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Photoactivatable CaMKII induces synaptic plasticity in single synapses

Nature communications, 2021-02, Vol.12 (1), p.751-751, Article 751

2021

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Chronic neuronal excitation leads to dual metaplasticity in the signaling for structural long-term potentiation

Cell reports (Cambridge), 2022-01, Vol.38 (1), p.110153, Article 110153

2022

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Heat-Induced Aggregation of Hen Ovalbumin Suggests a Key Factor Responsible for Serpin Polymerization

Biochemistry (Easton), 2018-09, Vol.57 (37), p.5415-5426

2018

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Refolding and Polymerization Pathways of Neuroserpin

Journal of molecular biology, 2010-11, Vol.403 (5), p.751-762

2010

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Latent S49P Neuroserpin Forms Polymers in the Dementia Familial Encephalopathy with Neuroserpin Inclusion Bodies

The Journal of biological chemistry, 2005-04, Vol.280 (14), p.13735-13741

2005

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Cleaved Serpin Refolds into the Relaxed State via a Stressed Conformer

The Journal of biological chemistry, 2008-06, Vol.283 (25), p.17568-17578

2008

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Susceptibilities of Phospholipid Membranes Containing Cholesterol or Ergosterol to Gramicidin and its Derivative Incorporated in Lysophospholipid Micelles

Journal of biochemistry (Tokyo), 2008-08, Vol.144 (2), p.167-176

2008

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ShadowR: a novel chromoprotein with reduced non-specific binding and improved expression in living cells

Scientific reports, 2019-08, Vol.9 (1), p.12072-11, Article 12072

2019

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Susceptibilities of Phospholipid Vesicles Containing Different Sterols to Amphotericin B–Loaded Lysophosphatidylcholine Micelles

Journal of biochemistry (Tokyo), 2003-07, Vol.134 (1), p.121-128

2003

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Refolding Mechanism of Ovalbumin

The Journal of biological chemistry, 2003-06, Vol.278 (26), p.23600-23609

2003

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1P076 Preparation of the latent form of pathogenic neuroserpins by refolding on a column.(Protein:Property,The 48th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri, 2010/08/15, Vol.50(supplement2), pp.S32

2010

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1P074 The structure of neuroserpin polymer is different from that proposed by the domain swap model.(Protein:Property,The 48th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri, 2010/08/15, Vol.50(supplement2), pp.S32

2010

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Effect of Aggregation of Amphotericin B on Lysophosphatidylcholine Micelles as Related to Its Complex Formation with Cholesterol or Ergosterol

Journal of biochemistry (Tokyo), 2001-05, Vol.129 (5), p.725-732

2001

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Interaction of Gramicidin with Lysophosphatidylcholine as Revealed by Calorimetry and Fluorescence Spectroscopy

Journal of biochemistry (Tokyo), 2001-11, Vol.130 (5), p.613-620

2001

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The 2.1-Å Crystal Structure of Native Neuroserpin Reveals Unique Structural Elements That Contribute to Conformational Instability

Journal of molecular biology, 2009-04, Vol.388 (1), p.11-20

2009

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2P110 Polymerization and folding of neuroserpin : implication for the conformational disease FENIB(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

Seibutsu Butsuri, 2006/10/01, Vol.46(supplement2), pp.S323

2006

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pH‐dependent stability of neuroserpin is mediated by histidines 119 and 138; Implications for the control of β‐sheet A and polymerization

Protein science, 2010-02, Vol.19 (2), p.220-228

2010

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pH-dependent stability of neuroserpin is mediated by histidines 119 and 138; Implications for the control of [beta]-sheet A and polymerization

Protein science, 2010-02, Vol.19 (2), p.220

2010

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Refolding mechanism of ovalbumin: investigation by using a starting urea-denatured disulfide isomer with mispaired CYS367-CYS382

The Journal of biological chemistry, 2003-06, Vol.278 (26), p.23600-23609

2003

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Refolding Process of Ovalbumin from Urea-denatured State

The Journal of biological chemistry, 1997-02, Vol.272 (7), p.3973-3979

1997

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Thermostability of refolded ovalbumin and S-ovalbumin

Bioscience, biotechnology, and biochemistry, 2005-05, Vol.69 (5), p.922-931

2005

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Refolding process of ovalbumin from urea-denatured state. Evidence for the involvement of nonproductive side chain interactions in an early intermediate

The Journal of biological chemistry, 1997-02, Vol.272 (7), p.3973-3979

1997

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Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB

European journal of biochemistry, 2004-08, Vol.271 (16), p.3360-3367

2004

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Refolding of Urea-Denatured Ovalbumin That Comprises Non-Native Disulfide Isomers

Journal of biochemistry (Tokyo), 1997-07, Vol.122 (1), p.83-89

1997

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Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers

European journal of biochemistry, 2004-08, Vol.271 (16), p.3360-3367

2004

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Photoactivatable CaMKII induces synaptic plasticity in single synapses

Chronic neuronal excitation leads to dual metaplasticity in the signaling for structural long-term potentiation

Heat-Induced Aggregation of Hen Ovalbumin Suggests a Key Factor Responsible for Serpin Polymerization

Refolding and Polymerization Pathways of Neuroserpin

Latent S49P Neuroserpin Forms Polymers in the Dementia Familial Encephalopathy with Neuroserpin Inclusion Bodies

Cleaved Serpin Refolds into the Relaxed State via a Stressed Conformer

Susceptibilities of Phospholipid Membranes Containing Cholesterol or Ergosterol to Gramicidin and its Derivative Incorporated in Lysophospholipid Micelles

ShadowR: a novel chromoprotein with reduced non-specific binding and improved expression in living cells

Susceptibilities of Phospholipid Vesicles Containing Different Sterols to Amphotericin B–Loaded Lysophosphatidylcholine Micelles

Refolding Mechanism of Ovalbumin

1P076 Preparation of the latent form of pathogenic neuroserpins by refolding on a column.(Protein:Property,The 48th Annual Meeting of the Biophysical Society of Japan)

1P074 The structure of neuroserpin polymer is different from that proposed by the domain swap model.(Protein:Property,The 48th Annual Meeting of the Biophysical Society of Japan)

Effect of Aggregation of Amphotericin B on Lysophosphatidylcholine Micelles as Related to Its Complex Formation with Cholesterol or Ergosterol

Interaction of Gramicidin with Lysophosphatidylcholine as Revealed by Calorimetry and Fluorescence Spectroscopy

The 2.1-Å Crystal Structure of Native Neuroserpin Reveals Unique Structural Elements That Contribute to Conformational Instability

2P110 Polymerization and folding of neuroserpin : implication for the conformational disease FENIB(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

pH‐dependent stability of neuroserpin is mediated by histidines 119 and 138; Implications for the control of β‐sheet A and polymerization

pH-dependent stability of neuroserpin is mediated by histidines 119 and 138; Implications for the control of [beta]-sheet A and polymerization

Refolding mechanism of ovalbumin: investigation by using a starting urea-denatured disulfide isomer with mispaired CYS367-CYS382

Refolding Process of Ovalbumin from Urea-denatured State

Thermostability of refolded ovalbumin and S-ovalbumin

Refolding process of ovalbumin from urea-denatured state. Evidence for the involvement of nonproductive side chain interactions in an early intermediate

Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB

Refolding of Urea-Denatured Ovalbumin That Comprises Non-Native Disulfide Isomers

Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers

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