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Metal binding affinities of Arabidopsis zinc and copper transporters: selectivities match the relative, but not the absolute, affinities of their amino-terminal domainsMolecular basis of the cooperative binding of Cu(I) and Cu(II) to the CopK protein from Cupriavidus metallidurans CH34The restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonistQuantification of copper binding to amyloid precursor protein domain 2 and its Caenorhabditis elegans ortholog. Implications for biological functionStructural basis of receptor sulfotyrosine recognition by a CC chemokine: the N-terminal region of CCR3 bound to CCL11/eotaxin-1The structural biology of BH3-only proteins.Self-assembled nanomaterials based on beta (β(3)) tetrapeptides.The N-terminal residues 43 to 60 form the interface for dopamine mediated α-synuclein dimerisation.Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax.Human β-defensin 3 contains an oncolytic motif that binds PI(4,5)P2 to mediate tumour cell permeabilisation.Structural biology of the Bcl-2 family and its mimicry by viral proteinsThe Bcl-2 family: structures, interactions and targets for drug discovery.Structural Insight into African Swine Fever Virus A179L-Mediated Inhibition of Apoptosis.The Bcl-2 Family in Host-Virus Interactions.Detection of Bcl-2 family member Bcl-G in mouse tissues using new monoclonal antibodies.Structural insight into an evolutionarily ancient programmed cell death regulator - the crystal structure of marine sponge BHP2 bound to LB-Bak-2.Stabilization of nontoxic Aβ-oligomers: insights into the mechanism of action of hydroxyquinolines in Alzheimer's disease.A structural investigation of NRZ mediated apoptosis regulation in zebrafishThe Bcl-2 Family: Ancient Origins, Conserved Structures, and Divergent MechanismsCrystal Structure of African Swine Fever Virus A179L with the Autophagy Regulator Beclin
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description
investigador
@es
researcher
@en
name
Mark G Hinds
@en
type
label
Mark G Hinds
@en
prefLabel
Mark G Hinds
@en
P31
P496
0000-0002-2856-5375