about
Recruitment of Bacillus subtilis RecN to DNA double-strand breaks in the absence of DNA end processingEffect of the BRCA2 CTRD domain on RAD51 filaments analyzed by an ensemble of single molecule techniques.Bacillus subtilis SbcC protein plays an important role in DNA inter-strand cross-link repairRestriction of replication fork regression activities by a conserved SMC complex.Combined optical and topographic imaging reveals different arrangements of human RAD54 with presynaptic and postsynaptic RAD51-DNA filamentsSFMetrics: an analysis tool for scanning force microscopy images of biomolecules.ATPase-dependent control of the Mms21 SUMO ligase during DNA repair.Bacillus subtilis polynucleotide phosphorylase 3'-to-5' DNase activity is involved in DNA repair.Early steps of double-strand break repair in Bacillus subtilis.Taking it one step at a time in homologous recombination repair.Chromosomal transformation in Bacillus subtilis is a non-polar recombination reactionDynamic structures of Bacillus subtilis RecN-DNA complexesMolecular recognition of DNA-protein complexes: a straightforward method combining scanning force and fluorescence microscopy.Protein-DNA interactions in high speed AFM: single molecule diffusion analysis of human RAD54.Targeting the Bacillus subtilis genome: an efficient and clean method for gene disruption.Human RAD50 makes a functional DNA-binding complex.Bacillus subtilis RecG branch migration translocase is required for DNA repair and chromosomal segregationSample preparation for SFM imaging of DNA, proteins, and DNA-protein complexes
P50
Q28488806-35ED7147-B602-4903-8E55-F321239956F9Q30503604-8519117F-5665-4FE7-BE41-4B1B840D979EQ33247050-8C7B0B8D-2AC8-4286-9DCB-167D5358CE5DQ34714389-D3C6A23F-D3D1-4C68-BB17-8DA61C663CA0Q34784344-3AD4BC2B-4EF7-43AB-B78B-11A65FA9C204Q35550400-478B6755-F16C-4912-B435-7B66061BC5FEQ35575863-6D589356-9F6C-4A96-8007-C408DB8E6DD3Q37259085-1E890425-0B42-4BE1-8029-F0014E724435Q38079073-F24C2C98-B20F-4A36-A35D-03EA628DD3F9Q38196596-2F40238A-EB0D-41F6-8A6A-C11BA4BF65CFQ39950708-654FC2AD-54DC-4CB3-A95B-E48B584C3E26Q42153624-BC959D69-78E6-4918-BA26-3EFCC3FE2B8AQ42914518-7F5C9169-963B-4612-A95E-DC2D9EF08018Q50671735-6EF7BEBF-3CD2-40B8-8198-AC31D8E0796AQ52580145-29A11935-C09C-434A-A1A2-0D318A5362D9Q52954655-F6249033-659D-4F4D-B677-753AFA5B2F69Q80639677-0BF8ABC4-D1FB-4D67-B3D6-D1040DDA2E42Q84935876-7236B696-392F-4D1E-9054-34B0FBD0FB63
P50
description
investigador
@es
researcher
@en
wetenschapper
@nl
name
Humberto Sanchez
@en
Humberto Sanchez
@nl
type
label
Humberto Sanchez
@en
Humberto Sanchez
@nl
prefLabel
Humberto Sanchez
@en
Humberto Sanchez
@nl
P31
P496
0000-0003-2137-1233