Výsledky vyhledávání - "Linda Whittaker"

Stabilization of a Protein by a Single Halogen-Based Aromatic Amplifier

Autor: Krystel El Hage, Nelson B. Phillips, Yen-Shan Chen, Balamurugan Dhayalan, Jonathan Whittaker, Kelley Carr, Linda Whittaker, Manijeh H. Phillips, Faramarz Ismail-Beigi, Markus Meuwly, Michael A. Weiss

The utility of halogenation in protein design is investigated by a combination of quantitative atomistic simulations and experiment. The approach is applied to insulin, a small, therapeutically relevant domain amenable to simulation and semi-synthesi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e7b5e6bc8c26a2edb3296decfd2c8a1d
https://doi.org/10.1101/2022.07.25.501420

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Aromatic Anchor at an Invariant Hormone-Receptor Interface

Autor: Jonathan Whittaker, Gabriella P. Cox, Nalinda P. Wickramasinghe, Michael A. Weiss, Brian J. Smith, John G. Menting, Faramarz Ismail-Beigi, Linda Whittaker, Vijay Pandyarajan, Zhuli Wan, Nelson B. Phillips, Michael C. Lawrence

Publikováno v: Journal of Biological Chemistry. 289:34709-34727

Crystallographic studies of insulin bound to fragments of the insulin receptor have recently defined the topography of the primary hormone-receptor interface. Here, we have investigated the role of PheB24, an invariant aromatic anchor at this interfa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b030c58a50c6cdb5cdea3108dec82b5e
https://doi.org/10.1074/jbc.m114.608562

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α-Helical element at the hormone-binding surface of the insulin receptor functions as a signaling element to activate its tyrosine kinase

Autor: Jonathan Whittaker, Charles T. Roberts, Michael C. Lawrence, Linda Whittaker, Faramarz Ismail-Beigi, Nelson B. Phillips, Michael A. Weiss

Publikováno v: Proceedings of the National Academy of Sciences. 109:11166-11171

The primary hormone-binding surface of the insulin receptor spans one face of the N-terminal β-helix of the α-subunit (the L1 domain) and an α-helix in its C-terminal segment (αCT). Crystallographic analysis of the free ectodomain has defined a c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::657c6c8fc0126b012131dc26718ba8be
https://doi.org/10.1073/pnas.1205681109

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Supramolecular Protein Engineering

Autor: Nelson B. Phillips, Michael A. Weiss, Qing Xin Hua, Faramarz Ismail-Beigi, Jonathan Whittaker, Zhu Li Wan, Kun Huang, Linda Whittaker, Shi Quan Hu

Publikováno v: Journal of Biological Chemistry. 285:11755-11759

Bottom-up control of supramolecular protein assembly can provide a therapeutic nanobiotechnology. We demonstrate that the pharmacological properties of insulin can be enhanced by design of “zinc staples” between hexamers. Paired (i, i+4) His subs

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::373891fc4c438315c2152ddf7916df51
https://doi.org/10.1074/jbc.c110.105825

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Contribution of Residue B5 to the Folding and Function of Insulin and IGF-I

Autor: Michael A. Weiss, Ming Liu, Linda Whittaker, Charles T. Roberts, Peter Arvan, Aubree A. Ng, Nelson B. Phillips, Stephen B. H. Kent, Youhei Sohma, Jonathan Whittaker, Qing Xin Hua, Shi Quan Hu

Publikováno v: Journal of Biological Chemistry. 285:5040-5055

Proinsulin exhibits a single structure, whereas insulin-like growth factors refold as two disulfide isomers in equilibrium. Native insulin-related growth factor (IGF)-I has canonical cystines (A6—A11, A7–B7, and A20—B19) maintained by IGF-bindi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b87f4a0507e50f0cdbfcc400440f1bca
https://doi.org/10.1074/jbc.m109.062992

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Design of an Insulin Analog with Enhanced Receptor Binding Selectivity

Autor: Nelson B. Phillips, Linda Whittaker, Bin Xu, Jonathan Whittaker, Ming Zhao, Faramarz Ismail-Beigi, Zhuli Wan, Michael A. Weiss, Panayotis G. Katsoyannis

Publikováno v: Journal of Biological Chemistry. 284:32178-32187

Insulin binds with high affinity to the insulin receptor (IR) and with low affinity to the type 1 insulin-like growth factor (IGF) receptor (IGFR). Such cross-binding, which reflects homologies within the insulin-IGF signaling system, is of clinical

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::81d5f6b0cafe8358555ef73e36e8f98d
https://doi.org/10.1074/jbc.m109.028399

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High-Affinity Insulin Binding: Insulin Interacts with Two Receptor Ligand Binding Sites

Autor: Linda Whittaker, Caili Hao, Jonathan Whittaker, Wen Fu

Publikováno v: Biochemistry. 47:12900-12909

The interaction of insulin with its receptor is complex. Kinetic and equilibrium binding studies suggest coexistence of high- and low-affinity binding sites or negative cooperativity. These phenomena and high-affinity interactions are dependent on th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64f3008a07f43c035eaeb19035bf69e2
https://doi.org/10.1021/bi801693h

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Characterization of a second ligand binding site of the insulin receptor

Autor: Caili Hao, Jonathan Whittaker, Linda Whittaker

Publikováno v: Biochemical and Biophysical Research Communications. 347:334-339

Insulin binding to its receptor is characterized by high affinity, curvilinear Scatchard plots, and negative cooperativity. These properties may be the consequence of binding of insulin to two receptor binding sites. The N-terminal L1 domain and the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1703612112b9005fdbd8c06ac418468
https://doi.org/10.1016/j.bbrc.2006.06.089

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