Gene Information
Gene symbol: XRCC4
Gene name: X-ray repair complementing defective repair in Chinese hamster cells 4
HGNC ID: 12831
Related Genes
| # | Gene Symbol | Number of hits |
| 1 | LIG4 | 1 hits |
Related Sentences
| # | PMID | Sentence |
| 1 | 9259561 | Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV. |
| 2 | 9705934 | DNA ligase IV binds to XRCC4 via a motif located between rather than within its BRCT domains. |
| 3 | 9705934 | DNA ligase IV binds to XRCC4 via a motif located between rather than within its BRCT domains. |
| 4 | 9705934 | DNA ligase IV binds to XRCC4 via a motif located between rather than within its BRCT domains. |
| 5 | 9705934 | DNA ligase IV binds to XRCC4 via a motif located between rather than within its BRCT domains. |
| 6 | 9705934 | DNA ligase IV binds to XRCC4 via a motif located between rather than within its BRCT domains. |
| 7 | 9705934 | It has recently been demonstrated that DNA ligase IV interacts with and is catalytically stimulated by the XRCC4 protein [2,3], which is essential for DNA double-strand break repair and the genomic rearrangement process of V(D)J recombination [4]. |
| 8 | 9705934 | It has recently been demonstrated that DNA ligase IV interacts with and is catalytically stimulated by the XRCC4 protein [2,3], which is essential for DNA double-strand break repair and the genomic rearrangement process of V(D)J recombination [4]. |
| 9 | 9705934 | It has recently been demonstrated that DNA ligase IV interacts with and is catalytically stimulated by the XRCC4 protein [2,3], which is essential for DNA double-strand break repair and the genomic rearrangement process of V(D)J recombination [4]. |
| 10 | 9705934 | It has recently been demonstrated that DNA ligase IV interacts with and is catalytically stimulated by the XRCC4 protein [2,3], which is essential for DNA double-strand break repair and the genomic rearrangement process of V(D)J recombination [4]. |
| 11 | 9705934 | It has recently been demonstrated that DNA ligase IV interacts with and is catalytically stimulated by the XRCC4 protein [2,3], which is essential for DNA double-strand break repair and the genomic rearrangement process of V(D)J recombination [4]. |
| 12 | 9705934 | DNA ligase IV is characterized by a unique carboxy-terminal tail comprising two BRCT (BRCA1 carboxyl terminus) domains. |
| 13 | 9705934 | DNA ligase IV is characterized by a unique carboxy-terminal tail comprising two BRCT (BRCA1 carboxyl terminus) domains. |
| 14 | 9705934 | DNA ligase IV is characterized by a unique carboxy-terminal tail comprising two BRCT (BRCA1 carboxyl terminus) domains. |
| 15 | 9705934 | DNA ligase IV is characterized by a unique carboxy-terminal tail comprising two BRCT (BRCA1 carboxyl terminus) domains. |
| 16 | 9705934 | DNA ligase IV is characterized by a unique carboxy-terminal tail comprising two BRCT (BRCA1 carboxyl terminus) domains. |
| 17 | 9705934 | It has been suggested that DNA ligase IV associates with XRCC4 via its tandem BRCT domains and that this may be a general model for protein-protein interactions between DNA repair proteins [3]. |
| 18 | 9705934 | It has been suggested that DNA ligase IV associates with XRCC4 via its tandem BRCT domains and that this may be a general model for protein-protein interactions between DNA repair proteins [3]. |
| 19 | 9705934 | It has been suggested that DNA ligase IV associates with XRCC4 via its tandem BRCT domains and that this may be a general model for protein-protein interactions between DNA repair proteins [3]. |
| 20 | 9705934 | It has been suggested that DNA ligase IV associates with XRCC4 via its tandem BRCT domains and that this may be a general model for protein-protein interactions between DNA repair proteins [3]. |
| 21 | 9705934 | It has been suggested that DNA ligase IV associates with XRCC4 via its tandem BRCT domains and that this may be a general model for protein-protein interactions between DNA repair proteins [3]. |
| 22 | 9705934 | We have performed a detailed deletional analysis of DNA ligase IV to define its XRCC4-binding domain and to characterize regions essential for its catalytic activity. |
| 23 | 9705934 | We have performed a detailed deletional analysis of DNA ligase IV to define its XRCC4-binding domain and to characterize regions essential for its catalytic activity. |
| 24 | 9705934 | We have performed a detailed deletional analysis of DNA ligase IV to define its XRCC4-binding domain and to characterize regions essential for its catalytic activity. |
| 25 | 9705934 | We have performed a detailed deletional analysis of DNA ligase IV to define its XRCC4-binding domain and to characterize regions essential for its catalytic activity. |
| 26 | 9705934 | We have performed a detailed deletional analysis of DNA ligase IV to define its XRCC4-binding domain and to characterize regions essential for its catalytic activity. |
| 27 | 9705934 | We find that a region in the carboxy-terminal tail of DNA ligase IV located between rather than within BRCT domains is necessary and sufficient to confer binding to XRCC4. |
| 28 | 9705934 | We find that a region in the carboxy-terminal tail of DNA ligase IV located between rather than within BRCT domains is necessary and sufficient to confer binding to XRCC4. |
| 29 | 9705934 | We find that a region in the carboxy-terminal tail of DNA ligase IV located between rather than within BRCT domains is necessary and sufficient to confer binding to XRCC4. |
| 30 | 9705934 | We find that a region in the carboxy-terminal tail of DNA ligase IV located between rather than within BRCT domains is necessary and sufficient to confer binding to XRCC4. |
| 31 | 9705934 | We find that a region in the carboxy-terminal tail of DNA ligase IV located between rather than within BRCT domains is necessary and sufficient to confer binding to XRCC4. |