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Evidence of Rapid Coaggregation of Globular Proteins during Amyloid Formation
Evidence of Rapid Coaggregation of Globular Proteins during Amyloid Formation
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Evidence of Rapid Coaggregation of Globular Proteins during Amyloid Formation

Dubey, Kriti ; Anand, Bibin G ; Temgire, Mayur K ; Kar, Karunakar

Biochemistry (Easton), 2014-12, Vol.53 (51), p.8001-8004 [Periódico revisado por pares]

United States: American Chemical Society

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2
Distance Mapping in Proteins Using Fluorescence Spectroscopy: Tyrosine, like Tryptophan, Quenches Bimane Fluorescence in a Distance-Dependent Manner
Distance Mapping in Proteins Using Fluorescence Spectroscopy: Tyrosine, like Tryptophan, Quenches Bimane Fluorescence in a Distance-Dependent Manner
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Distance Mapping in Proteins Using Fluorescence Spectroscopy: Tyrosine, like Tryptophan, Quenches Bimane Fluorescence in a Distance-Dependent Manner

Jones Brunette, Amber M ; Farrens, David L

Biochemistry (Easton), 2014-10, Vol.53 (40), p.6290-6301 [Periódico revisado por pares]

United States: American Chemical Society

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3
Hypochlorous Acid-Mediated Protein Oxidation:  How Important Are Chloramine Transfer Reactions and Protein Tertiary Structure?
Hypochlorous Acid-Mediated Protein Oxidation:  How Important Are Chloramine Transfer Reactions and Protein Tertiary Structure?
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Hypochlorous Acid-Mediated Protein Oxidation:  How Important Are Chloramine Transfer Reactions and Protein Tertiary Structure?

Pattison, David I ; Hawkins, Clare L ; Davies, Michael J

Biochemistry (Easton), 2007-08, Vol.46 (34), p.9853-9864 [Periódico revisado por pares]

United States: American Chemical Society

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4
Delineation of Solution Burst-Phase Protein Folding Events by Encapsulating the Proteins in Silica Gels
Delineation of Solution Burst-Phase Protein Folding Events by Encapsulating the Proteins in Silica Gels
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Delineation of Solution Burst-Phase Protein Folding Events by Encapsulating the Proteins in Silica Gels

Okabe, Takahiro ; Tsukamoto, Seiichi ; Fujiwara, Kazuo ; Shibayama, Naoya ; Ikeguchi, Masamichi

Biochemistry (Easton), 2014-06, Vol.53 (23), p.3858-3866 [Periódico revisado por pares]

United States: American Chemical Society

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5
Amyloid Protofibril is Highly Voluminous and Compressible
Amyloid Protofibril is Highly Voluminous and Compressible
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Amyloid Protofibril is Highly Voluminous and Compressible

Akasaka, Kazuyuki ; Latif, Abdul Raziq Abdul ; Nakamura, Akihiro ; Matsuo, Koichi ; Tachibana, Hideki ; Gekko, Kunihiko

Biochemistry (Easton), 2007-09, Vol.46 (37), p.10444-10450 [Periódico revisado por pares]

United States: American Chemical Society

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6
Mechanistic Studies of the Folding of Human Lysozyme and the Origin of Amyloidogenic Behavior in Its Disease-Related Variants
Mechanistic Studies of the Folding of Human Lysozyme and the Origin of Amyloidogenic Behavior in Its Disease-Related Variants
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Mechanistic Studies of the Folding of Human Lysozyme and the Origin of Amyloidogenic Behavior in Its Disease-Related Variants

Canet, Denis ; Sunde, Margaret ; Last, Alexander M. ; Miranker, Andrew ; Spencer, Andrew ; Robinson, Carol V. ; Dobson, Christopher M.

Biochemistry (Easton), 1999-05, Vol.38 (20), p.6419-6427 [Periódico revisado por pares]

United States: American Chemical Society

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7
Equilibrium and Kinetics of the Folding and Unfolding of Canine Milk Lysozyme
Equilibrium and Kinetics of the Folding and Unfolding of Canine Milk Lysozyme
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Equilibrium and Kinetics of the Folding and Unfolding of Canine Milk Lysozyme

Nakatani, Hiroyasu ; Maki, Kosuke ; Saeki, Kimiko ; Aizawa, Tomoyasu ; Demura, Makoto ; Kawano, Keiichi ; Tomoda, Shuji ; Kuwajima, Kunihiro

Biochemistry (Easton), 2007-05, Vol.46 (17), p.5238-5251 [Periódico revisado por pares]

United States: American Chemical Society

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8
Improving the Sensitivity and Dynamic Range of Reagentless Fluorescent Immunosensors by Knowledge-Based Design
Improving the Sensitivity and Dynamic Range of Reagentless Fluorescent Immunosensors by Knowledge-Based Design
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Improving the Sensitivity and Dynamic Range of Reagentless Fluorescent Immunosensors by Knowledge-Based Design

Renard, Martial ; Bedouelle, Hugues

Biochemistry (Easton), 2004-12, Vol.43 (49), p.15453-15462 [Periódico revisado por pares]

United States: American Chemical Society

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9
Characterization of Kinetic Folding Intermediates of Recombinant Canine Milk Lysozyme by Stopped-Flow Circular Dichroism
Characterization of Kinetic Folding Intermediates of Recombinant Canine Milk Lysozyme by Stopped-Flow Circular Dichroism
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Characterization of Kinetic Folding Intermediates of Recombinant Canine Milk Lysozyme by Stopped-Flow Circular Dichroism

Nakao, Masaharu ; Maki, Kosuke ; Arai, Munehito ; Koshiba, Takumi ; Nitta, Katsutoshi ; Kuwajima, Kunihiro

Biochemistry (Easton), 2005-05, Vol.44 (17), p.6685-6692 [Periódico revisado por pares]

United States: American Chemical Society

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10
Internal Motion of Lysozyme Studied by Time-Resolved Fluorescence Depolarization of Tryptophan Residues
Internal Motion of Lysozyme Studied by Time-Resolved Fluorescence Depolarization of Tryptophan Residues
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Internal Motion of Lysozyme Studied by Time-Resolved Fluorescence Depolarization of Tryptophan Residues

Nishimoto, Etsuko ; Yamashita, Shoji ; Szabo, Arthur G ; Imoto, Taiji

Biochemistry (Easton), 1998-04, Vol.37 (16), p.5599-5607 [Periódico revisado por pares]

United States: American Chemical Society

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