| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-104 |
Sentence |
denotes |
The structural investigation of glycosaminoglycan binding to CXCL12 displays distinct interaction sites. |
| T1 |
0-104 |
Sentence |
denotes |
The structural investigation of glycosaminoglycan binding to CXCL12 displays distinct interaction sites. |
| TextSentencer_T2 |
105-270 |
Sentence |
denotes |
The stromal cell-derived factor 1α (CXCL12) belongs to the CXC chemokine family and plays an important role in tissue regeneration and the recruitment of stem cells. |
| T2 |
105-270 |
Sentence |
denotes |
The stromal cell-derived factor 1α (CXCL12) belongs to the CXC chemokine family and plays an important role in tissue regeneration and the recruitment of stem cells. |
| TextSentencer_T3 |
271-394 |
Sentence |
denotes |
Here, a stable chemotactic gradient is essential that is formed by the interaction of CXCL12 with the extracellular matrix. |
| T3 |
271-394 |
Sentence |
denotes |
Here, a stable chemotactic gradient is essential that is formed by the interaction of CXCL12 with the extracellular matrix. |
| TextSentencer_T4 |
395-654 |
Sentence |
denotes |
Binding properties of CXCL12 to naturally occurring glycosaminoglycans (GAGs) as well as to the artificial highly sulfated hyaluronic acid (HA) are investigated by using a combination of NMR spectroscopy, molecular modeling and molecular dynamics simulations. |
| T4 |
395-654 |
Sentence |
denotes |
Binding properties of CXCL12 to naturally occurring glycosaminoglycans (GAGs) as well as to the artificial highly sulfated hyaluronic acid (HA) are investigated by using a combination of NMR spectroscopy, molecular modeling and molecular dynamics simulations. |
| TextSentencer_T5 |
655-765 |
Sentence |
denotes |
Our results demonstrate a preferred protein binding for the sulfated GAGs heparin (HE) and highly sulfated HA. |
| T5 |
655-765 |
Sentence |
denotes |
Our results demonstrate a preferred protein binding for the sulfated GAGs heparin (HE) and highly sulfated HA. |
| TextSentencer_T6 |
766-859 |
Sentence |
denotes |
Furthermore, we could demonstrate that the orientation of the sulfate is crucial for binding. |
| T6 |
766-859 |
Sentence |
denotes |
Furthermore, we could demonstrate that the orientation of the sulfate is crucial for binding. |
| TextSentencer_T7 |
860-998 |
Sentence |
denotes |
All sulfated GAGs interact with the CXCL12 GAG-binding motif (K24-H25-L26-K27-R41-K43-R47), where K27 and R41 represent the anchor points. |
| T7 |
860-998 |
Sentence |
denotes |
All sulfated GAGs interact with the CXCL12 GAG-binding motif (K24-H25-L26-K27-R41-K43-R47), where K27 and R41 represent the anchor points. |
| TextSentencer_T8 |
999-1250 |
Sentence |
denotes |
Furthermore, differences could be observed in the second interaction interface of CXCL12: both HE and highly sulfated HA interfere with the receptor-binding motif, while chondroitin sulfate binds different amino acids in close proximity to this motif. |
| T8 |
999-1250 |
Sentence |
denotes |
Furthermore, differences could be observed in the second interaction interface of CXCL12: both HE and highly sulfated HA interfere with the receptor-binding motif, while chondroitin sulfate binds different amino acids in close proximity to this motif. |
| TextSentencer_T9 |
1251-1423 |
Sentence |
denotes |
CXCL12 does not interact with HA, which was directly demonstrated by NMR spectroscopy and molecular modeling and explained by the lack of sulfate groups of the HA molecule. |
| T9 |
1251-1423 |
Sentence |
denotes |
CXCL12 does not interact with HA, which was directly demonstrated by NMR spectroscopy and molecular modeling and explained by the lack of sulfate groups of the HA molecule. |