R. Werther

发表

AcrIIA22 is a novel anti-CRISPR that impairs SpyCas9 activity by relieving DNA torsion of target plasmids

B. Stoddard, Kevin J. Forsberg, Harmit S. Malik, 2020 .

Post-translationally Abnormal Collagens of Prolyl 3-Hydroxylase-2 Null Mice Offer a Pathobiological Mechanism for the High Myopia Linked to Human LEPREL1 Mutations*

Brendan H. Lee, D. Eyre, David M. Hudson, 2015, The Journal of Biological Chemistry.

Tuning DNA binding affinity and cleavage specificity of an engineered gene-targeting nuclease via surface display, flow cytometry and cellular analyses

B. Stoddard, A. Lambert, A. Greninger, 2017, Protein engineering, design & selection : PEDS.

Evolutionary Origins of C-Terminal (GPP)n 3-Hydroxyproline Formation in Vertebrate Tendon Collagen

D. Eyre, David M. Hudson, Jiann-Jiu Wu, 2014, PloS one.

Structural studies of blood coagulation factor VIII in complexes with inhibitory antibodies

R. Werther, 2012 .

Structure of the factor VIII C2 domain in a ternary complex with 2 inhibitor antibodies reveals classical and nonclassical epitopes.

Shannon L Meeks, S. Meeks, J. Healey, 2013, Blood.

Characterization and Solution Structure of the Factor VIII C2 Domain in a Ternary Complex with Classical and Non-classical Inhibitor Antibodies*

S. Meeks, J. Healey, P. Lollar, 2013, The Journal of Biological Chemistry.

Crystallographic analyses illustrate significant plasticity and efficient recoding of meganuclease target specificity

M. Pogson, B. Stoddard, A. Lambert, 2017, Nucleic acids research.

The novel anti-CRISPR AcrIIA22 relieves DNA torsion in target plasmids and impairs SpyCas9 activity

B. Stoddard, Kevin J. Forsberg, Harmit S. Malik, 2021, bioRxiv.

Optimization of Protein Thermostability and Exploitation of Recognition Behavior to Engineer Altered Protein-DNA Recognition.

B. Stoddard, A. Lambert, J. Hallinan, 2020, Structure.

Structure, substrate binding and activity of a unique AAA+ protein: the BrxL phage restriction factor

B. Shen, B. Stoddard, L. Doyle, 2023, Nucleic acids research.