c4 peptide macrotrap cartridge (Michrom)
90
Structured Review
Michrom
c4 peptide macrotrap cartridge
C4 Peptide Macrotrap Cartridge, supplied by Michrom, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c4+peptide+macrotrap+cartridge/c4+peptide+macrotrap+cartridge/pm17176086-123-13-17
Average 90 stars, based on 1 article reviews
C4 Peptide Macrotrap Cartridge, supplied by Michrom, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c4+peptide+macrotrap+cartridge/c4+peptide+macrotrap+cartridge/pm17176086-123-13-17
Average 90 stars, based on 1 article reviews
c4 peptide macrotrap cartridge - by Bioz Stars,
2026-09
90/100 stars
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other:Article Title: Use of hydrogen/deuterium exchange mass spectrometry and mutagenesis as a tool to identify the binding region of inhibitors targeting the human mitotic kinesin Eg5. Article Snippet: An experimental procedure associating both hydrogen/deuterium exchange mass spectrometry (H/D-MS) and mutagenesis was developed to identify the protein-binding region of small inhibitors targeting the motor domain of the human mitotic kinesin Eg5.. All the tested inhibitors decrease the deuterium incorporation rate of the same peptides corresponding to the following secondary structure elements: loop L5/helix a2 (region Tyr125-Glu145) and strand b5/helix a3 (region Ile202-Leu227).. Replacement of these two regions by the equivalent ones from N. crassa conventional kinesin heavy chain completely abolishes the modification of the deuterium incorporation rate by the inhibitors as well as their effects on the basal ATPase activity. Article Title: Identification of the protein binding region of S-trityl-L-cysteine, a new potent inhibitor of the mitotic kinesin Eg5. Article Snippet: Human Eg5, a mitotic motor of the kinesin superfamily, is involved in the formation and maintenance of the mitotic spindle.. The recent discovery of small molecules that inhibit HsEg5 by binding to its catalytic motor domain leading to mitotic arrest has attracted more interest in Eg5 as a potential anticancer drug target.. We have used hydrogen-deuterium exchange mass spectrometry and directed mutagenesis to identify the secondary structure elements that form the binding sites of new Eg5 inhibitors, in particular for S-trityl-L-cysteine, a potent inhibitor of Eg5 activity in Vitro and in cell-based assays. Article Title: Molecular dissection of the inhibitor binding pocket of mitotic kinesin Eg5 reveals mutants that confer resistance to antimitotic agents. Article Snippet: Present address: S. Brier, Departm Clark Hall, MSC03-2060, University Albuquerque, NM 87131-0001, USA Abbreviations used: ACES, N-(2-a aminoethane sulfonic acid; DMSO, EGTA, ethyleneglycol-bis(β-aminoe N′-tetraacetic acid; H/D, hydrogen/ electrospray ionization; LC-MS, liqu mass spectrometry; m/z, mass to ch microtubules; TFA, trifluoroacetic ac S-trityl-L-cysteine.. E-mail address of the correspondi Frank.Kozielski@ibs.fr Article Title: The marine natural product adociasulfate-2 as a tool to identify the MT-binding region of kinesins. Article Snippet: Kinesins are molecular motors that transport cargo along microtubules (MTs).. To move forward the motor must attach to the MT in a defined orientation and detach from it in a process that is driven by ATP hydrolysis.. The knowledge of the motor-MT interface is essential for a detailed understanding of how kinesins move along MTs and how they are related to other molecular motors such as myosins or dyneins. |