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Listeria monocytogenes internalin B activates junctional endocytosis to accelerate intestinal invasionChemodetection and Destruction of Host Urea Allows Helicobacter pylori to Locate the Epithelium.The adherens junctions control susceptibility to Staphylococcus aureus α-toxinHelicobacter pylori CheZ(HP) and ChePep form a novel chemotaxis-regulatory complex distinct from the core chemotaxis signaling proteins and the flagellar motor.Bone morphogenetic protein 2 induces pulmonary angiogenesis via Wnt-beta-catenin and Wnt-RhoA-Rac1 pathways.Pathobiology of Helicobacter pylori-Induced Gastric Cancer.BMP promotes motility and represses growth of smooth muscle cells by activation of tandem Wnt pathwaysRegulation of Helicobacter pylori Virulence Within the Context of Iron Deficiency.Quantitative Imaging of Gut Microbiota Spatial Organization.Multiple Acid Sensors Control Helicobacter pylori Colonization of the StomachThe basolateral vesicle sorting machinery and basolateral proteins are recruited to the site of enteropathogenic E. coli microcolony growth at the apical membrane.Three-Dimensional Human Skin Models to Understand Staphylococcus aureus Skin Colonization and InfectionThe Use of Short, Animated, Patient-Centered Springboard Videos to Underscore the Clinical Relevance of Preclinical Medical Student Education.Helicobacter pylori Activates and Expands Lgr5(+) Stem Cells Through Direct Colonization of the Gastric Glands.The complete genome sequence of Helicobacter pylori strain G27.A dual function antibiotic-transporter conjugate exhibits superior activity in sterilizing MRSA biofilms and killing persister cellsHigh-resolution mapping reveals that microniches in the gastric glands control Helicobacter pylori colonization of the stomachControlling Epithelial Polarity: A Human Enteroid Model for Host-Pathogen InteractionsShigella navigates tight cornersIdentification of a S. aureus virulence factor by activity-based protein profiling (ABPP)The soluble extracellular domain of E-cadherin interferes with EPEC adherence via interaction with the Tir:intimin complexProfiling of rotavirus 3'UTR-binding proteins reveals the ATP synthase subunit ATP5B as a host factor that supports late-stage virus replicationA Multi-Institution Collaboration to Define Core Content and Design Flexible Curricular Components for a Foundational Medical School Course: Implications for National Curriculum ReformA Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to Promote α-Toxin Cytotoxicity
P50
Q27314798-4EFF2FE4-1BB1-40DA-83D0-A421A661A720Q27318534-469E6822-0E36-4236-8CDC-9A08C828E6ABQ27321037-6A03849D-B3B2-437E-B7A8-ACF2659D06BDQ27347620-87EE3E35-0B25-4966-859E-CD76D008FA8CQ30485381-D211BABE-E67D-4A4F-AFA8-FFCBF8CB3454Q33361550-D7AACFA8-18C0-4A40-BF5F-5F0C9E1F8723Q34483074-2ACB5BA8-E071-4864-A3D2-FB1682384BD8Q35661908-D3482207-9D54-49DC-8A77-7EAD0997FF62Q35800507-9DB4C0E1-EBF4-4A65-A916-81ED76A210A0Q36254144-1F6D2D18-1037-4638-BD89-B357DCC1E066Q36411343-4CBE915D-2C54-4F8A-9DAE-9F7C581A7DB4Q38190950-CF811F78-4849-4A34-9D60-EBD3DBCAABA9Q39000039-92F2201E-5050-4126-A7BB-7129AE98E4C2Q41458995-1962EF6D-62ED-432D-A294-62D990BF55CAQ41863855-C0A9D97D-D836-4B87-B7CD-9FF77240BD71Q58616701-482A817C-C6D4-4FAA-B4C2-0AB38F465BDCQ64071671-6099C014-1E2D-4A87-B673-83123F9D4886Q64099675-A3CE9DE2-FD3E-4B86-95B5-5DE93F7F18EBQ83945157-B93FABDE-7E1C-4032-81B4-94315D9A1FF7Q88702115-AB79FE14-6818-467B-8036-5A789ECE372EQ89151691-6132C00E-3B59-48DB-9841-C1D85E913F45Q91633508-1217E910-BD28-4092-BA17-1F3CAB2CD238Q91881400-D3D04E99-7648-4C19-815F-6E47528FD613Q93274015-4A02DCD6-B870-466B-9E8F-0C5F71346A30
P50
description
researcher ORCID ID = 0000-0002-5601-4490
@en
wetenschapper
@nl
name
Manuel Amieva
@ast
Manuel Amieva
@en
Manuel Amieva
@es
Manuel Amieva
@nl
type
label
Manuel Amieva
@ast
Manuel Amieva
@en
Manuel Amieva
@es
Manuel Amieva
@nl
prefLabel
Manuel Amieva
@ast
Manuel Amieva
@en
Manuel Amieva
@es
Manuel Amieva
@nl
P1053
U-2581-2017
P106
P21
P31
P496
0000-0002-5601-4490