期刊论文

Liu, Ke

英文

Methods

1046-2023

2020

175

72-78

10.1016/j.ymeth.2019.07.002

National Natural Science Foundation of ChinaNational Natural Science Foundation of China [31770834, 31300629]; Hubei natural science foundationNatural Science Foundation of Hubei Province [2017CFB513]; U.S. Department of Energy, Office of Biological and Environmental ResearchUnited States Department of Energy (DOE) [DE-AC02-06CH11357]; Canada Foundation for InnovationCanada Foundation for Innovation [1097737]; Eshelman Institute for Innovation [1097737]; AbbVie [1097737]; Bayer Pharma AG [1097737]; Boehringer IngelheimBoehringer Ingelheim [1097737]; Genome Canada through Ontario Genomics InstituteGenome Canada [1097737, OGI-055]; Innovative Medicines Initiative (EU/EFPIA) [ULTRA-DD grant] [1097737, 115766]; JanssenJohnson & Johnson USAJanssen Biotech Inc [1097737]; Merck KGaA, Darmstadt, Germany [1097737]; MSD [1097737]; Ontario Ministry of ResearchMinistry of Research and Innovation, Ontario [1097737]; Novartis Pharma AG [1097737]; Innovation and Science (MRIS) [1097737]; PfizerPfizer [1097737]; Sao Paulo Research Foundation-FAPESPFundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [1097737]; TakedaTakeda Pharmaceutical Company Ltd [1097737]; Wellcome [1097737]

本校为第一且通讯机构

The interaction of Tudor domain-containing proteins (TDRDs) with P-element-induced wimpy testis (PIWI) proteins plays critical roles in transposon silencing and spermatogenesis. Most human TDRDs recognize PIWI proteins in a methylarginine-dependent manner via their extended Tudor (eTudor) domains, except TDRD2, which prefers an unmethylated PIWI protein. In order to illustrate the recognition of unmethylated PIWI proteins by TDRD2, we extensively tried co-crystallization of the TDRD2 eTudor with different PIWIL1 peptides, but to no avail. Recombinant antigen-binding fragments (Fabs) have been ...