| P50 | author | Changwen Jin | Q89444375 |
| P2093 | author name string | Fei Xue | |
| | Bin Xia | |
| | Jiaxuan Chen | |
| | Nan Zhong | |
| | Shengnan Zhang | |
| | Xiaobai Ren | |
| | Xue Kang | |
| | Zhiyong Lou | |
| P2860 | cites work | 3D domain swapping: as domains continue to swap | Q24644990 |
| | Polyvalent Interactions in Biological Systems: Implications for Design and Use of Multivalent Ligands and Inhibitors | Q88519588 |
| | Design of wide-spectrum inhibitors targeting coronavirus main proteases | Q24817106 |
| | PROCHECK: a program to check the stereochemical quality of protein structures | Q26778411 |
| | Processing of X-ray diffraction data collected in oscillation mode | Q26778468 |
| | Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain | Q27639290 |
| | Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs | Q27641252 |
| | The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor | Q27642450 |
| | Production of authentic SARS-CoV M(pro) with enhanced activity: application as a novel tag-cleavage endopeptidase for protein overproduction | Q27643422 |
| | Domain-swapped dimerization of the HIV-1 capsid C-terminal domain | Q27644067 |
| | Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations | Q27648944 |
| | Mechanism for Controlling the Dimer-Monomer Switch and Coupling Dimerization to Catalysis of the Severe Acute Respiratory Syndrome Coronavirus 3C-Like Protease | Q27649949 |
| | A structural view of the inactivation of the SARS coronavirus main proteinase by benzotriazole esters | Q27650857 |
| | Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization | Q27652525 |
| | C-terminal domain of sars-CoV main protease can form a 3d domain-swapped dimer | Q27654334 |
| | Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure | Q27655351 |
| | Coot: model-building tools for molecular graphics | Q27860505 |
| | 1H, 13C and 15N chemical shift referencing in biomolecular NMR | Q27860609 |
| | Solvent content of protein crystals | Q27860807 |
| | NMRPipe: a multidimensional spectral processing system based on UNIX pipes | Q27860859 |
| | MOLMOL: a program for display and analysis of macromolecular structures | Q27860873 |
| | Phasercrystallographic software | Q27860930 |
| | NMR View: A computer program for the visualization and analysis of NMR data | Q27860951 |
| | Refinement of macromolecular structures by the maximum-likelihood method | Q27861011 |
| | PHENIX: building new software for automated crystallographic structure determination | Q27861044 |
| | Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage | Q29615331 |
| | Multivalent engagement of chromatin modifications by linked binding modules | Q29617236 |
| | A method for efficient isotopic labeling of recombinant proteins | Q29617364 |
| | Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase | Q34270281 |
| | Proteoglycan control of cell movement during wound healing and cancer spreading | Q34438624 |
| | A novel biological actions acquired by ribonuclease through oligomerization | Q34803286 |
| | Coronavirus in severe acute respiratory syndrome (SARS). | Q35203012 |
| | Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer | Q35994898 |
| | Structural insights into SARS coronavirus proteins | Q36303186 |
| | Characterization and inhibition of SARS-coronavirus main protease | Q36447438 |
| | Drug design targeting the main protease, the Achilles' heel of coronaviruses | Q36683633 |
| | Protein acrobatics in pairs--dimerization via domain swapping | Q37177524 |
| | Without its N-finger, the main protease of severe acute respiratory syndrome coronavirus can form a novel dimer through its C-terminal domain. | Q41780919 |
| | Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode | Q41884048 |
| | Plasminogen activator inhibitor type 1 promotes the self-association of vitronectin into complexes exhibiting altered incorporation into the extracellular matrix | Q43858114 |
| | pH-dependent conformational flexibility of the SARS-CoV main proteinase (M(pro)) dimer: molecular dynamics simulations and multiple X-ray structure analyses | Q43919382 |
| | 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 for design of highly specific protease inhibitors | Q44511959 |
| | Characterization of SARS main protease and inhibitor assay using a fluorogenic substrate | Q44899503 |
| | Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations | Q45126666 |
| | Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease. | Q46438629 |
| | Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide. | Q46747607 |
| | Correlation between dissociation and catalysis of SARS-CoV main protease. | Q46753157 |
| | The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase. | Q46837006 |
| | The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain | Q46944645 |
| | Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome. | Q51660929 |
| | Enzymatic activity of the SARS coronavirus main proteinase dimer. | Q53625273 |
| | A novel coronavirus and SARS | Q73806367 |
| | SARS CoV main proteinase: The monomer-dimer equilibrium dissociation constant | Q79403449 |
| | Only one protomer is active in the dimer of SARS 3C-like proteinase | Q82972241 |
| P433 | issue | 4 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | structural biology | Q908902 |
| | 3C-like proteinase [SARS-Cov] | Q89455671 |
| | SARS-CoV-1 | Q85438966 |
| P304 | page(s) | 371-83 | |
| P577 | publication date | 2010-04-01 | |
| P1433 | published in | Protein & Cell | Q26854012 |
| P1476 | title | Three-dimensional domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main protease | |
| P478 | volume | 1 | |