Itsuki Anzai
Overview
Explore the profile of Itsuki Anzai including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
18
Citations
193
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
11.
Torii S, Ono C, Suzuki R, Morioka Y, Anzai I, Fauzyah Y, et al.
Cell Rep
. 2021 Apr;
35(3):109014.
PMID: 33838744
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been identified as the causative agent of coronavirus disease 2019 (COVID-19). Although multiple mutations have been observed in SARS-CoV-2, functional analysis of...
12.
Fauzyah Y, Ono C, Torii S, Anzai I, Suzuki R, Izumi T, et al.
Antiviral Res
. 2020 Dec;
186:104999.
PMID: 33346055
The discovery of novel antivirals to treat hepatitis B virus (HBV) infection is urgently needed, as the currently available drugs mainly target viral proteins at replication step, whereas host factors...
13.
Anzai I, Tokuda E, Handa S, Misawa H, Akiyama S, Furukawa Y
Free Radic Biol Med
. 2019 Dec;
147:187-199.
PMID: 31863908
Misfolded Cu/Zn-superoxide dismutase (SOD1) is a pathological species in a subset of amyotrophic lateral sclerosis (ALS). Oxidative stress is known to increase in affected spinal cords of ALS and is...
14.
Tokuda E, Anzai I, Nomura T, Toichi K, Watanabe M, Ohara S, et al.
Mol Neurodegener
. 2017 Jan;
12(1):2.
PMID: 28057013
Background: Dominant mutations in Cu/Zn-superoxide dismutase (SOD1) gene cause a familial form of amyotrophic lateral sclerosis (SOD1-ALS) with accumulation of misfolded SOD1 proteins as intracellular inclusions in spinal motor neurons....
15.
Anzai I, Tokuda E, Mukaiyama A, Akiyama S, Endo F, Yamanaka K, et al.
Protein Sci
. 2016 Dec;
26(3):484-496.
PMID: 27977888
Misfolding of mutant Cu/Zn-superoxide dismutase (SOD1) is a pathological hallmark in a familial form of amyotrophic lateral sclerosis. Pathogenic mutations have been proposed to monomerize SOD1 normally adopting a homodimeric...
16.
Anzai I, Toichi K, Tokuda E, Mukaiyama A, Akiyama S, Furukawa Y
Front Mol Biosci
. 2016 Aug;
3:40.
PMID: 27556028
Dominant mutations in Cu/Zn-superoxide dismutase (SOD1) gene have been shown to cause a familial form of amyotrophic lateral sclerosis (SOD1-ALS). A major pathological hallmark of this disease is abnormal accumulation...
17.
Furukawa Y, Anzai I, Akiyama S, Imai M, Cruz F, Saio T, et al.
J Biol Chem
. 2015 Dec;
291(8):4144-55.
PMID: 26694608
Misfolding of Cu,Zn-superoxide dismutase (SOD1) is a pathological change in the familial form of amyotrophic lateral sclerosis caused by mutations in the SOD1 gene. SOD1 is an enzyme that matures...
18.
Sakurai Y, Anzai I, Furukawa Y
J Biol Chem
. 2014 Jun;
289(29):20139-49.
PMID: 24917671
Enzymatic activation of Cu,Zn-superoxide dismutase (SOD1) requires not only binding of a catalytic copper ion but also formation of an intramolecular disulfide bond. Indeed, the disulfide bond is completely conserved...