Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies.
about
Sequence determinants of protein aggregation: tools to increase protein solubility.Protein quantity on the air-solid interface determines degradation rates of human growth hormone in lyophilized samples.Nonnative interactions between cysteines direct productive assembly of P22 tailspike protein.Protein aggregation as bacterial inclusion bodies is reversible.Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation.A Plant-Produced Bacteriophage Tailspike Protein for the Control of Salmonella.Influence of the valine zipper region on the structure and aggregation of the basic leucine zipper (bZIP) domain of activating transcription factor 5 (ATF5).Intermediates and the folding of proteins L and G.Folding and aggregation of designed proteins.The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilizationThe effects of proteoglycan surface patterning on neuronal pathfinding.Cotranslational folding promotes beta-helix formation and avoids aggregation in vivo.The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.Protein aggregation determinants from a simplified model: cooperative folders resist aggregation.Monoclonal antibodies assisting refolding of firefly luciferase.Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike.A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates.Effects of culture temperature and pH on flag-tagged COMP angiopoietin-1 (FCA1) production from recombinant CHO cells: FCA1 aggregation.Homogeneous stalled ribosome nascent chain complexes produced in vivo or in vitro.
P2860
Q24795353-CBD7CDAF-3157-46D3-9E96-D891E39C7AE0Q30360134-44D2A6E1-8123-493A-B903-6EB0F2B05C99Q34183606-62EC7E1F-41AF-489A-9BA1-E6977762FE79Q34513908-110CA195-B83C-4B6B-8CC9-A1BBBED8258DQ36281062-76280646-6EF8-4EEE-9EF7-32BD74715262Q36441987-22D2A839-8124-4211-88FB-962DC83FF1D6Q36502656-D85B44CF-EFED-4DFE-AC99-A24E0DDEB721Q36519494-F2C94DCB-1731-4DE8-BABE-F40E77E3E68CQ36628119-BAC2F802-A71B-43B5-AC7E-00CE0044394AQ36639162-C18CE639-D68C-4AFD-981B-A1268D436AEEQ37684819-4D857004-0937-4AED-B4AA-618A91744B73Q41140712-1AE75CBB-6AAD-4D8A-A786-7A6EE1F4B326Q41881003-0194894F-B041-4563-9ADC-9FA91F7B9BB3Q43093815-5D542297-B08F-4AE2-84F8-38D596CB0E21Q43094972-217C06B0-CD9E-4BF7-BE07-93C93D9DF57DQ43095088-46F80E7D-0B1E-43EC-AEF2-CA22895B9332Q46509993-6EFC1F8E-29B3-453E-B080-AA74DAD88A50Q50115731-FAC95A86-5D5F-4F26-9A48-F0D396287AE6Q51768403-B59782D1-F23B-427B-B66F-17BC38498293Q54478521-C296903E-5D05-4399-9209-015004E34349
P2860
Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Conformation of P22 tailspike ...... obed by monoclonal antibodies.
@ast
Conformation of P22 tailspike ...... obed by monoclonal antibodies.
@en
type
label
Conformation of P22 tailspike ...... obed by monoclonal antibodies.
@ast
Conformation of P22 tailspike ...... obed by monoclonal antibodies.
@en
prefLabel
Conformation of P22 tailspike ...... obed by monoclonal antibodies.
@ast
Conformation of P22 tailspike ...... obed by monoclonal antibodies.
@en
P2093
P2860
P356
P1433
P1476
Conformation of P22 tailspike ...... obed by monoclonal antibodies.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560060111
P577
1997-01-01T00:00:00Z