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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Trafficking protein particle complex 4

SBD, Synbindin, Trs23
mouse homolog binds syndecan-2 and may play a role in synaptic vesicle transport and dendritic spine formation [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: CAN, HSP70, ACID, SBDS, V1a
Papers on SBD
70-kDa heat shock protein coated magnetic nanocarriers as a nanovaccine for induction of anti-tumor immune response in experimental glioma.
Multhoff et al., Saint Petersburg, Russia. In J Control Release, Jan 2016
We could show that binding activity of Hsp70-SPIONs to the substrate-binding domain (SBD) is highly dependent on the ATPase activity of its nucleotide-binding domain NBD), as shown by (31)P NMR spectroscopy.
Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP.
Liu et al., Richmond, United States. In Structure, Jan 2016
BiP contains two functional domains: a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD).
NMR assignments of the peptidyl-prolyl cis-trans isomerase domain of trigger factor from E. coli.
Hsu et al., Taipei, Taiwan. In Biomol Nmr Assign, Dec 2015
It binds via its ribosome binding domain (RBD) to the ribosomal tunnel exit and facilitates co-translational folding of a broad range of protein substrates primarily through interactions with the substrate binding domain (SBD) adjacent to the RBD.
Pathways of allosteric regulation in Hsp70 chaperones.
Mayer et al., Heidelberg, Germany. In Nat Commun, 2014
Central to the protein folding activity of Hsp70 chaperones is their ability to interact with protein substrates in an ATP-controlled manner, which relies on allosteric regulation between their nucleotide-binding (NBD) and substrate-binding domains (SBD).
Domain Motions and Functionally-Key Residues of l-Alanine Dehydrogenase Revealed by an Elastic Network Model.
Su et al., Qinhuangdao, China. In Int J Mol Sci, 2014
Accompanying the conformational transition, both the 1,4-dihydronicotinamide adenine dinucleotide (NAD)-binding domain (NBD) and the substrate-binding domain (SBD) move in a highly coupled way.
Insights into the molecular mechanism of allostery in Hsp70s.
Kityk et al., Heidelberg, Germany. In Front Mol Biosci, 2014
Key to their versatility is the recognition of a short degenerate sequence motif, present in practically all polypeptides, and a bidirectional allosteric intramolecular regulation mechanism linking their N-terminal nucleotide binding domain (NBD) and their C-terminal polypeptide substrate binding domain (SBD).
Aβ1-25-Derived Sphingolipid-Domain Tracer Peptide SBD Interacts with Membrane Ganglioside Clusters via a Coil-Helix-Coil Motif.
Mu et al., Singapore, Singapore. In Int J Mol Sci, 2014
The Amyloid-β (Aβ)-derived, sphingolipid binding domain (SBD) peptide is a fluorescently tagged probe used to trace the diffusion behavior of sphingolipid-containing microdomains in cell membranes through binding to a constellation of glycosphingolipids, sphingomyelin, and cholesterol.
An update on the recent literature on sickle cell bone disease.
Osunkwo, Atlanta, United States. In Curr Opin Endocrinol Diabetes Obes, 2013
PURPOSE OF REVIEW: To summarize the findings of the recent publications on sickle cell bone disease (SBD).
Hsp70 chaperone dynamics and molecular mechanism.
Mayer, Heidelberg, Germany. In Trends Biochem Sci, 2013
The chaperone functions of heat shock protein (Hsp)70 involve an allosteric control mechanism between the nucleotide-binding domain (NBD) and polypeptide substrate-binding domain (SBD): ATP binding and hydrolysis regulates the affinity for polypeptides, and polypeptide binding accelerates ATP hydrolysis.
An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones.
Gierasch et al., Amherst Center, United States. In Cell, 2013
The allosteric mechanism of Hsp70 molecular chaperones enables ATP binding to the N-terminal nucleotide-binding domain (NBD) to alter substrate affinity to the C-terminal substrate-binding domain (SBD) and substrate binding to enhance ATP hydrolysis.
Effect of early enteral nutrition after hepatectomy in hepatocellular carcinoma patients.
Joh et al., Seoul, South Korea. In Korean J Hepatobiliary Pancreat Surg, 2012
Forty two patients took a sip of water (SOW) at postoperative day (POD)#1, soft blended diet (SBD) at POD#2 (early diet group, ED group), otherwise 60 patients took a SOW at POD#3, SBD at POD#4 (conventional diet group, CD group).
TRAPPC4-ERK2 interaction activates ERK1/2, modulates its nuclear localization and regulates proliferation and apoptosis of colorectal cancer cells.
Fang et al., Shanghai, China. In Plos One, 2010
Data demonstrate that TRAPPC4 may regulate cell proliferation and apoptosis in CRC by interaction with ERK2 and phosphorylating ERK1/2 as well as modulating the subcellular location of pERK1/2 to activate the relevant signaling pathway.
Human Inducible Hsp70: Structures, Dynamics, and Interdomain Communication from All-Atom Molecular Dynamics Simulations.
Ripoll et al., Dijon, France. In J Chem Theory Comput, 2010
Hsp70 is comprised of two main domains: an N-terminal nucleotide binding domain (NBD) and a C-terminal substrate protein binding domain (SBD).
The carbohydrate-binding module family 20--diversity, structure, and function.
Svensson et al., Frederiksberg, Denmark. In Febs J, 2009
Structures of CBM20s, including the first example of a full-length glucoamylase featuring both the catalytic domain and the SBD, are summarized, and distinct architectural and functional features of the two SBDs and roles of pivotal amino acids in binding are described.
Crystal structure of human synbindin reveals two conformations of longin domain.
Gong et al., Hefei, China. In Biochem Biophys Res Commun, 2009
The three-dimensional structure of human synbindin, which contains a longin domain and an atypical PDZ domain is presented.
Inhibitors of Protein Folding: DnaK
Pellecchia et al., Bethesda, United States. In Unknown Journal, 2009
Specifically, these probes would alter DnaK through interactions with its substrate-binding domain (SBD).
Structural basis of Smad2 recognition by the Smad anchor for receptor activation.
Shi et al., Princeton, United States. In Science, 2000
The crystal structure of a Smad2 MH2 domain in complex with the Smad-binding domain (SBD) of SARA has been determined at 2.2 angstrom resolution.
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