetics
650	0	4	_aRNA, Messenger _xchemistry
650	0	4	_aRNA-Binding Proteins _xchemistry
650	0	4	_aRegulatory Sequences, Nucleic Acid _xgenetics
650	0	4	_aRibonucleoprotein, U1 Small Nuclear _xchemistry
650	0	4	_aStructure-Activity Relationship
650	0	4	_aSubstrate Specificity
700	1		_aGunderson, S I
700	1		_aMattaj, I W
700	1		_aKay, L E
700	1		_aNeuhaus, D
700	1		_aVarani, G
773	0		_tNature structural biology _gvol. 7 _gno. 4 _gp. 329-35
856	4	0	_uhttps://doi.org/10.1038/74101 _zAvailable from publisher's website
999			_c10695613 _d10695613