000 01679 a2200457 4500
005 20250513105131.0
264 0 _c19970116
008 199701s 0 0 eng d
022 _a0027-8424
024 7 _a10.1073/pnas.93.24.13659
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aZheng, R
245 0 0 _aZinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity.
_h[electronic resource]
260 _bProceedings of the National Academy of Sciences of the United States of America
_cNov 1996
300 _a13659-64 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
650 0 4 _aAmino Acid Sequence
650 0 4 _aApoenzymes
_xchemistry
650 0 4 _aCatalysis
650 0 4 _aCircular Dichroism
650 0 4 _aConserved Sequence
650 0 4 _aCystine
650 0 4 _aDNA, Viral
_xchemistry
650 0 4 _aHIV Integrase
_xchemistry
650 0 4 _aHIV-1
_xenzymology
650 0 4 _aKinetics
650 0 4 _aMacromolecular Substances
650 0 4 _aMutagenesis, Site-Directed
650 0 4 _aOligodeoxyribonucleotides
_xchemistry
650 0 4 _aPoint Mutation
650 0 4 _aProtein Conformation
650 0 4 _aProtein Folding
650 0 4 _aRecombinant Proteins
_xchemistry
650 0 4 _aSpectrophotometry, Atomic
650 0 4 _aSubstrate Specificity
650 0 4 _aZinc
_xanalysis
700 1 _aJenkins, T M
700 1 _aCraigie, R
773 0 _tProceedings of the National Academy of Sciences of the United States of America
_gvol. 93
_gno. 24
_gp. 13659-64
856 4 0 _uhttps://doi.org/10.1073/pnas.93.24.13659
_zAvailable from publisher's website
999 _c8935306
_d8935306