Monoclonal antibody epitope mapping describes tailspike beta-helix folding and aggregation intermediates.

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The C-terminus of the P22 tailspike protein acts as an independent oligomerization domain for monomeric proteins.Cotranslational folding promotes beta-helix formation and avoids aggregation in vivo.Homogeneous stalled ribosome nascent chain complexes produced in vivo or in vitro.

P2860

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P2860

Monoclonal antibody epitope mapping describes tailspike beta-helix folding and aggregation intermediates.

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http://www.wikidata.org/entity/Q50091591

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2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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name

Monoclonal antibody epitope ma ...... and aggregation intermediates.

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Monoclonal antibody epitope ma ...... and aggregation intermediates.

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type

Item

label

Monoclonal antibody epitope ma ...... and aggregation intermediates.

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Monoclonal antibody epitope ma ...... and aggregation intermediates.

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prefLabel

Monoclonal antibody epitope ma ...... and aggregation intermediates.

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Monoclonal antibody epitope ma ...... and aggregation intermediates.

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P1476

Monoclonal antibody epitope ma ...... and aggregation intermediates.

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P2093

Jonathan King

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

Madhulika Jain

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

Michael S Evans

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

P2860

Structure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fab-lysozyme complex

Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage

Molecular chaperones in the cytosol: from nascent chain to folded protein

Protein folding and misfolding

Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike

Folding of newly translated proteins in vivo: the role of molecular chaperones

Multipin peptide libraries for antibody and receptor epitope screening and characterization.

Amyloid fibers are water-filled nanotubes.

Exploring protein-protein interactions with phage display.

BETAWRAP: successful prediction of parallel beta -helices from primary sequence reveals an association with many microbial pathogens

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23032-23040

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scholarly article

P356

10.1074/JBC.M501963200

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English

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280

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Patricia L Clark

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2005-04-14T00:00:00Z

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P698

15833745

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Monoclonal antibody epitope mapping describes tailspike beta-helix folding and aggregation intermediates.

about

P2860

P2860

Monoclonal antibody epitope mapping describes tailspike beta-helix folding and aggregation intermediates.

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P1433

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P2860

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P407

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P478

P50

P577

P698