Sequence requirements of the ATP-binding site within the C-terminal nucleotide-binding domain of mouse P-glycoprotein: structure-activity relationships for flavonoid binding

Autor: D B McIntosh, A. Di Pietro, J M Jault, Denis Barron, Hélène Baubichon-Cortay, Tino Krell, Jean-Baptiste Daskiewicz, H de Wet, G. Conseil

Sequence requirements of the ATP-binding site within the C-terminal nucleotide-binding domain (NBD2) of mouse P-glycoprotein were investigated by using two recombinantly expressed soluble proteins of different lengths and photoactive ATP analogues, 8

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::321c2cf229624b667cdd0facca96e856
https://ora.ox.ac.uk/objects/uuid:e9887f4b-5a54-41c3-bb30-193027f3d503

Four Parallel Pathways in T4 Ligase‐Catalyzed Repair of Nicked DNA with Diverse Bending Angles.

Autor: Li, Na¹ (AUTHOR), Ma, Jianbing² (AUTHOR), Fu, Hang^2,3,4 (AUTHOR), Yang, Zhiwei¹ (AUTHOR), Xu, Chunhua² (AUTHOR), Li, Haihong⁵ (AUTHOR), Zhao, Yimin¹ (AUTHOR), Zhao, Yizhen¹ (AUTHOR), Chen, Shuyu¹ (AUTHOR), Gou, Lu¹ (AUTHOR), Zhang, Xinghua⁶ (AUTHOR), Zhang, Shengli¹ (AUTHOR), Li, Ming^2,3,7 (AUTHOR), Hou, Ximiao⁵ (AUTHOR) houximiao@nwsuaf.edu.cn, Zhang, Lei¹ (AUTHOR) zhangleio@mail.xjtu.edu.cn, Lu, Ying^2,3,7 (AUTHOR) yinglu@iphy.ac.cn

Publikováno v: Advanced Science. 7/3/2024, Vol. 11 Issue 25, p1-9. 9p.

Glutaraldehyde cross-links Lys-492 and Arg-678 at the active site of sarcoplasmic reticulum Ca(2+)-ATPase

Autor: D B, McIntosh

Publikováno v: The Journal of biological chemistry. 267(31)

It has been shown previously that glutaraldehyde cross-links the Ca(2+)-ATPase of sarcoplasmic reticulum intramolecularly at the active site, involving residues participating in nucleotide binding and the conformational change that results in Ca2+ re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5c8872fdeaf83e67a6584016c09df644
https://pubmed.ncbi.nlm.nih.gov/1429585

Mechanism of inhibition of sarcoplasmic reticulum Ca2(+)-ATPase by active site cross-linking. Impairment of nucleotide binding slows nucleotide-dependent phosphoryl transfer, and loss of active site flexibility stabilizes occluded forms and blocks E2-P formation

Autor: D C, Ross, G A, Davidson, D B, McIntosh

Publikováno v: The Journal of biological chemistry. 266(7)

Investigation of the properties of Ca2(+)-ATPase of sarcoplasmic reticulum cross-linked at the active site with glutaraldehyde showed that ATP binding affinity and rate of ATP-dependent phosphorylation and Ca2+ occlusion were decreased 2-3 orders of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cc9e46e441b675691a7860795a28385d
https://pubmed.ncbi.nlm.nih.gov/1825656

A Simple Device for Measuring Survival Time of Artificial Nests

Autor: I. J. Ball, D. B. Mcintosh, R. J. Gazda

Publikováno v: The Journal of Wildlife Management. 58:793

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9f96475b5c58f6432aede5bf8ce1cabc
https://doi.org/10.2307/3809695