Real-time heterogeneous protein-protein interaction between αA-crystallin N-terminal mutants and αB-crystallin using quartz crystal microbalance (QCM).

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Real-time heterogeneous protein-protein interaction between αA-crystallin N-terminal mutants and αB-crystallin using quartz crystal microbalance (QCM).

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http://www.wikidata.org/entity/Q53604350

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2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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name

Real-time heterogeneous protei ...... tz crystal microbalance (QCM).

@en

Real-time heterogeneous protei ...... ng quartz crystal microbalance

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type

Item

label

Real-time heterogeneous protei ...... tz crystal microbalance (QCM).

@en

Real-time heterogeneous protei ...... ng quartz crystal microbalance

@nl

prefLabel

Real-time heterogeneous protei ...... tz crystal microbalance (QCM).

@en

Real-time heterogeneous protei ...... ng quartz crystal microbalance

@nl

P1476

Real-time heterogeneous protei ...... tz crystal microbalance (QCM).

@en

P2093

Bency Thankappan

http://www.w3.org/2001/XMLSchema#string

Hiroaki Sakaue

http://www.w3.org/2001/XMLSchema#string

Kalimuthusamy Natarajaseenivasan

http://www.w3.org/2001/XMLSchema#string

Kumarasamy Anbarasu

http://www.w3.org/2001/XMLSchema#string

Norihiko Fujii

http://www.w3.org/2001/XMLSchema#string

Noriko Fujii

http://www.w3.org/2001/XMLSchema#string

Rasiah Pratheepa kumari

http://www.w3.org/2001/XMLSchema#string

Srinivasagan Ramkumar

http://www.w3.org/2001/XMLSchema#string

P2860

Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay

Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q

Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin

Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin

Identification of subunit-subunit interaction sites in αA-WT crystallin and mutant αA-G98R crystallin using isotope-labeled cross-linker and mass spectrometry

Phe71 is essential for chaperone-like function in alpha A-crystallin

Arginine 54 and Tyrosine 118 residues of {alpha}A-crystallin are crucial for lens formation and transparency

Alpha-crystallin can function as a molecular chaperone

A positive charge preservation at position 116 of alpha A-crystallin is critical for its structural and functional integrity.

The R116C mutation in alpha A-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis.

P2888

s00726-015-1935-z

P304

1035-1043

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P31

scholarly article

P356

10.1007/S00726-015-1935-Z

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2015-02-19T00:00:00Z

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P5875

272498976

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P698

25694240

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