| scholarly article | Q13442814 |
| P50 | author | Jianxing Song | Q37375660 |
| Jiahai Shi | Q55457251 | ||
| P2093 | author name string | J Sivaraman | |
| P2860 | cites work | Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination | Q26778405 |
| 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 | ||
| Crystal structures reveal an induced-fit binding of a substrate-like Aza-peptide epoxide to SARS coronavirus main peptidase | Q27643459 | ||
| Structures of Two Coronavirus Main Proteases: Implications for Substrate Binding and Antiviral Drug Design | Q27649375 | ||
| Coot: model-building tools for molecular graphics | Q27860505 | ||
| Likelihood-enhanced fast translation functions | Q27860634 | ||
| Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling | Q27860847 | ||
| The CCP4 suite: programs for protein crystallography | Q27861090 | ||
| SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions | Q29615882 | ||
| Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase | Q34270281 | ||
| Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases | Q34340015 | ||
| Reversible unfolding of the severe acute respiratory syndrome coronavirus main protease in guanidinium chloride | Q35613695 | ||
| Long-range cooperative interactions modulate dimerization in SARS 3CLpro. | Q36943869 | ||
| 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 | ||
| Three-dimensional model of a substrate-bound SARS chymotrypsin-like cysteine proteinase predicted by multiple molecular dynamics simulations: catalytic efficiency regulated by substrate binding | Q45250514 | ||
| Mechanism of the maturation process of SARS-CoV 3CL protease | Q46402178 | ||
| Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease. | Q46438629 | ||
| Mutational and inhibitive analysis of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer-based assays | Q46481277 | ||
| Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide. | Q46747607 | ||
| 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 | ||
| Quaternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease | Q47893269 | ||
| Insight into the activity of SARS main protease: Molecular dynamics study of dimeric and monomeric form of enzyme. | Q51109313 | ||
| Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50 | Q78605578 | ||
| SARS CoV main proteinase: The monomer-dimer equilibrium dissociation constant | Q79403449 | ||
| P433 | issue | 9 | |
| P921 | main subject | Coronaviridae | Q1134583 |
| severe acute respiratory syndrome | Q103177 | ||
| P304 | page(s) | 4620-9 | |
| P577 | publication date | 2008-05-01 | |
| P1433 | published in | Journal of Virology | Q1251128 |
| P1476 | title | Mechanism for Controlling the Dimer-Monomer Switch and Coupling Dimerization to Catalysis of the Severe Acute Respiratory Syndrome Coronavirus 3C-Like Protease | |
| P478 | volume | 82 |
| Q47860927 | A monomer-dimer nanoswitch that mimics the working principle of the SARS-CoV 3CLpro enzyme controls copper-catalysed cyclopropanation. |
| Q106873492 | A small molecule compound with an indole moiety inhibits the main protease of SARS-CoV-2 and blocks virus replication |
| Q37870810 | Activation and maturation of SARS-CoV main protease |
| Q50483332 | Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C-like protease (SARS-CoV 3CLpro) from its polyproteins. |
| Q37336376 | Chimeric exchange of coronavirus nsp5 proteases (3CLpro) identifies common and divergent regulatory determinants of protease activity |
| Q36583222 | Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity. |
| Q51555115 | Crystal Dehydration in Membrane Protein Crystallography. |
| Q27651657 | Crystal Structure and NMR Binding Reveal That Two Small Molecule Antagonists Target the High Affinity Ephrin-binding Channel of the EphA4 Receptor |
| Q100728904 | Curcumin Allosterically Inhibits the Dengue NS2B-NS3 Protease by Disrupting Its Active Conformation |
| Q33921124 | Dynamically-driven enhancement of the catalytic machinery of the SARS 3C-like protease by the S284-T285-I286/A mutations on the extra domain |
| Q28477275 | Dynamically-driven inactivation of the catalytic machinery of the SARS 3C-like protease by the N214A mutation on the extra domain |
| Q93135778 | Effector responsive hydroformylation catalysis |
| Q43001880 | Essential covalent linkage between the chymotrypsin-like domain and the extra domain of the SARS-CoV main protease |
| Q98778509 | Feline coronavirus drug inhibits the main protease of SARS-CoV-2 and blocks virus replication |
| Q30995149 | From self-sorted coordination libraries to networking nanoswitches for catalysis. |
| Q91899768 | Heteroleptic copper phenanthroline complexes in motion: From stand-alone devices to multi-component machinery |
| Q92096264 | Identification of Potential Binders of the Main Protease 3CLpro of the COVID-19 via Structure-Based Ligand Design and Molecular Modeling |
| Q41884048 | Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode |
| Q35925764 | Ligand-induced Dimerization of Middle East Respiratory Syndrome (MERS) Coronavirus nsp5 Protease (3CLpro): IMPLICATIONS FOR nsp5 REGULATION AND THE DEVELOPMENT OF ANTIVIRALS. |
| Q34107407 | Maturation mechanism of severe acute respiratory syndrome (SARS) coronavirus 3C-like proteinase. |
| Q27684519 | Mechanism for controlling the monomer-dimer conversion of SARS coronavirus main protease |
| Q111086158 | Modulation of the monomer-dimer equilibrium and catalytic activity of SARS-CoV-2 main protease by a transition-state analog inhibitor |
| Q27660870 | Mutation of Asn28 Disrupts the Dimerization and Enzymatic Activity of SARS 3CL pro |
| Q33767743 | Mutation of Glu-166 blocks the substrate-induced dimerization of SARS coronavirus main protease. |
| Q90166107 | NBCZone: Universal three-dimensional construction of eleven amino acids near the catalytic nucleophile and base in the superfamily of (chymo)trypsin-like serine fold proteases |
| Q38752322 | Recent progress in the discovery of inhibitors targeting coronavirus proteases |
| Q108146965 | Regulation of the Dimerization and Activity of SARS-CoV-2 Main Protease through Reversible Glutathionylation of Cysteine 300 |
| Q37469524 | SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity. |
| Q27704746 | Structural basis for the dimerization and substrate recognition specificity of porcine epidemic diarrhea virus 3C-like protease |
| Q59352622 | Structurally- and dynamically-driven allostery of the chymotrypsin-like proteases of SARS, Dengue and Zika viruses |
| Q36657519 | Structure of Main Protease from Human Coronavirus NL63: Insights for Wide Spectrum Anti-Coronavirus Drug Design |
| Q35592656 | Structures of the Middle East respiratory syndrome coronavirus 3C-like protease reveal insights into substrate specificity |
| Q35943856 | Temperature-sensitive mutants and revertants in the coronavirus nonstructural protein 5 protease (3CLpro) define residues involved in long-distance communication and regulation of protease activity |
| Q27666447 | Three-dimensional domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main protease |
| Q27655351 | Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure |
| Q108146970 | X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease |
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