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Akademický článek

Tau Protein and Tauopathies: Exploring Tau Protein-Protein and Microtubule Interactions, Cross-Interactions and Therapeutic Strategies.

Autor: Di Lorenzo D; Department of Chemistry, Organic and Bioorganic Chemistry, Bielefeld University, Universitätsstraße 25, D-33615, Bielefeld, Germany.

Publikováno v: ChemMedChem [ChemMedChem] 2024 Nov 04; Vol. 19 (21), pp. e202400180. Date of Electronic Publication: 2024 Sep 22.

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Akademický článek

Statistical Survey of Chemical and Geometric Patterns on Protein Surfaces as a Blueprint for Protein‐Mimicking Nanoparticles.

Autor: McBride, John M.¹ (AUTHOR) jmmcbride@protonmail.com, Koshevarnikov, Aleksei² (AUTHOR), Siek, Marta¹ (AUTHOR), Grzybowski, Bartosz A.^1,2,3 (AUTHOR) grzybor72@unist.ac.kr, Tlusty, Tsvi^1,3 (AUTHOR) tsvi@unist.ac.kr

Publikováno v: Small Structures. Sep2024, Vol. 5 Issue 9, p1-12. 12p.

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Deamidation of HPr, a phosphocarrier protein of the phosphoenolpyruvate:sugar phosphotransferase system, involves asparagine 38 (HPr-1) and asparagine 12 (HPr-2) in isoaspartyl acid formation

Autor: R. E. Klevit, P. K. Hammen, W. Hengstenberg, Sadhana Sharma, F. Georges, E. B. Waygood, A. Leung, Anderson Jw

Publikováno v: Journal of Biological Chemistry. 268:17695-17704

Histidine-containing protein, HPr, of the phosphoenolpyruvate:sugar phosphotransferase system in Escherichia coli, when incubated at elevated temperatures forms many species of protein. The two major species are HPr-1 and HPr-2, which have been shown

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::88b94d01d12e3a8514ebb29759538e9b
https://doi.org/10.1016/s0021-9258(17)46760-3

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The involvement of the arginine 17 residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli

Autor: F. Georges, K Pullen, R. E. Klevit, E. B. Waygood, Anderson Jw

Publikováno v: Journal of Biological Chemistry. 268:12325-12333

Histidine-containing protein, HPr, of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system has an active site His-15 that is phosphorylated to form N delta 1-P-histidine. The nearby conserved residue, Arg-17, has been replaced by:

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::baaaed1d46af92800fc4b4cf3663cb36
https://doi.org/10.1016/s0021-9258(18)31393-0

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Akademický článek

Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.

Autor: Kochańczyk T; Structural Biology Program, Sloan Kettering Institute, 1275 York Avenue, New York, New York, 10065, USA., Fishman M; Structural Biology Program, Sloan Kettering Institute, 1275 York Avenue, New York, New York, 10065, USA., Lima CD; Structural Biology Program, Sloan Kettering Institute, 1275 York Avenue, New York, New York, 10065, USA.; Howard Hughes Medical Institute, 1275 York Avenue, New York, New York, 10065, USA.

Publikováno v: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Sep 23, pp. e202400659. Date of Electronic Publication: 2024 Sep 23.

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Structure of a BRCA1-BARD1 heterodimeric RING-RING complex

Autor: P S, Brzovic, P, Rajagopal, D W, Hoyt, M C, King, R E, Klevit

Publikováno v: Nature structural biology. 8(10)

The RING domain of the breast and ovarian cancer tumor suppressor BRCA1 interacts with multiple cognate proteins, including the RING protein BARD1. Proper function of the BRCA1 RING domain is critical, as evidenced by the many cancer-predisposing mut

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0b5e8540f79f657dfc79af05b3916faf
https://pubmed.ncbi.nlm.nih.gov/11573079

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BRCA1 RING domain cancer-predisposing mutations. Structural consequences and effects on protein-protein interactions

Autor: P S, Brzovic, J E, Meza, M C, King, R E, Klevit

Publikováno v: The Journal of biological chemistry. 276(44)

Cancer-predisposing missense mutations in the RING domain of BRCA1 primarily target Zn(2+)-liganding residues. Here we report on the structural consequences of such mutations introduced into the second Zn(2+) site (Site II) of the BRCA1 RING domain a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::694c2d8f893d1a5963f00bc29b42e235
https://pubmed.ncbi.nlm.nih.gov/11526114

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A folding transition and novel zinc finger accessory domain in the transcription factor ADR1

Autor: P M, Bowers, L E, Schaufler, R E, Klevit

Publikováno v: Nature structural biology. 6(5)

The region responsible for sequence-specific DNA binding by the transcription factor ADR1 contains two Cys2-His2 zinc fingers and an additional N-terminal proximal accessory region (PAR). The N-terminal (non-finger) PAR is unstructured in the absence

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a65f73bd5664db0e91103d740c37f506
https://pubmed.ncbi.nlm.nih.gov/10331877

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Increased helix and protein stability through the introduction of a new tertiary hydrogen bond

Autor: R W, Peterson, E M, Nicholson, R, Thapar, R E, Klevit, J M, Scholtz

Publikováno v: Journal of molecular biology. 286(5)

In an effort to quantify the importance of hydrogen bonding and alpha-helix formation to protein stability, a capping box motif was introduced into the small phosphocarrier protein HPr. Previous studies had confirmed that Ser46, at the N-cap position

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a4ece72a6d11f89d6edecdcb7fa6502c
https://pubmed.ncbi.nlm.nih.gov/10064718

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