| scholarly article | Q13442814 |
| P2093 | author name string | Lewis E Kay | |
| Rafal Augustyniak | |||
| P2860 | cites work | The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system | Q24603386 |
| Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution | Q24649924 | ||
| Prokaryotic ubiquitin-like protein modification | Q26998484 | ||
| Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR | Q27649095 | ||
| A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G | Q27651724 | ||
| A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding | Q27704200 | ||
| Solution structure of calcium-free calmodulin | Q27729471 | ||
| Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution | Q27730197 | ||
| Protein disaggregation mediated by heat-shock protein Hsp104. | Q27940314 | ||
| The ubiquitin-proteasome system | Q28305844 | ||
| Molecular chaperones in protein folding and proteostasis | Q29547715 | ||
| Proteasomes and their kin: proteases in the machine age | Q29614359 | ||
| AAA+ proteins: have engine, will work | Q29617410 | ||
| Molecular chaperones and protein quality control | Q29617795 | ||
| Stepwise unfolding of a β barrel protein by the AAA+ ClpXP protease. | Q30155499 | ||
| Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques | Q30167627 | ||
| Optimal isotope labelling for NMR protein structure determinations. | Q30353197 | ||
| Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E. coli lysate | Q30423139 | ||
| Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine. | Q30473723 | ||
| The role of beta-sheet interactions in domain stability, folding, and target recognition reactions of calmodulin. | Q52553654 | ||
| Mitochondria Unfold Precursor Proteins by Unraveling Them From Their N-termini | Q57851896 | ||
| Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein | Q58037850 | ||
| The structure of apo-calmodulin. A 1H NMR examination of the carboxy-terminal domain | Q72659658 | ||
| The Janus face of the archaeal Cdc48/p97 homologue VAT: protein folding versus unfolding | Q73137131 | ||
| Temperature jump kinetic study of the stability of apo-calmodulin | Q78679350 | ||
| Relaxation rates of degenerate 1H transitions in methyl groups of proteins as reporters of side-chain dynamics | Q83874609 | ||
| Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study | Q30789737 | ||
| Active unfolding of precursor proteins during mitochondrial protein import | Q33887722 | ||
| Ligand binding and thermodynamic stability of a multidomain protein, calmodulin | Q33916867 | ||
| Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY). | Q34063898 | ||
| ClpXP, an ATP-powered unfolding and protein-degradation machine | Q34198403 | ||
| Comparison of the protein-unfolding pathways between mitochondrial protein import and atomic-force microscopy measurements | Q34212599 | ||
| Mechanochemical basis of protein degradation by a double-ring AAA+ machine | Q34308388 | ||
| A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases | Q34552766 | ||
| AAA+ ATPases: achieving diversity of function with conserved machinery | Q34693562 | ||
| Protein unfolding--an important process in vivo? | Q35064539 | ||
| The archaeal proteasome is regulated by a network of AAA ATPases | Q36386004 | ||
| Calcium-dependent folding of single calmodulin molecules | Q36397975 | ||
| Insights into the molecular architecture of the 26S proteasome | Q37274386 | ||
| E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP. | Q37570875 | ||
| Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase | Q37593375 | ||
| Structural biology of the proteasome | Q38081952 | ||
| Cdc48: a swiss army knife of cell biology | Q38156177 | ||
| Bringing dynamic molecular machines into focus by methyl-TROSY NMR. | Q38218233 | ||
| Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models | Q38492496 | ||
| NMR Studies of Large Proteins | Q39448611 | ||
| Multistep protein unfolding during nanopore translocation | Q40120691 | ||
| Chemical shifts as a tool for structure determination | Q40576242 | ||
| Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase. | Q41257359 | ||
| Structure of a AAA+ unfoldase in the process of unfolding substrate. | Q41598312 | ||
| Identification of the Cdc48•20S proteasome as an ancient AAA+ proteolytic machine. | Q41953180 | ||
| Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase. | Q42289897 | ||
| Protein co-translocational unfolding depends on the direction of pulling | Q42878378 | ||
| Effects of local protein stability and the geometric position of the substrate degradation tag on the efficiency of ClpXP denaturation and degradation | Q43015117 | ||
| Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates. | Q43151994 | ||
| Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins | Q43161110 | ||
| Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding | Q43218186 | ||
| ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal | Q43681662 | ||
| Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel | Q44038790 | ||
| ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation | Q44283109 | ||
| Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes | Q44554807 | ||
| Unfolding intermediate of a multidomain protein, calmodulin, in urea as revealed by small-angle X-ray scattering | Q44579152 | ||
| Knots can impair protein degradation by ATP-dependent proteases | Q46163099 | ||
| VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase | Q46763702 | ||
| An isotope labeling strategy for methyl TROSY spectroscopy | Q47228423 | ||
| Mitochondria-targeting sequence, a multi-role sorting sequence recognized at all steps of protein import into mitochondria | Q48034307 | ||
| Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum. | Q48052667 | ||
| Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing. | Q48373223 | ||
| Thermal unfolding simulations of apo-calmodulin using leap-dynamics. | Q52022848 | ||
| P433 | issue | 21 | |
| P304 | page(s) | E4786-E4795 | |
| P577 | publication date | 2018-05-07 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Cotranslocational processing of the protein substrate calmodulin by an AAA+ unfoldase occurs via unfolding and refolding intermediates | |
| P478 | volume | 115 |
| Q92513029 | A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery |
| Q91724058 | An allosteric network in spastin couples multiple activities required for microtubule severing |
| Q64231635 | Structure and mechanism of the ESCRT pathway AAA+ ATPase Vps4 |
| Q83232072 | Structure of Vps4 with circular peptides and implications for translocation of two polypeptide chains by AAA+ ATPases |
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