About: Hiroki Nagai

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

researcher (ORCID 0000-0003-1659-2197)

Attributes	Values
rdf:type	Item
description	forskare (sv) ikertzailea (eu) 연구원 (ko) গবেষক (bn) 研究者 (ja) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) hulumtues (sq) onderzoeker (nl) researcher (ORCID 0000-0003-1659-2197) (en)
exact match	wds:Q38327867-96354541-1989-43B5-AEEE-6D91E5183371
exact match	https://scigraph.springernature.com/person.0667417556.80
rdfs:label	Hiroki Nagai (en) Hiroki Nagai (es) Hiroki Nagai (it) Hiroki Nagai (nl) Hiroki Nagai (sl) Hiroki Nagai (ast)
skos:prefLabel	Hiroki Nagai (en) Hiroki Nagai (es) Hiroki Nagai (it) Hiroki Nagai (nl) Hiroki Nagai (sl) Hiroki Nagai (ast)
name	Hiroki Nagai (en) Hiroki Nagai (es) Hiroki Nagai (it) Hiroki Nagai (nl) Hiroki Nagai (sl) Hiroki Nagai (ast)
Scopus author ID	wds:Q38327867-30E851B9-6311-4B81-A762-F92D3FAADE52
Scopus author ID	7403083866
given name	wds:Q38327867-2F9DB485-248E-49F7-99B7-DE3768F7E306
given name	Hiroki
instance of	wds:Q38327867-BD0AB9F2-D49E-43BE-9D6A-21586448DD29
instance of	Homo sapiens
occupation	wds:Q38327867-E21BD55D-FBD4-4725-9F75-6B285FBAEF4C
employer	wds:Q38327867-46797A0F-F235-40C5-9771-89F1E9085890
sex or gender	wds:Q38327867-573861DC-DBE5-48F3-A318-CA47ED05E183
date of birth	wds:Q38327867-374911E7-CBB3-4E24-9C23-CEC93ED9CE20
family name	wds:Q38327867-8b17cd19-4190-ed77-257f-c500393cecf5
occupation	researcher
employer	Gifu University School of Medicine
sex or gender	male
date of birth	2000-01-01 00:00:00Z (xsd:dateTime)
family name	Nagai
ORCID iD	wds:Q38327867-D06120C4-8945-41B0-8F45-573EDA3C0921
Dimensions author ID	wds:Q38327867-A67A821B-D39F-496E-9F83-56C9B75AB7D4
ORCID iD	https://orcid.org/0000-0003-1659-2197
ORCID iD	0000-0003-1659-2197
Dimensions author ID	0667417556.80
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q38327867
is author of	A C-terminal translocation signal required for Dot/Icm-dependent delivery of the Legionella RalF protein to host cells Systematic sequencing of theEscherichia coligenome: analysis of the 0 – 2.4 min region Show me the substrates: modulation of host cell function by type IV secretion systems. Molecular and structural analysis of Legionella DotI gives insights into an inner membrane complex essential for type IV secretion. Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes Identification of Icm protein complexes that play distinct roles in the biogenesis of an organelle permissive for Legionella pneumophila intracellular growth Native structure of a type IV secretion system core complex essential for Legionella pathogenesis A distinct segment of the sigma 32 polypeptide is involved in DnaK-mediated negative control of the heat shock response in Escherichia coli. Crystal Structure of Legionella DotD: Insights into the Relationship between Type IVB and Type II/III Secretion Systems The structure of RalF, an ADP-ribosylation factor guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site Modulation of the ubiquitination machinery by Legionella. Regions of the Escherichia coli primary sigma factor sigma70 that are involved in interaction with RNA polymerase core enzyme Amoebal endosymbiont Neochlamydia genome sequence illuminates the bacterial role in the defense of the host amoebae against Legionella pneumophila Conformational switching of Escherichia coli RNA polymerase-promoter binary complex is facilitated by elongation factor GreA and GreB. Functional domains of Escherichia coli single-stranded DNA binding protein as assessed by analyses of the deletion mutants. Legionella metaeffector exploits host proteasome to temporally regulate cognate effector. Type IVB Secretion Systems of Legionella and Other Gram-Negative Bacteria. Polymerase arrest at the lambdaP(R) promoter during transcription initiation GroEL is involved in activation of Escherichia coli RNA polymerase devoid of the omega subunit in vivo The machinery at endoplasmic reticulum-plasma membrane contact sites contributes to spatial regulation of multiple Legionella effector proteins The Type IVB secretion system: an enigmatic chimera Bacterial effector-involved temporal and spatial regulation by hijack of the host ubiquitin pathway Bacterial secretion system skews the fate of Legionella-containing vacuoles towards LC3-associated phagocytosis Reduction in abortive transcription from the lambdaPR promoter by mutations in region 3 of the sigma70 subunit of Escherichia coli RNA polymerase Roles and regulation of the heat shock sigma factor sigma 32 in Escherichia coli. Microbially cleaved immunoglobulins are sensed by the innate immune receptor LILRA2 Protochlamydia induces apoptosis of human HEp-2 cells through mitochondrial dysfunction mediated by chlamydial protease-like activity factor Legionella RavZ Plays a Role in Preventing Ubiquitin Recruitment to Bacteria-Containing Vacuoles Subversion of Host Membrane Dynamics by the Legionella Dot/Icm Type IV Secretion System. Acanthamoeba S13WT relies on its bacterial endosymbiont to backpack human pathogenic bacteria and resist Legionella infection on solid media Draft Genome Sequences of Legionella pneumophila JR32 and Lp01 Laboratory Strains Domesticated in Japan Regulation of the heat shock response in E coli: involvement of positive and negative cis-acting elements in translation control of sigma 32 synthesis Amoebal endosymbiont Neochlamydia protects host amoebae against Legionella pneumophila infection by preventing Legionella entry. Emerging insights into bacterial deubiquitinases Identification and functional characterization of K(+) transporters encoded by Legionella pneumophila kup genes. LotA, a Legionella deubiquitinase, has dual catalytic activity and contributes to intracellular growth. Hijacking the Host Proteasome for the Temporal Degradation of Bacterial Effectors
is author of	wds:Q34060526-3895D84D-ED18-4325-95BB-C4AFF4ED785B wds:Q35152952-04C7FE30-A8CC-48BE-AD33-31379A78C584 wds:Q39418282-7EB05CBF-DFBD-46E7-A94A-530C48A4BE26 wds:Q34505503-CD140942-5E14-4A46-BE1F-C1060FF44779 wds:Q35072782-CBF94501-A3E2-434C-A1CC-11DF9ED15699 wds:Q52767597-A41AF0C3-2154-4ABF-A155-A946D3E076FC wds:Q88253175-0A9DB10C-BB81-4CD3-8BF3-5CBFC69F30E5 wds:Q37710890-E3D89D3B-0155-4B5C-A209-A76C3B72EC13

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