نتایج جستجو برای: scaffold proteins

تعداد نتایج: 575018  

Journal: :ACS Chemical Biology 2021

Knowledge about interrelationships between different proteins is crucial in fundamental research for the elucidation of protein networks and pathways. Furthermore, it especially critical chemical biology to identify further key regulators a disease take advantage polypharmacology effects. Here, we present new concept that combines scaffold-based analysis bioactivity data with subsequent screeni...

2017
Zhe Feng Anna Caballe Alan Wainman Steven Johnson Andreas F.M. Haensele Matthew A. Cottee Paul T. Conduit Susan M. Lea Jordan W. Raff

In flies, Centrosomin (Cnn) forms a phosphorylation-dependent scaffold that recruits proteins to the mitotic centrosome, but how Cnn assembles into a scaffold is unclear. We show that scaffold assembly requires conserved leucine zipper (LZ) and Cnn-motif 2 (CM2) domains that co-assemble into a 2:2 complex in vitro. We solve the crystal structure of the LZ:CM2 complex, revealing that both protei...

2015
Janna L. Fierst

Modern high-throughput DNA sequencing has made it possible to inexpensively produce genome sequences, but in practice many of these draft genomes are fragmented and incomplete. Genetic linkage maps based on recombination rates between physical markers have been used in biology for over 100 years and a linkage map, when paired with a de novo sequencing project, can resolve mis-assemblies and anc...

Journal: :Journal of Chemical Information and Modeling 2021

Nanodisc technology is increasingly being applied for structural and biophysical studies of membrane proteins. In this work, we present a general protocol constructing molecular models nanodiscs dynamics simulations. The written in python based on geometric equations, making it fast easy to modify, enabling automation customization silico. novelty the ability construct any scaffold protein (MSP...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2012
James J McCann Liqiang Zheng Daniel Rohrbeck Suren Felekyan Ralf Kühnemuth R Bryan Sutton Claus A M Seidel Mark E Bowen

Scaffold proteins form a framework to organize signal transduction by binding multiple partners within a signaling pathway. This shapes the output of signal responses as well as providing specificity and localization. The Membrane Associated Guanylate Kinases (MAGuKs) are scaffold proteins at cellular junctions that localize cell surface receptors and link them to downstream signaling enzymes. ...

2017
Rawin Poonperm Hideaki Takata Susumu Uchiyama Kiichi Fukui

Kinesin family member 4 (KIF4) and condensins I and II are essential chromosomal proteins for chromosome organization by locating primarily to the chromosome scaffold. However, the mechanism of how KIF4 and condensins localize to the chromosome scaffold is poorly understood. Here, we demonstrate a close relationship between the chromosome localization of KIF4 and condensin I, but not condensin ...

2012
Enora Moutin Fabrice Raynaud Jonathan Roger Emilie Pellegrino Vincent Homburger Federica Bertaso Vincent Ollendorff Joël Bockaert Laurent Fagni Julie Perroy

Scaffolding proteins interact with membrane receptors to control signaling pathways and cellular functions. However, the dynamics and specific roles of interactions between different components of scaffold complexes are poorly understood because of the dearth of methods available to monitor binding interactions. Using a unique combination of single-cell bioluminescence resonance energy transfer...

2017
Rebecca Shi Patrick Redman Dipanwita Ghose Yan Liu Xiaobai Ren Lei J Ding Mingna Liu Kendrick J Jones Weifeng Xu

Shank proteins, one of the principal scaffolds in the postsynaptic density (PSD) of the glutamatergic synapses, have been associated with autism spectrum disorders and neuropsychiatric diseases. However, it is not known whether different Shank family proteins have distinct functions in regulating synaptic transmission, and how they differ from other scaffold proteins in this aspect. Here, we in...

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