IndraLab

Statements


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No evidence text available

No evidence text available

sparser
"As USP1's interaction with FANCD2 is dependent on the N-terminus, we wanted to determine whether this is specific for hs FANCD2, so we similarly assayed interactions of hs FANCI and hs PCNA."

reach
"Further experiments showed that USP1 physically interacts with FANCD2 and that the two proteins colocalize in chromatin after DNA damage XREF_BIBR."

sparser
"Furthermore, USP1 physically associates with FANCD2, and the proteins colocalize in chromatin after DNA damage."

No evidence text available

reach
"Furthermore, USP1 physically associates with FANCD2, and the proteins colocalize in chromatin after DNA damage."

reach
"As USP1's interaction with FANCD2 is dependent on the N-terminus, we wanted to determine whether this is specific for hsFANCD2, so we similarly assayed interactions of hsFANCI and hsPCNA."

No evidence text available

sparser
"In addition, USP1 Δ1Δ2 -R22A only partially interacts with hs FANCD2, and USP1 Δ1Δ2 -R22K does not weaken the substrate interaction—both results are consistent with the hs FANCD2-Ub deubiquitination assays ( xref and xref )."

sparser
"Together, these data indicate that the N-terminus of USP1 directly interacts with FANCD2."

sparser
"It is possible that a more specific inhibitor could block FANCD2USP1 interaction, such as the N-terminus, and may provide a more specific therapy."

sparser
"Further experiments showed that USP1 physically interacts with FANCD2 and that the two proteins colocalize in chromatin after DNA damage xref ."

sparser
"The N-terminus of USP1 binds specifically to FANCD2, and not FANCI or PCNA."

reach
"XREF_BIBR, XREF_BIBR USP1 binds to FANCD2 and the inhibition of USP1 leads to the accumulation of monoubiquitylated FANCD2 and mitomycin C hypersensitivity, suggesting that failure to deubiquitylate FANCD2, like impaired ubiquitylation, inhibits its function in repairing DNA interstrand cross-links."

reach
"Like mono-ubiquitylated FANCD2, USP1 levels are regulated during the cell cycle, and USP1 has also been shown to interact directly with FANCD2 and to co-localise with chromatin."

reach
"This inactivation of the pathway occurs when USP1, a de-ubiquitinating enzyme, associates with FANCD2 within the nuclear foci and removes the monoubiquitin moiety [XREF_BIBR]."

reach
"UAF1 SLD2 binds directly to a SIM in FANCI, bridging the interaction between USP1 and UAF1 and FANCD2 and FANCI."

sparser
"This interaction between USP1 and FANCD2 ties the FA pathway to the TLS pathway as USP1 has since been found to also be the DUB for PCNA."

sparser
"These data indicate the USP1 binding to hs FANCD2, which is almost completely dependent on the N-terminus of USP1."