منابع مشابه
Discovering Domains Mediating Protein Interactions
Background: Protein-protein interactions do not provide any direct information regarding the domains within the proteins that mediate the interactions. The majority of proteins are multi domain proteins and the interaction between them is often defined by the pairs of their domains. Most of the former studies focus only on interacting domain pairs. However they do not consider the in...
متن کاملdiscovering domains mediating protein interactions
background: protein-protein interactions do not provide any direct information regarding the domains within the proteins that mediate the interactions. the majority of proteins are multi domain proteins and the interaction between them is often defined by the pairs of their domains. most of the former studies focus only on interacting domain pairs. however they do not consider the interaction...
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Sales on the Internet have increased significantly during the last decade, and so, it is crucial for companies to retain customers on their web site. Among all strategies towards this goal, providing customers with a flexible search tool is a crucial issue. In this paper, we propose an approach, called TIGER, for handling such flexibility automatically. More precisely, if the search criteria of...
متن کاملUsa1 Protein Facilitates Substrate Ubiquitylation through Two Separate Domains
BACKGROUND Defects in protein folding are recognized as the root of many neurodegenerative disorders. In the endoplasmic reticulum (ER), secretory proteins are subjected to a stringent quality control process to eliminate misfolded proteins by the ER-associated degradation (ERAD) pathway. A novel ERAD component Usa1 was recently identified. However, the specific role of Usa1 in ERAD remains obs...
متن کاملGenerating thermal stable variants of protein domains through phage display.
Often in protein design research, one desires to generate thermally stable variants of a protein or domain. One route to identifying mutations that yield domains that remain folded and active at a higher temperature is through the use of directed evolution. A library of protein domain variants can be generated by mutagenic PCR, expressed on the surface of bacteriophage M13, and subjected to hea...
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ژورنال
عنوان ژورنال: Nature Reviews Molecular Cell Biology
سال: 2018
ISSN: 1471-0072,1471-0080
DOI: 10.1038/s41580-018-0088-9