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Article

The Na+ binding channel of human coagulation proteases: novel insights on the structure and allosteric modulation revealed by molecular surface analysis.

Biophysical chemistry - 1 Feb 2006

Silva Floriano P, Antunes Octávio A C, de Alencastro Ricardo B, De Simone Salvatore G

Abstract excerpt

Thrombovascular diseases result from imbalanced haemostasis and comprise important health problems in the aging population worldwide. The activity of enzymes pertaining to the coagulation cascade of mammalians exhibit several control mechanisms in order to maintain a proper balance between bleeding and thrombosis. For instance, human coagulation serine proteases carrying a F225 or Y225 are allosteric modulated by...

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Identifiers

PMID: 16288954
DOI: 10.1016/j.bpc.2005.10.001

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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