J
José Luis Millán
Researcher at Sanford-Burnham Institute for Medical Research
Publications - 6
Citations - 804
José Luis Millán is an academic researcher from Sanford-Burnham Institute for Medical Research. The author has contributed to research in topics: Alkaline phosphatase & Phosphatase. The author has an hindex of 6, co-authored 6 publications receiving 705 citations. Previous affiliations of José Luis Millán include Umeå University.
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Journal ArticleDOI
Alkaline Phosphatases : Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes
TL;DR: This mini-review focuses exclusively on structural and functional features of mammalian alkaline phosphatases as identified by crystallography and probed by site-directed mutagenesis and kinetic analysis and their structural andfunctional relatedness to a large superfamily of enzymes that includes nucleotide pyrophosphatase/phosphodiesterase.
Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes
TL;DR: This mini-review focuses exclusively on structural and functional features of mammalian alkaline phosphatases as identified by crystallography and probed by site-directed mutagenesis and kinetic analysis.
Journal ArticleDOI
Structural Studies of Human Placental Alkaline Phosphatase in Complex with Functional Ligands.
Paola Llinas,Enrico A. Stura,André Ménez,Zoltan Kiss,Torgny Stigbrand,José Luis Millán,José Luis Millán,Marie Hélène Le Du +7 more
TL;DR: A comparison of the structures of the other human isozymes and PLAP suggests that the peripheral binding site may be involved in the functional specialization of the PLAP isozyme, and highlights the crucial role played by position 429 at the active site in the modulation of the catalytic process.
Journal ArticleDOI
Catalytic signature of a heat-stable, chimeric human alkaline phosphatase with therapeutic potential
Tina Kiffer-Moreira,Campbell R. Sheen,Kellen Cristina da Silva Gasque,Maytê Bolean,Pietro Ciancaglini,Andrea van Elsas,Marc Hoylaerts,José Luis Millán +7 more
TL;DR: A chimeric enzyme (ChimAP) is generated that retains the structural folding of IAP, but displays greatly increased stability, active site Zn2+ binding, increased transphosphorylation, a higher turnover number and narrower substrate specificity.
Journal ArticleDOI
Functional significance of calcium binding to tissue-nonspecific alkaline phosphatase.
Marc Hoylaerts,Soetkin Van kerckhoven,Tina Kiffer-Moreira,Campbell R. Sheen,Sonoko Narisawa,José Luis Millán +5 more
TL;DR: During skeletal mineralization, the building Ca2+ gradient first activates TNAP, but gradually inactivates it at high Ca2- concentrations, toward completion of mineralization.