P. Bayley

Publications165
h-index39
Citations5,215
Highly Influential Citations113
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Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion.
TLDR
CD, electron microscopic, and sedimentation analyses show that bromelain-solubilized hemagglutinin (BHA) aggregates as protein-protein rosettes and acquires the ability to bind both lipid vesicles and nonionic detergent. Expand
The crystal structure of the globular domain of sheep prion protein.
TLDR
Analysis of the sheep PrP structure identifies two possible loci for the initiation of beta-sheet mediated polymerisation that provide sites within the PrPc monomer that could readily give rise to early intermediate species on the pathway to the formation of aggregated PrPSc containing additional intermolecular beta-structure. Expand
Ligand binding and thermodynamic stability of a multidomain protein, calmodulin
TLDR
The greater affinity of the C‐domain for Ca2+ causes it to be more stable than the N‐domain at [Ca2+] ≤0.3 mM, consistent with measured Mg2+ affinities. Expand
Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences
TLDR
The interaction of calmodulin with the M13 sequence can be dissected on both a structural and kinetic basis into partial reactions involving intermediates comprising distinct regions of the target sequence, and a general mechanism for the calcium regulation of cal modulin‐dependent enzyme activation is proposed. Expand
Kinetics of calcium dissociation from calmodulin and its tryptic fragments. A stopped-flow fluorescence study using Quin 2 reveals a two-domain structure.
TLDR
The kinetic properties of the two proteolytic fragments are closely similar to the fast and slowly dissociating sites of nativecalmodulin, supporting the idea that calmodulin is constructed from two largely independent domains. Expand
The kinetics of calcium binding to calmodulin: Quin 2 and ANS stopped-flow fluorescence studies.
TLDR
These experiments provide confirmation that the calcium induced conformational change cannot be resolved kinetically from the calcium binding or dissociation, and by inference this conformationalchange is not a rate-limiting process in the function of calmodulin. Expand
Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes.
TLDR
The results indicate that the heat-induced changes in hemagglutinin which allow fusion activity result in partial denaturation of the molecule, and the changes in structure required for fusion at low pH and normal temperature are specifically restricted. Expand
Kinetic Control of the Dissociation Pathway of Calmodulin-Peptide Complexes*
TLDR
Numerical simulation of the mechanism of dissociation reactions induced by calcium chelators for complexes of Drosophila calmodulin with target peptides shows that subtle changes in the peptide sequence can have significant effects on both the Dissociation rates and also the dissociation pathway. Expand
A Lateral Cap model of microtubule dynamic instability
TLDR
A quantitative kinetic model is presented in which only the terminal layer of the multi‐start helical microtubule lattice contains tubulin‐GTP molecules, comprising a ‘Lateral Cap’, which readily reproduces the decisive experimental evidence of micro Tubule dynamics, and predicts a co‐operative mechanism for microtubules transitions. Expand
Evidence that the amantadine-induced, M2-mediated conversion of influenza A virus hemagglutinin to the low pH conformation occurs in an acidic trans Golgi compartment.
TLDR
Results indicate that the alteration in HA is the direct consequence of exposure to an adverse low pH and provide further support for the conclusion that the M2 protein, the target of amantadine action, is involved in regulating vesicular pH, a function important for the correct maturation of the HA glycoprotein. Expand
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