Linkers in the structural biology of protein–protein interactions
VP Reddy Chichili, V Kumar, J Sivaraman - Protein science, 2013 - Wiley Online Library
Linkers or spacers are short amino acid sequences created in nature to separate multiple
domains in a single protein. Most of them are rigid and function to prohibit unwanted …
domains in a single protein. Most of them are rigid and function to prohibit unwanted …
A practical overview of protein disorder prediction methods
In the past few years there has been a growing awareness that a large number of proteins
contain long disordered (unstructured) regions that often play a functional role. However …
contain long disordered (unstructured) regions that often play a functional role. However …
Intrinsic disorder in measles virus nucleocapsids
MR Jensen, G Communie… - Proceedings of the …, 2011 - National Acad Sciences
The genome of measles virus is encapsidated by multiple copies of the nucleoprotein (N),
forming helical nucleocapsids of molecular mass approaching 150 Megadalton. The …
forming helical nucleocapsids of molecular mass approaching 150 Megadalton. The …
Near-atomic cryo-EM structure of the helical measles virus nucleocapsid
I Gutsche, A Desfosses, G Effantin, WL Ling, M Haupt… - Science, 2015 - science.org
Measles is a highly contagious human disease. We used cryo–electron microscopy and
single particle–based helical image analysis to determine the structure of the helical …
single particle–based helical image analysis to determine the structure of the helical …
Functional mapping of the nucleoprotein of Ebola virus
S Watanabe, T Noda, Y Kawaoka - Journal of virology, 2006 - Am Soc Microbiol
At 739 amino acids, the nucleoprotein (NP) of Ebola virus is the largest nucleoprotein of the
nonsegmented negative-stranded RNA viruses, and like the NPs of other viruses, it plays a …
nonsegmented negative-stranded RNA viruses, and like the NPs of other viruses, it plays a …
The matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein
M Iwasaki, M Takeda, Y Shirogane, Y Nakatsu… - Journal of …, 2009 - Am Soc Microbiol
The genome of measles virus (MV) is encapsidated by the nucleocapsid (N) protein and
associates with RNA-dependent RNA polymerase to form the ribonucleoprotein complex …
associates with RNA-dependent RNA polymerase to form the ribonucleoprotein complex …
[HTML][HTML] Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation
P Devaux, V von Messling, W Songsungthong… - Virology, 2007 - Elsevier
The measles virus (MV) P gene encodes three proteins: P, an essential polymerase cofactor,
and C and V, which have multiple functions including immune evasion. We show here that …
and C and V, which have multiple functions including immune evasion. We show here that …
The intrinsically disordered C‐terminal domain of the measles virus nucleoprotein interacts with the C‐terminal domain of the phosphoprotein via two distinct sites and …
Measles virus is a negative‐sense, single‐stranded RNA virus within theMononegavirales
order, which includes several human pathogens, including rabies, Ebola, Nipah, and …
order, which includes several human pathogens, including rabies, Ebola, Nipah, and …
Nucleocapsid structure of negative strand RNA virus
M Luo, JR Terrell, SA Mcmanus - Viruses, 2020 - mdpi.com
Negative strand RNA viruses (NSVs) include many important human pathogens, such as
influenza virus, Ebola virus, and rabies virus. One of the unique characteristics that NSVs …
influenza virus, Ebola virus, and rabies virus. One of the unique characteristics that NSVs …
Interaction of the C-terminal domains of sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family
K Houben, D Marion, N Tarbouriech… - Journal of …, 2007 - Am Soc Microbiol
Interaction of the C-terminal domains of Sendai virus (SeV) P and N proteins is crucial for
RNA synthesis by correctly positioning the polymerase complex (L+ P) onto the …
RNA synthesis by correctly positioning the polymerase complex (L+ P) onto the …