Yoshinori Akiyama

ORCID: 0000-0003-4483-5408
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About
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Research Areas
  • Bacterial Genetics and Biotechnology
  • RNA and protein synthesis mechanisms
  • Cerebrovascular and Carotid Artery Diseases
  • Intracranial Aneurysms: Treatment and Complications
  • Protein Structure and Dynamics
  • Acute Ischemic Stroke Management
  • Enzyme Structure and Function
  • Endoplasmic Reticulum Stress and Disease
  • Cellular transport and secretion
  • Bacteriophages and microbial interactions
  • Optical Network Technologies
  • Lipid Membrane Structure and Behavior
  • Vascular Malformations Diagnosis and Treatment
  • Glycosylation and Glycoproteins Research
  • Neuroscience and Neuropharmacology Research
  • Moyamoya disease diagnosis and treatment
  • Photonic and Optical Devices
  • Advanced Photonic Communication Systems
  • Biochemical and Molecular Research
  • Heat shock proteins research
  • Traumatic Brain Injury and Neurovascular Disturbances
  • Neurosurgical Procedures and Complications
  • Enzyme Production and Characterization
  • Peptidase Inhibition and Analysis
  • Escherichia coli research studies

Kyoto University
2016-2025

Shizuoka City Shimizu Hospital
2025

Tenri Hospital
2009-2024

Saitama University
2024

International Rescue System
2022

Life Science Institute
2017

Baruch S. Blumberg Institute
2016

Yoshino Kogyosho (Japan)
2014-2015

Saitama Medical University
2009

Tokyo Institute of Technology
2009

Background and Purpose— About one half of those who develop adult-onset moyamoya disease experience intracranial hemorrhage. Despite the extremely high frequency rebleeding attacks poor prognosis, measures to prevent have not been established. The purpose this study is determine whether extracranial–intracranial bypass can reduce incidence improve patient prognosis. Methods— This was a multicentered, prospective, randomized, controlled trial conducted by 22 institutes in Japan. Adult...

10.1161/strokeaha.113.004386 article EN Stroke 2014-03-26

Escherichia coli YaeL (EcfE) is a homolog of human site-2 protease (S2P), membrane-bound zinc metalloprotease involved in regulated intramembrane proteolysis. We have shown previously that YaeL, having essential active site motifs the cytoplasmic domain, indispensable for viability. Here, we obtained rpoE , encoding an extracytoplasmic stress response ς factor (ς E ), as multicopy suppressor against yaeL disruption. Whereas thought to be activated by cleavage RseA on periplasmic side DegS...

10.1101/gad.1002302 article EN Genes & Development 2002-08-15

Background and Purpose— The primary results of the Japan Adult Moyamoya Trial revealed statistically marginal superiority bypass surgery over medical treatment alone in preventing rebleeding moyamoya disease. purpose this analysis is to test prespecified subgroup hypothesis that natural course surgical effects vary depending on hemorrhagic site at onset. Methods— site, classified as either anterior or posterior, was only stratifying variable for randomization. Statistical analyses were...

10.1161/strokeaha.115.010819 article EN Stroke 2015-12-09

Endovascular therapy (EVT) has been found to reduce functional disability in patients with acute stroke due large-vessel occlusion. However, the extent of ischemic region, measured using Alberta Stroke Program Early Computed Tomography Scores, may limit efficacy EVT.To compare and safety EVT according ASPECTS 3 or less vs 4 5.The Recovery by Salvage for Cerebral Ultra-acute Embolism-Japan Large Ischemic Core Trial (RESCUE-Japan LIMIT) was an open-label randomized clinical trial conducted...

10.1001/jamaneurol.2022.3285 article EN JAMA Neurology 2022-10-10

The membrane-bound AAA protease FtsH is the key player controlling protein quality in bacteria. Two single-pass membrane proteins, HflK and HflC, interact with to modulate its proteolytic activity. Here, we present structure of entire FtsH-HflKC complex, comprising 12 copies both all which reciprocally form a cage, as well four hexamers periplasmic domains transmembrane helices enclosed inside cage cytoplasmic situated at base cage. K61/D62/S63 β2-β3 loop domain directly HflK, contributing...

10.1016/j.celrep.2022.110890 article EN cc-by-nc-nd Cell Reports 2022-05-01

The FtsH protein is a membrane-bound ATPase of Escherichia coli that was proposed to be involved in membrane assembly as well degradation some unstable proteins. SecY, subunit translocase, dependently degraded vivo when it fails associate with its partner (the SecE protein). We constructed series mutants which mutations were introduced into conserved residues the two ATP binding consensus sequences or zinc sequence FtsH. purified wild-type and mutant proteins by making use polyhistidine tag...

