scholarly article | Q13442814 |
P356 | DOI | 10.3109/10409238.2014.925421 |
P698 | PubMed publication ID | 24915503 |
P2093 | author name string | Walid A Houry | |
Kaiyin Liu | |||
Adedeji Ologbenla | |||
P2860 | cites work | Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1 | Q27643627 |
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Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism | Q27660298 | ||
Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR | Q27660397 | ||
Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations | Q27663549 | ||
Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP. | Q27664573 | ||
The Clp chaperones and proteases of the human malaria parasite Plasmodium falciparum | Q27664851 | ||
A conformational switch underlies ClpP protease function | Q27667731 | ||
Structural Switching of Staphylococcus aureus Clp Protease: A KEY TO UNDERSTANDING PROTEASE DYNAMICS | Q27673403 | ||
Structural insights into the conformational diversity of ClpP from Bacillus subtilis | Q27675546 | ||
Insights into Structural Network Responsible for Oligomerization and Activity of Bacterial Virulence Regulator Caseinolytic Protease P (ClpP) Protein | Q27676956 | ||
Helix Unfolding/Refolding Characterizes the Functional Dynamics of Staphylococcus aureus Clp Protease | Q27677829 | ||
Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad | Q27678774 | ||
Molecular architecture and assembly of the eukaryotic proteasome | Q27693890 | ||
Crystal structure of heat shock locus V (HslV) from Escherichia coli | Q27738799 | ||
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis | Q27748258 | ||
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ClpP hydrolyzes a protein substrate processively in the absence of the ClpA ATPase: mechanistic studies of ATP-independent proteolysis | Q30848480 | ||
STRAP: editor for STRuctural Alignments of Proteins | Q30986215 | ||
Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase. | Q32063825 | ||
Proteasomes and other self-compartmentalizing proteases in prokaryotes | Q33542295 | ||
Binding of the ClpA unfoldase opens the axial gate of ClpP peptidase | Q33824950 | ||
Local and global mobility in the ClpA AAA+ chaperone detected by cryo-electron microscopy: functional connotations | Q33853445 | ||
The ClpP N-terminus coordinates substrate access with protease active site reactivity | Q34061068 | ||
Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release | Q34133375 | ||
ClpXP, an ATP-powered unfolding and protein-degradation machine | Q34198403 | ||
Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP. | Q34364492 | ||
Paradigms of protein degradation by the proteasome | Q34410240 | ||
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Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli. | Q34728633 | ||
Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. | Q34737150 | ||
The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes | Q35226259 | ||
Prokaryotic proteasomes: nanocompartments of degradation | Q37606186 | ||
Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease | Q40002824 | ||
The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation | Q45258108 | ||
Activators of cylindrical proteases as antimicrobials: identification and development of small molecule activators of ClpP protease | Q47579181 | ||
ClpA and ClpX ATPases bind simultaneously to opposite ends of ClpP peptidase to form active hybrid complexes | Q47904809 | ||
Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms | Q48036866 | ||
Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site. | Q53623920 | ||
Quantitative dynamics and binding studies of the 20S proteasome by NMR | Q59082478 | ||
P433 | issue | 5 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 400-412 | |
P577 | publication date | 2014-06-10 | |
P1433 | published in | Critical Reviews in Biochemistry and Molecular Biology | Q5186661 |
P1476 | title | Dynamics of the ClpP serine protease: a model for self-compartmentalized proteases | |
P478 | volume | 49 |
Q92513029 | A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery |
Q34463606 | AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control |
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Q89983079 | An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR |
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Q91388634 | ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores |
Q93067396 | Consequences of the loss of catalytic triads in chloroplast CLPPR protease core complexes in vivo |
Q48126792 | Discovery of a Unique Clp Component, ClpF, in Chloroplasts: A Proposed Binary ClpF-ClpS1 Adaptor Complex Functions in Substrate Recognition and Delivery |
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Q48194392 | Structures, Functions, and Interactions of ClpT1 and ClpT2 in the Clp Protease System of Arabidopsis Chloroplasts. |
Q36070569 | The Mitochondrial Unfoldase-Peptidase Complex ClpXP Controls Bioenergetics Stress and Metastasis. |
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