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An increasing number of disease-associated proteins have been reported to physically associate with the ER-mitochondria interface, and cause structural and/or functional perturbations of this compartment.
In S. pombe, two MAPKAPKs, Srk1 (also known as Mkp1) and Cmk2 (also known as Mkp2), have been reported to physically interact with and be activated via phosphorylation by the Sty1 MAPK (Hog1 homologue) [10], [11].
The Ets transcription factor ELK1 has previously been reported to physically interact with HIF-2α protein, but not HIF-1α protein [13] and to facilitate the activation of CITED2, a gene whose response to hypoxia is primarily mediated by HIF-2α [13].
HOX transcript antisense RNA has been reported to physically associate with PRC2 and to epigenetically regulate multiple target genes.
The TTK protein has been reported to physically interact with TRL proteins and to repress TRL-mediated even-skipped activation [ 20].
p53 and Sp1 families of transcription factors have been reported to physically and functionally interact in the induction of cell-cycle arrest and proapoptotic genes [ 16].
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Human RECQ1 was reported to physically interact with Topo IIIα [14], and Rad51 focus formation after DNA damage is not dependent on RECQ1 in mouse cells [8].
Recently, a GFP-tagged β-Arrestin 2 was reported to physically interact with the WT and a WHIM-associated CXCR4 mutant receptor (CXCR41013), providing evidence that a 15-residue C-terminal truncation of CXCR4 does not prevent β-Arrestin 2 binding to the receptor [31].
Shc was reported to physically interact with SHIP and increase its activity (64).
CCN3 was reported to physically interact with fibulin-1C, integrins, Notch and S100A4.
In an ectopic expression system, Panx1 was reported to physically interact directly with actin [ 6].
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CEO of Professional Science Editing for Scientists @ prosciediting.com