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The crystal structure of protein MJ1225 from Methanocaldococcus jannaschii shows strong conservation of key structural features seen in the eukaryal gamma-AMPKStructural basis of regulation and oligomerization of human cystathionine -synthase, the central enzyme of transsulfurationStructural Basis of the Oncogenic Interaction of Phosphatase PRL-1 with the Magnesium Transporter CNNM2.Purification, crystallization and preliminary crystallographic analysis of protein MJ1225 from Methanocaldococcus jannaschii, a putative archaeal homologue of gamma-AMPKStructural insight into the molecular mechanism of allosteric activation of human cystathionine β-synthase by S-adenosylmethioninePurification, crystallization and preliminary crystallographic analysis of human cystathionine β-synthase.Purification, crystallization and preliminary crystallographic analysis of the full-length cystathionine β-synthase from Apis melliferaPurification, crystallization and preliminary crystallographic analysis of the catalytic core of cystathionine β-synthase from Saccharomyces cerevisiae.CBS domains: Ligand binding sites and conformational variability.Purification, crystallization and preliminary crystallographic analysis of the CBS pair of the human metal transporter CNNM4.Purification, crystallization and preliminary crystallographic analysis of the CBS-domain protein MJ1004 from Methanocaldococcus jannaschii.Nucleotide binding triggers a conformational change of the CBS module of the magnesium transporter CNNM2 from a twisted towards a flat structure.Crystal structure of cystathionine β-synthase from honeybee Apis mellifera.Nucleotide-induced conformational transitions in the CBS domain protein MJ0729 of Methanocaldococcus jannaschiiCurrent Structural Knowledge on the CNNM Family of Magnesium Transport MediatorsStructural Insights into the Intracellular Region of the Human Magnesium Transport Mediator CNNM4
P50
Q27660470-B554B122-8301-4C8C-A9CB-EC070204AAC7Q27679976-70938012-DD8D-4E8E-B8D9-9E4D8423E9BDQ30835607-2FBD60B6-20EF-47EA-B87A-37BAB5F3B9F2Q33490081-B283EB33-B64F-42C1-83BB-393BC5063589Q34218322-8D089935-EF7E-4C85-95F2-2AECE0531B76Q36448196-996E9125-77CC-4079-982D-7F3D82ED6F2CQ36448200-886CA68D-3BBB-4EA2-B6AA-30AC18CD4217Q37621407-00BFBB41-60CA-48AC-8CA6-3C338582078FQ38155722-08E6B7C3-C6FE-4E69-9685-B394EFFBC86FQ41777733-B498393E-2954-4478-BC8C-A2A272CBECCAQ42673013-7DB31C83-5AEC-4C49-85D2-F563B2DAA214Q44643323-1DDBB11A-8868-4742-8BC7-1F184F26B834Q49594997-9C987107-77B9-4F9C-A2D1-8E65FFE25F2FQ58323777-7DF05C5B-1852-48F4-B4C0-5960251F4716Q64057201-A81513B0-A54A-4679-87E2-84120C8C52CFQ92013216-2227E469-9C92-49E8-91FA-9493F7C55DEF
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Iker Oyenarte
@ast
Iker Oyenarte
@en
Iker Oyenarte
@es
Iker Oyenarte
@nl
type
label
Iker Oyenarte
@ast
Iker Oyenarte
@en
Iker Oyenarte
@es
Iker Oyenarte
@nl
prefLabel
Iker Oyenarte
@ast
Iker Oyenarte
@en
Iker Oyenarte
@es
Iker Oyenarte
@nl
P106
P108
P1153
32367792600
P31
P496
0000-0002-2870-3344