[HTML][HTML] Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining …

J Shi, Z Wei, J Song - Journal of Biological Chemistry, 2004 - ASBMB
The severe acute respiratory syndrome (SARS) 3C-like protease consists of two distinct
folds, namely the N-terminal chymotrypsin fold containing the domains I and II hosting the …

[引用][C] Dissection Study on the Severe Acute Respiratory Syndrome 3C-like Protease Reveals the Critical Role of the Extra Domain in Dimerization of the Enzyme

J Shi, Z Wei, J Song - Journal of Biological Chemistry, 2004 - cir.nii.ac.jp
Dissection Study on the Severe Acute Respiratory Syndrome 3C-like Protease Reveals the
Critical Role of the Extra Domain in Dimerization of the Enzyme | CiNii Research CiNii 国立 …

Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme. Defining the …

J Shi, Z Wei, J Song - Journal of Biological Chemistry, 2004 - scholars.cityu.edu.hk
The severe acute respiratory syndrome (SARS) 3C-like protease consists of two distinct
folds, namely the N-terminal chymotrypsin fold containing the domains I and II hosting the …

[HTML][HTML] Dissection Study on the Severe Acute Respiratory Syndrome 3C-like Protease Reveals the Critical Role of the Extra Domain in Dimerization of the Enzyme …

J Shi, Z Wei, J Song - Journal of Biological Chemistry, 2004 - Elsevier
The severe acute respiratory syndrome (SARS) 3C-like protease consists of two distinct
folds, namely the N-terminal chymotrypsin fold containing the domains I and II hosting the …

Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the …

J Shi, Z Wei, J Song - The Journal of biological chemistry, 2004 - pubmed.ncbi.nlm.nih.gov
The severe acute respiratory syndrome (SARS) 3C-like protease consists of two distinct
folds, namely the N-terminal chymotrypsin fold containing the domains I and II hosting the …

Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the …

J Shi, Z Wei, J Song - The Journal of Biological Chemistry, 2004 - europepmc.org
The severe acute respiratory syndrome (SARS) 3C-like protease consists of two distinct
folds, namely the N-terminal chymotrypsin fold containing the domains I and II hosting the …

Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme. Defining the …

J Song, J Shi, Z Wei - 2004 - scholarbank.nus.edu.sg
Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical
role of the extra domain in dimerization of the enzyme. Defining the extra domain as a new target …

[HTML][HTML] Dissection Study on the Severe Acute Respiratory Syndrome 3C-like Protease Reveals the Critical Role of the Extra Domain in Dimerization of the Enzyme …

J Shi, Z Wei, J Song - The Journal of Biological Chemistry, 2004 - ncbi.nlm.nih.gov
The severe acute respiratory syndrome (SARS) 3C-like protease consists of two distinct
folds, namely the N-terminal chymotrypsin fold containing the domains I and II hosting the …

[引用][C] Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining …

J SHI - J. Biol. Chem., 2004 - cir.nii.ac.jp
Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical
role of the extra domain in dimerization of the enzyme : defining the extra domain as a new …

[引用][C] Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme. Defining …

J SHI, Z WEI, J SONG - The Journal of …, 2004 - American Society for Biochemistry …