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α-Actinin is an actin binding protein, which forms anti-parallel homodimers and hinges actin filaments into bundles (Sjöblom et al., 2008).
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In the case of PNPase, which is a phosphorolytic RNA-degrading protein found in bacteria and the chloroplasts and mitochondria of some eukaryotic organisms, two RNase PH domains, and both an S1 and KH RNA binding domain are part of a single protein, which forms a trimeric complex that adopts a structure almost identical to that of the exosome.
Compared with the CRD of mannose-binding protein, the CRD of MGL contains an extra glycine-rich loop extending from the surface of the protein, which forms a key part of the galactose-binding site (Kolatkar et al. 1998).
EWS encodes a putative RNA binding protein, which together with TLS/FUS and TAFII68/TAF15 form the TET family of proteins with presumptive roles in transcription and splicing [8].
The L1 ORF1 encodes a 40 kDa RNA binding protein which interacts with the L1 transcript to form a ribonucleoprotein (RNP) particle [22], [23].
A long poly(A) tail is thought to be stimulatory to translation through the binding of cytoplasmic poly(A) binding proteins, which recruit initiation factors and form a closed-loop complex through their association with the translation initiation factor eIF-4G [7].
As adulthood progresses, sex steroid levels decline because of an increase in sex hormone binding proteins, which reduces the concentration of the free form [ 31].
The β sheet forms a binding cleft lined with neutral, nonaromatic residues, unlike most single-stranded DNA binding proteins which use aromatic and charged residues.
Further, during processing of lipoproteins in the liver cells, the natural stereoisomer of α-TOH associates with the highly specific α-TOH-binding protein, which inserts this most active form of VE into nascent very low-density lipoprotein that is, in turn, resecreted into circulation via the hepatic vein (Terasawa et al, 2000).
The guanylate-binding proteins (GBPs) form a group of interferon-γ inducible GTP-binding proteins which belong to the family of dynamin-related proteins.
This Gram-positive bacterium possesses specific surface proteins such as fibronectin-binding proteins, collagen-binding proteins, and fibrinogen-binding proteins, which have been implicated as mediators in specific bacterial binding to the extracellular matrix and subsequent biofilm development [1, 5 7].
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