2022
DOI: 10.1016/j.jmb.2022.167638
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Electrostatics Drive the Molecular Chaperone BiP to Preferentially Bind Oligomerized States of a Client Protein

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Cited by 2 publications
(2 citation statements)
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“…ProIGF2 can oligomerize, a property shared by many other secreted peptide hormones (26); both BiP and Grp94 influence proIGF2 oligomerization. Multiple BiP binding sites have been identified on proIGF2, and interestingly, Grp94 binds these regions with an affinity that is too weak to quantify (6). This weakening of client binding from BiP to Grp94 appears to be analogous to the energetically uphill client binding from ERdj3 to BiP discussed above.…”
Section: Coordination Between Bip and Grp94mentioning
confidence: 94%
“…ProIGF2 can oligomerize, a property shared by many other secreted peptide hormones (26); both BiP and Grp94 influence proIGF2 oligomerization. Multiple BiP binding sites have been identified on proIGF2, and interestingly, Grp94 binds these regions with an affinity that is too weak to quantify (6). This weakening of client binding from BiP to Grp94 appears to be analogous to the energetically uphill client binding from ERdj3 to BiP discussed above.…”
Section: Coordination Between Bip and Grp94mentioning
confidence: 94%
“…The charge of a protein contributes significantly to a variety of biochemical, biophysical, and biological phenomena. As interest in high concentration protein therapeutics (biologics) increases, it is apparent that accurate estimations of protein charge and charge distribution are needed. Challenges in the development of high-concentration biologics include undesirable properties of potential therapeutic proteins such as high solution viscosity and aggregation or limited solubility, which lead to difficulties in manufacturing, long-term storage, and delivery to patients .…”
Section: Introductionmentioning
confidence: 99%