Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site | Nature Structural & Molecular Biology
Identification of MLH2/hPMS1 dominant mutations that prevent DNA mismatch repair function | Communications Biology
The unstructured linker of Mlh1 contains a motif required for endonuclease function which is mutated in cancers | PNAS
Anti-PMS1 Antibody (A28098) | Antibodies.com
Figure 1 from Dominant Mutations in S. cerevisiae PMS1 Identify the Mlh1- Pms1 Endonuclease Active Site and an Exonuclease 1-Independent Mismatch Repair Pathway | Semantic Scholar
PMS1 Antibody (E-3) | SCBT - Santa Cruz Biotechnology
PMS1 - an overview | ScienceDirect Topics
PMS1 Polyclonal Antibody (PA5-100752)
PMS1 Overexpression Lysate (NBP2-09011): Novus Biologicals
PMS1 Fusion Protein Ag1158 | Proteintech
PMS1 (PMS1 postmeiotic segregation increased 1 (S. cerevisiae))
Mlh2 forms foci that partially colocalize with Pms1.
Dominant Mutations in S. cerevisiae PMS1 Identify the Mlh1-Pms1 Endonuclease Active Site and an Exonuclease 1-Independent Mismatch Repair Pathway | PLOS Genetics
Dominant Mutations in S. cerevisiae PMS1 Identify the Mlh1-Pms1 Endonuclease Active Site and an Exonuclease 1-Independent Mismatch Repair Pathway | PLOS Genetics