000 | 02017 a2200541 4500 | ||
---|---|---|---|
005 | 20250516033554.0 | ||
264 | 0 | _c20110715 | |
008 | 201107s 0 0 eng d | ||
022 | _a1091-6490 | ||
024 | 7 |
_a10.1073/pnas.1101262108 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aKochan, Grazyna | |
245 | 0 | 0 |
_aCrystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming. _h[electronic resource] |
260 |
_bProceedings of the National Academy of Sciences of the United States of America _cMay 2011 |
||
300 |
_a7745-50 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 | _aAmino Acid Substitution |
650 | 0 | 4 |
_aAminopeptidases _xchemistry |
650 | 0 | 4 | _aAntigen Presentation |
650 | 0 | 4 |
_aCatalytic Domain _xgenetics |
650 | 0 | 4 | _aCrystallography, X-Ray |
650 | 0 | 4 |
_aHLA-B27 Antigen _xmetabolism |
650 | 0 | 4 | _aHumans |
650 | 0 | 4 | _aMinor Histocompatibility Antigens |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 | _aMutagenesis, Site-Directed |
650 | 0 | 4 | _aPolymorphism, Single Nucleotide |
650 | 0 | 4 | _aProtein Conformation |
650 | 0 | 4 | _aProtein Processing, Post-Translational |
650 | 0 | 4 | _aProtein Structure, Tertiary |
650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
650 | 0 | 4 |
_aSpondylitis, Ankylosing _xenzymology |
700 | 1 | _aKrojer, Tobias | |
700 | 1 | _aHarvey, David | |
700 | 1 | _aFischer, Roman | |
700 | 1 | _aChen, Liye | |
700 | 1 | _aVollmar, Melanie | |
700 | 1 | _avon Delft, Frank | |
700 | 1 | _aKavanagh, Kathryn L | |
700 | 1 | _aBrown, Matthew A | |
700 | 1 | _aBowness, Paul | |
700 | 1 | _aWordsworth, Paul | |
700 | 1 | _aKessler, Benedikt M | |
700 | 1 | _aOppermann, Udo | |
773 | 0 |
_tProceedings of the National Academy of Sciences of the United States of America _gvol. 108 _gno. 19 _gp. 7745-50 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1073/pnas.1101262108 _zAvailable from publisher's website |
999 |
_c20773807 _d20773807 |