Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein.

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Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein.

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Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein.

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Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein.

@en

Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein.

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Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein.

@en

Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein.

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P1476

Membrane-associated human tyrosinase is an enzymatically active monomeric glycoprotein

@en

P2093

Emilios K Dimitriadis

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Kenneth L Young

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Monika B Dolinska

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Nicole J Kus

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P2860

BRENDA, enzyme data and metabolic information

First structures of an active bacterial tyrosinase reveal copper plasticity

Update on the regulation of mammalian melanocyte function and skin pigmentation

pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus

Oculocutaneous albinism type 1: link between mutations, tyrosinase conformational stability, and enzymatic activity.

BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA.

C-terminus glycans with critical functional role in the maturation of secretory glycoproteins.

Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis.

Albinism-causing mutations in recombinant human tyrosinase alter intrinsic enzymatic activity.

Oculocutaneous albinism type 1: the last 100 years.

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e0198247

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scholarly article

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10.1371/JOURNAL.PONE.0198247

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English

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P478

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P50

P T Wingfield

Yuri V Sergeev

P577

2018-06-05T00:00:00Z

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P698

29870551

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P932

5988326

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