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1.
Structure of the cell-binding component of the Clostridium difficile binary toxin reveals a di-heptamer macromolecular assembly.
Proc Natl Acad Sci U S A
; 117(2): 1049-1058, 2020 01 14.
Article
in English
| MEDLINE | ID: mdl-31896582
2.
An asymmetry that leads to activity.
Proc Natl Acad Sci U S A
; 116(36): 17614-17615, 2019 09 03.
Article
in English
| MEDLINE | ID: mdl-31427532
3.
Characterizing inhibitors of human AP endonuclease 1.
PLoS One
; 18(1): e0280526, 2023.
Article
in English
| MEDLINE | ID: mdl-36652434
4.
Binding and Functional Folding (BFF): A Physiological Framework for Studying Biomolecular Interactions and Allostery.
J Mol Biol
; 434(23): 167872, 2022 12 15.
Article
in English
| MEDLINE | ID: mdl-36354074
5.
1HN, 13C, and 15N resonance assignments of the Clostridioides difficile receptor binding domain 2 (CDTb, residues 757-876).
Biomol NMR Assign
; 15(1): 35-39, 2021 04.
Article
in English
| MEDLINE | ID: mdl-33034833
6.
1HN, 13C, and 15N backbone resonance assignments of the SET/TAF-1ß/I2PP2A oncoprotein (residues 23-225).
Biomol NMR Assign
; 15(2): 383-387, 2021 10.
Article
in English
| MEDLINE | ID: mdl-34156643
7.
Physiologically Relevant Free Ca2+ Ion Concentrations Regulate STRA6-Calmodulin Complex Formation via the BP2 Region of STRA6.
J Mol Biol
; 433(22): 167272, 2021 11 05.
Article
in English
| MEDLINE | ID: mdl-34592217
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