scholarly article | Q13442814 |
P2093 | author name string | José Luis Millán | |
Boguslaw Stec | |||
Anton Cheltsov | |||
P2860 | cites work | A revised mechanism for the alkaline phosphatase reaction involving three metal ions | Q27625079 |
Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity | Q27628998 | ||
The 1.9 A crystal structure of heat-labile shrimp alkaline phosphatase | Q27639246 | ||
Efficient anisotropic refinement of macromolecular structures using FFT | Q27861028 | ||
Features and development of Coot | Q27861079 | ||
The CCP4 suite: programs for protein crystallography | Q27861090 | ||
Function assignment to conserved residues in mammalian alkaline phosphatases | Q34122485 | ||
Structural evidence of functional divergence in human alkaline phosphatases | Q34153784 | ||
Structural studies of human placental alkaline phosphatase in complex with functional ligands. | Q34425176 | ||
Alkaline Phosphatases : Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes | Q34769227 | ||
Molecular mechanism of uncompetitive inhibition of human placental and germ-cell alkaline phosphatase | Q38326693 | ||
Residues determining the binding specificity of uncompetitive inhibitors to tissue-nonspecific alkaline phosphatase | Q45100417 | ||
Mammalian Alkaline Phosphatases | Q57349374 | ||
Mammalian alkaline phosphatases are allosteric enzymes | Q73648552 | ||
P433 | issue | Pt 8 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | biophysics | Q7100 |
condensed matter physics | Q214781 | ||
structural biology | Q908902 | ||
protein interaction domains and motifs | Q70688808 | ||
P304 | page(s) | 866-70 | |
P577 | publication date | 2010-07-27 | |
2010-08-01 | |||
P1433 | published in | Acta Crystallographica Section F: Structural Biology Communications | Q1924863 |
P1476 | title | Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site | |
P478 | volume | 66 |