about
sameAs
Identification of an amyloid fibril forming peptide comprising residues 46-59 of apolipoprotein A-IEvolution of quaternary structure in a homotetrameric enzymeStructure and evolution of a novel dimeric enzyme from a clinically important bacterial pathogenSubstrate-mediated Stabilization of a Tetrameric Drug Target Reveals Achilles Heel in AnthraxThe structure of human interleukin-11 reveals receptor-binding site features and structural differences from interleukin-6Notch ligand delta-like1: X-ray crystal structure and binding affinityDeterminants of oligosaccharide specificity of the carbohydrate-binding modules of AMP-activated protein kinaseA repeat sequence domain of the ring-exported protein-1 of Plasmodium falciparum controls export machinery architecture and virulence protein traffickingFrom knock-out phenotype to three-dimensional structure of a promising antibiotic target from Streptococcus pneumoniaeSelective inhibition of apicoplast tryptophanyl-tRNA synthetase causes delayed death in Plasmodium falciparumThe crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance.A tetrameric structure is not essential for activity in dihydrodipicolinate synthase (DHDPS) from Mycobacterium tuberculosis.Grappling with anisotropic data, pseudo-merohedral twinning and pseudo-translational noncrystallographic symmetry: a case study involving pyruvate kinase.The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thalianaMethionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I.Phospholipids enhance nucleation but not elongation of apolipoprotein C-II amyloid fibrilsNBD-labeled phospholipid accelerates apolipoprotein C-II amyloid fibril formation but is not incorporated into mature fibrils.An equilibrium model for linear and closed-loop amyloid fibril formation.Simultaneous binding of the anti-cancer IgM monoclonal antibody PAT-SM6 to low density lipoproteins and GRP78Fluphenazine·HCl and Epigallocatechin Gallate Modulate the Rate of Formation and Structural Properties of Apolipoprotein C-II Amyloid Fibrils.Insight into the self-association of key enzymes from pathogenic species.The Role of Lipid in Misfolding and Amyloid Fibril Formation by Apolipoprotein C-II.Biochemical and Structural Insights into Doublecortin-like Kinase Domain 1.Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of N-acetylmannosamine-6-phosphate 2-epimerase from methicillin-resistant Staphylococcus aureusCloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of N-acetylmannosamine kinase from methicillin-resistant Staphylococcus aureus.Phosphorylation of the dimeric cytoplasmic domain of the phytosulfokine receptor, PSKR1.Hydrogen/Deuterium Exchange and Molecular Dynamics Analysis of Amyloid Fibrils Formed by a D69K Charge-Pair Mutant of Human Apolipoprotein C-II.Chameleon 'aggregation-prone' segments of apoA-I: A model of amyloid fibrils formed in apoA-I amyloidosis.Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine.Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of AggregationStructure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association.Exploring the dihydrodipicolinate synthase tetramer: how resilient is the dimer-dimer interface?Lipids enhance apolipoprotein C-II-derived amyloidogenic peptide oligomerization but inhibit fibril formation.Diagnostics for amyloid fibril formation: where to begin?Sedimentation Velocity Analysis of the Size Distribution of Amyloid Oligomers and Fibrils.Phospholipid interaction induces molecular-level polymorphism in apolipoprotein C-II amyloid fibrils via alternative assembly pathways.Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax.Identification of a second binding site on the TRIM25 B30.2 domain.Unravelling the Carbohydrate-Binding Preferences of the Carbohydrate-Binding Modules of AMP-Activated Protein Kinase.Intra- and Intersubunit Ion-Pair Interactions Determine the Ability of Apolipoprotein C-II Mutants To Form Hybrid Amyloid Fibrils.
P50
Q24323500-7177E57A-8C90-408C-83C6-41A0152BC1A8Q27650846-FACF7291-6451-45F1-A736-A297E54F49D9Q27651442-BCB0C413-B66A-46C3-8055-D410EADEB46BQ27658380-092F1A34-C277-4C1D-9F07-158ED8AD7DBBQ27695574-B50FA77C-FB69-4AC0-BA01-E4AB0660685BQ27698064-638A1915-E847-4732-94B8-0B003AFADA14Q27698507-D812CC7D-6E10-41EB-A4AD-646C9899CB63Q27974135-7C012693-5836-4504-A986-D53D756FF32CQ28537699-25A8640A-1871-4FF4-8B88-1BEDF73FD64AQ30043256-A5F5DD33-7192-4F54-9DE4-B16CFFDD74E4Q30351094-49C0B432-2447-4D8A-985D-E6B7E8E9DE0CQ30403842-F5FD015D-BEF4-4D1A-B455-230615B6D45CQ31069962-9AB3787E-7CAF-4DBD-BB0A-8CD1EABEF1EAQ33583391-040A93C0-9D46-4D1D-A87D-ABB9F7770396Q33719586-4CA9DFFE-A03B-4998-86D6-4C7152559CA4Q33918726-508D22F3-A372-4F20-B812-467834BAD72FQ34149504-65BADEEB-B37C-4404-939E-60B5FB0BCCFAQ34149516-0E862847-3BB5-49E6-9716-4FF488904E53Q34688701-D69BE4B8-BA53-45CB-B477-7885D58E8546Q35645408-1B52D1EC-95B3-4637-9FF5-CBD59D639F25Q36175893-D7BCC151-79A3-4387-B608-C784A6C146E9Q38543424-CB6D3E08-212D-4EBA-B8D6-AB401897146AQ38829370-6B515094-1630-42AD-9BAD-E20FC66AA28FQ39194448-1EE577D4-4D4E-499E-BA76-4C6494FB597EQ39194456-BE6027E1-5B55-4212-A8C5-952E64381B29Q39528639-DA47F502-9E01-437A-83F5-8BBC19D94F05Q40713451-3773CD50-87AC-4109-B386-EC6589728F47Q40863460-61E94A9F-256A-449C-93EE-8A8BC29E71D6Q41292352-374105E6-EDBA-4749-8FB0-863915B20703Q42380610-E2102DE9-4978-461C-825D-16E21F23FE64Q42611868-DACD5C8E-E716-414F-9DF6-6D1BAC528AD7Q43240381-67C309C8-6AC2-4EA9-85B1-E2B734C28114Q45963588-A36707E8-B877-463B-ACD8-81F41F4DD3EDQ46323492-690EE757-E359-4816-8749-93BD15DB8D47Q46663031-3670D4C4-337B-4254-9161-CB4548E2A494Q46898280-58DD63DB-30B3-41CC-8852-0576A1C6CA42Q47208042-B6BF3BF9-D774-4D3A-967E-1C834909FBECQ47273478-020C2D5A-8CC6-4A92-B004-7888F4414C1EQ47343320-FA867109-5D4F-4ADC-9E87-B636DE1CEA8BQ48204430-13ABFFA5-B567-470B-A37D-ABCC8DC47EBF
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Griffin MDW
@ast
Griffin MDW
@es
Michael Griffin
@en
Michael Griffin
@nl
type
label
Griffin MDW
@ast
Griffin MDW
@es
Michael Griffin
@en
Michael Griffin
@nl
altLabel
Michael D W Griffin
@en
prefLabel
Griffin MDW
@ast
Griffin MDW
@es
Michael Griffin
@en
Michael Griffin
@nl
P735
P106
P1153
56208125700
P31
P4012
P496
0000-0001-9845-7735