10.1074/jbc.271.49.31196 article EN cc-by Journal of Biological Chemistry 1996-12-01

It was shown previously that the Escherichia coli gene ppfA (dsbA) encodes a periplasmic protein, and its inactivation leads to deficiency in disulfide bond formation of envelope proteins (Kamitani, S., Aki-

10.1016/s0021-9258(18)41691-2 article EN cc-by Journal of Biological Chemistry 1992-11-01

Escherichia coli FtsH is a membrane‐bound ATPase with proteolytic activity against the SecY subunit of protein translocase. We now report that membrane‐embedded F 0 part H + ‐ATPase another substrate FtsH. Pulse‐chase experiments showed unstable when it alone (without subunits b and c ) was oversynthesized stabilized in ftsH mutants. Selective ATP‐dependent degradation by purified demonstrated vitro. These results suggest serves as quality‐control mechanism to avoid potentially harmful...

10.1016/s0014-5793(96)01283-5 article EN FEBS Letters 1996-12-09

Significance Outer membrane proteins (OMPs) are involved in important cellular activities Gram-negative bacteria. Although the bepA (formerly yfgC ) gene encoding a putative metalloprotease has been implicated quality control of OMPs, its specific function remains unclear. This study reveals that BepA promotes assembly LptD, an OMP transport lipopolysaccharides, which undergoes intramolecular disulfide rearrangement during biogenesis. also degradation incorrectly folded LptD. BamA, another...

10.1073/pnas.1312012110 article EN Proceedings of the National Academy of Sciences 2013-09-03

Significance Bacteria living in seawater must cope with low-sodium environments that they may encounter. Here we show an unexpected finding remodeling of the Sec protein export machinery plays a pivotal role this adaptation. Vibrio alginolyticus possesses alternative SecDF1 and SecDF2 homologs use transmembrane gradient Na + H , respectively, to enhance by cooperating SecYEG translocon. The synthesis is induced low-Na environments, induction essential for bacterium survive low salinity....

10.1073/pnas.1513001112 article EN Proceedings of the National Academy of Sciences 2015-09-21

Abstract Background: The abnormal accumulation of misfolded proteins outside the plasma (cytoplasmic or inner) membrane up‐regulates synthesis a class envelope‐localized catalysts protein folding and degradation. pathway for this transmembrane signalling is mediated by CpxR‐CpxA two‐component phospho‐relay mechanism. Results: We now show that an abnormality in proteins, due either to impairment FtsH, protease acting against integral overproduction substrate activates stress response pathway....

10.1046/j.1365-2443.2002.00554.x article EN Genes to Cells 2002-06-25

The refolding of the tetrameric enzyme tryptophanase was facilitated by chaperonin GroE. Maximum yield molecules (about 80%) attained in presence a 15-fold excess GroE 21-mer over monomer. GroEL subunit required for this improvement yield, whereas GroES not. Light scattering experiments reaction revealed that bound to folding intermediates and suppressed their aggregation. ATP efficient dissociation from GroEL. However, our indicated dissociated readily not only ATP, but also...

10.1016/s0021-9258(19)37111-x article EN cc-by Journal of Biological Chemistry 1992-09-01

The cII gene product of bacteriophage λ is unstable and required for the establishment lysogenization. Its intracellular amount important decision between lytic growth Two genetic loci Escherichia coli are crucial these commitments infecting genome. One them, hflA encodes HflKC membrane protein complex, which has been believed to be a protease degrading protein. However, both its absence overproduction stabilized in vivo proposed serine protease-like sequence motif HflC was dispensable...

10.1073/pnas.94.11.5544 article EN Proceedings of the National Academy of Sciences 1997-05-27

Escherichia coli HtpX is a putative membrane-bound zinc metalloprotease that has been suggested to participate in the proteolytic quality control of membrane proteins conjunction with FtsH, and ATP-dependent protease. Here, we biochemically characterized confirmed its activities against soluble proteins. underwent self-degradation upon cell disruption or solubilization. Consequently, purified under denaturing conditions then refolded it presence chelator. When supplemented Zn2+, enzyme...

10.1074/jbc.m506180200 article EN cc-by Journal of Biological Chemistry 2005-08-03

Mutations which cause poor growth at a low temperature, affect aspects of protein secretion, and map in or around secY (prlA) were characterized. The prlA1012 mutant, previously shown to suppress secA mutation, proved have wild-type gene, indicating that this mutation cannot be taken as genetic evidence for the secA-secY interaction. Two cold-sensitive mutants, secY39 secY40 had been selected by their ability enhance expression, contained single-amino-acid alterations same cytoplasmic domain...

10.1128/jb.172.12.7005-7010.1990 article EN Journal of Bacteriology 1990-12-01

✓ Eleven cases of moyamoya disease refractory to indirect non-anastomotic revascularization, including encephalomyosynangiosis in two, encephaloduroarteriosynangiosis seven, and encephalomyoarteriosynangiosis are described. The patients suffered from recurrent cerebral ischemic symptoms, further operative intervention, superficial temporal artery-middle artery anastomosis intracranial omental transplantation, was performed. choice maneuver depended on the availability scalp arteries nature...

10.3171/jns.1988.68.4.0537 article EN Journal of neurosurgery 1988-04-01
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