Solution structure of the second DSRM domain in Interferon-induced, double-stranded RNA-activated protein kinase

He, Fangli; Muto, Yuko; Inoue, Masatoshi; Kigawa, T.; Shirouzu, Mikako; Terada, T.; Yokoyama, S.; Initiative, Proteomics

doi:10.2210/pdb1x48/pdb

2005

DOI: 10.2210/pdb1x48/pdb

|View full text |Cite

Solution structure of the second DSRM domain in Interferon-induced, double-stranded RNA-activated protein kinase

Fangli He¹,

Yuko Muto²,

Masatoshi Inoue³

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2016

Publication Types

Select...

Article1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Genome-wide survey of putative RNA-binding proteins encoded in the human proteome

Ghosh

Sowdhamini

2016

Mol. BioSyst.

View full text Add to dashboard Cite

RNA-binding proteins (RBPs) are involved in various post-transcriptional gene regulatory processes and are also functionally important members of the ribosome and the spliceosome. However, RBPs and their interactions with RNA are less well-studied in comparison to DNA-binding proteins. We have classified the existing RBP structures, available in complexes with RNA and RNA/DNA hybrids, into different structural families and created Hidden Markov Models (HMMs). These structure-centric family HMMs, along with the sequence-centric family HMMs, were used as a primary database to systematically search the human proteome for the presence of putative RBPs. We have found more than 2600 gene products with RBP signatures in humans, of which around 28% are likely to bind to RNA but not DNA, whereas 9% might bind to both RNA and DNA. 11% of them do not contain an explicit functional annotation yet. Nearly 30% of the putative RBPs are exclusively nuclear, 15% have known disease associations and around 30% are enzymes. Around 40% of the proteins identified in this study are novel and have not been reported by recent large-scale studies on human RBPs.

show abstract

Genome-wide survey of putative RNA-binding proteins encoded in the human proteome

Ghosh

Sowdhamini

2016

Mol. BioSyst.

View full text Add to dashboard Cite

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Solution structure of the second DSRM domain in Interferon-induced, double-stranded RNA-activated protein kinase

Cited by 1 publication

References 0 publications

Genome-wide survey of putative RNA-binding proteins encoded in the human proteome

Genome-wide survey of putative RNA-binding proteins encoded in the human proteome

Contact Info

Product

Resources

About