BindingDB Entry 50046925: Synthesis, experimental evaluation and molecular modelling of hydroxamate derivatives as zinc metalloproteinase inhibitors.

Small molecule binding data for protein ADAM17, Collagenase, Pseudolysin, and Thermolysin, Uniprot P00800, P08253, P14756, P14780, and P78536

Bibliographic Details
Main Author: BindingDB
Format: Dataset
Language:English
Published: BindingDB 2017
Subjects:
ADAM17, Collagenase, Pseudolysin, and Thermolysin, UiT The Arctic University of Norway, Affinity
Arctic
Norway
Arctic University of Norway
UiT The Arctic University of Norway
Online Access:https://dx.doi.org/10.7270/q2ht2r63
https://www.bindingdb.org/entry/50046925
id ftdatacite:10.7270/q2ht2r63
record_format openpolar
spelling ftdatacite:10.7270/q2ht2r63 2023-05-15T18:49:24+02:00 BindingDB Entry 50046925: Synthesis, experimental evaluation and molecular modelling of hydroxamate derivatives as zinc metalloproteinase inhibitors. BindingDB 2017 https://dx.doi.org/10.7270/q2ht2r63 https://www.bindingdb.org/entry/50046925 en eng BindingDB https://www.ebi.ac.uk/chembl/ https://www.ebi.ac.uk/chembl/ https://dx.doi.org/10.1016/j.ejmech.2015.11.019 Attribution 3.0 United States ADAM17, Collagenase, Pseudolysin, and Thermolysin, UiT The Arctic University of Norway, Affinity Protein-ligand binding data dataset Dataset 2017 ftdatacite https://doi.org/10.7270/q2ht2r63 https://doi.org/10.1016/j.ejmech.2015.11.019 2021-11-05T12:55:41Z Small molecule binding data for protein ADAM17, Collagenase, Pseudolysin, and Thermolysin, Uniprot P00800, P08253, P14756, P14780, and P78536 Dataset Arctic University of Norway UiT The Arctic University of Norway DataCite Metadata Store (German National Library of Science and Technology) Arctic Norway
institution Open Polar
collection DataCite Metadata Store (German National Library of Science and Technology)
op_collection_id ftdatacite
language English
topic ADAM17, Collagenase, Pseudolysin, and Thermolysin, UiT The Arctic University of Norway, Affinity
spellingShingle ADAM17, Collagenase, Pseudolysin, and Thermolysin, UiT The Arctic University of Norway, Affinity
BindingDB
BindingDB Entry 50046925: Synthesis, experimental evaluation and molecular modelling of hydroxamate derivatives as zinc metalloproteinase inhibitors.
topic_facet ADAM17, Collagenase, Pseudolysin, and Thermolysin, UiT The Arctic University of Norway, Affinity
description Small molecule binding data for protein ADAM17, Collagenase, Pseudolysin, and Thermolysin, Uniprot P00800, P08253, P14756, P14780, and P78536
format Dataset
author BindingDB
author_facet BindingDB
author_sort BindingDB
title BindingDB Entry 50046925: Synthesis, experimental evaluation and molecular modelling of hydroxamate derivatives as zinc metalloproteinase inhibitors.
title_short BindingDB Entry 50046925: Synthesis, experimental evaluation and molecular modelling of hydroxamate derivatives as zinc metalloproteinase inhibitors.
title_full BindingDB Entry 50046925: Synthesis, experimental evaluation and molecular modelling of hydroxamate derivatives as zinc metalloproteinase inhibitors.
title_fullStr BindingDB Entry 50046925: Synthesis, experimental evaluation and molecular modelling of hydroxamate derivatives as zinc metalloproteinase inhibitors.
title_full_unstemmed BindingDB Entry 50046925: Synthesis, experimental evaluation and molecular modelling of hydroxamate derivatives as zinc metalloproteinase inhibitors.
title_sort bindingdb entry 50046925: synthesis, experimental evaluation and molecular modelling of hydroxamate derivatives as zinc metalloproteinase inhibitors.
publisher BindingDB
publishDate 2017
url https://dx.doi.org/10.7270/q2ht2r63
https://www.bindingdb.org/entry/50046925
geographic Arctic
Norway
geographic_facet Arctic
Norway
genre Arctic University of Norway
UiT The Arctic University of Norway
genre_facet Arctic University of Norway
UiT The Arctic University of Norway
op_relation https://www.ebi.ac.uk/chembl/
https://www.ebi.ac.uk/chembl/
https://dx.doi.org/10.1016/j.ejmech.2015.11.019
op_rights Attribution 3.0 United States
op_doi https://doi.org/10.7270/q2ht2r63
https://doi.org/10.1016/j.ejmech.2015.11.019
_version_ 1766243004943695872

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