Ac-IEEVD-OH

Ref. 3D-PP48170

Produktinformation

• Name: Ac-IEEVD-OH

Beschreibung

Peptide Ac-IEEVD-OH is a Research Peptide with significant interest within the field academic and medical research. This peptide is available for purchase at Cymit Quimica in multiple sizes and with a specification of your choice. Recent citations using Ac-IEEVD-OH include the following: Chaperone-interacting TPR proteins in Caenorhabditis elegans V Haslbeck, JM Eckl, CJO Kaiser , K Papsdorf - Journal of molecular , 2013 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0022283613003331 Exploration of the Binding Determinants of Protein Phosphatase 5 (PP5) Reveals a Chaperone-Independent Activation Mechanism S Devi, A Charvat, Z Millbern, N Vinueza - Journal of Biological , 2024 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0021925824019367 Structure of the TPR domain of AIP: lack of client protein interaction with the C-terminal alpha-7 helix of the TPR domain of AIP is sufficient for pituitary adenoma RML Morgan , LC Hernandez-Ramaca­rez , G Trivellin - PloS one, 2012 - journals.plos.orghttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0053339 Hsp90 as a Member of Dicarboxylate Clamp TPR Protein Interaction Network: Implication in Human Diseases and Prospect as a Drug Target R Kumar , B Winblad, PF Pavlov - Heat Shock Protein 90 in Human , 2019 - Springerhttps://link.springer.com/chapter/10.1007/978-3-030-23158-3_14 The study of structural and mechanistic features of Hsp70/CHIP-driven protein quality control PA Don - 2023 - rave.ohiolink.eduhttps://rave.ohiolink.edu/etdc/view?acc_num=miami167155209682274 Two distinct classes of cochaperones compete for the EEVD motif in heat shock protein 70 to tune its chaperone activities OT Johnson , CM Nadel, EC Carroll , T Arhar - Journal of Biological , 2022 - ASBMBhttps://www.jbc.org/article/S0021-9258(22)00137-5/abstract Two distinct classes of co-chaperones compete for the EEVD motif in heat shock protein 70 (Hsp70) to tune its activity OT Johnson , CM Nadel, EC Carroll , T Arhar - bioRxiv, 2021 - biorxiv.orghttps://www.biorxiv.org/content/10.1101/2021.10.18.464838.abstract Binding properties of the quaternary assembly protein SPAG1 ME Chagot, R Dos Santos Morais - Biochemical , 2019 - portlandpress.comhttps://portlandpress.com/biochemj/article-abstract/476/11/1679/219592 Interaction with the membrane-anchored protein CHIC2 constrains the ubiquitin ligase activity of CHIP MD Callahan, M Hodul , EC Carroll , M Ravalin - bioRxiv, 2023 - biorxiv.orghttps://www.biorxiv.org/content/10.1101/2023.07.17.549407.abstract The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex MC Smith , KM Scaglione , VA Assimon, S Patury - Biochemistry, 2013 - ACS Publicationshttps://pubs.acs.org/doi/abs/10.1021/bi4009209 C-end Binding by TPR Co-chaperones Links Proteolysis and Protein Homeostasis MA Ravalin - 2019 - search.proquest.comhttps://search.proquest.com/openview/7f8b07f9d9151c510d5ddf8cae77492b/1?pq-origsite=gscholar&cbl=18750&diss=y Discovery and Characterization of Chaperone-Independent Substrates of the CHIP Ubiquitin Ligase M Callahan - 2023 - search.proquest.comhttps://search.proquest.com/openview/ce5689e24737b06bcd0f9abd67ad0b7d/1?pq-origsite=gscholar&cbl=18750&diss=y Structure-based discovery of small molecule inhibitors of FKBP51-Hsp90 protein-protein interaction L Wang, R Kumar , B Winblad, PF Pavlov - European Journal of Medicinal , 2024 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0223523424002368 The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90 KLIM Blundell, M Pal, SM Roe, LH Pearl - PLoS One, 2017 - journals.plos.orghttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0173543 The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain JN Connarn, VA Assimon, RA Reed, E Tse - Journal of Biological , 2014 - ASBMBhttps://www.jbc.org/article/S0021-9258(19)74811-X/abstract Molecular basis for TPR domain-mediated regulation of protein phosphatase 5 J Yang, SM Roe, MJ Cliff , MA Williams - The EMBO , 2005 - embopress.orghttps://www.embopress.org/doi/abs/10.1038/sj.emboj.7600496 Unraveling the CHIP: Hsp70 complex as an information processor for protein quality control J VanPelt, RC Page - Biochimica et Biophysica Acta (BBAhttps://www.sciencedirect.com/science/article/pii/S1570963916302321 1H, 15N and 13C resonance assignments for free and IEEVD peptide-bound forms of the tetratricopeptide repeat domain from the human E3 ubiquitin ligase CHIP H Zhang , C McGlone, MM Mannion - Biomolecular NMR , 2017 - Springerhttps://link.springer.com/article/10.1007/s12104-016-9710-y Biophysical Study of the Ubiquitin Ligase CHIP and Interactions with the Molecular Chaperones Hsp70 and Hsp90 H Zhang - 2017 - rave.ohiolink.eduhttps://rave.ohiolink.edu/etdc/view?acc_num=miami1511192922525393 Control of Androgen Receptor Signaling in Prostate Cancer by the Cochaperone Small Glutamine-Rich Tetratricopeptide Repeat Containing Protein alpha G Buchanan , C Ricciardelli , JM Harris , J Prescott - Cancer research, 2007 - AACRhttps://aacrjournals.org/cancerres/article-abstract/67/20/10087/533644 The remarkable multivalency of the Hsp70 chaperones ERP Zuiderweg, LE Hightower, JE Gestwicki - Cell Stress and Chaperones, 2017 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S1355814523001724 Luminescence complementation assay for measurement of binding to protein C-termini in live cells CM Nadel, X Ran, JE Gestwicki - Analytical biochemistry, 2020 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0003269720304796 On the structure and function of Sorghum bicolor CHIP (carboxyl terminus of Hsc70-interacting protein): A link between chaperone and proteasome systems CC Goncalves, GMS Pinheiro, KM Dahlström - Plant science, 2020 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0168945220301096 "œTuning" the ATPase activity of Hsp90 C Prodromou , RML Morgan - Regulation of Ca2+-ATPases, V-ATPases , 2016 - Springerhttps://link.springer.com/chapter/10.1007/978-3-319-24780-9_23 The non-canonical Hop protein from Caenorhabditis elegans exerts essential functions and forms binary complexes with either Hsc70 or Hsp90 AM Gaiser, F Brandt, K Richter - Journal of molecular biology, 2009 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0022283609007694 CHIP: a co-chaperone for degradation by the proteasome AL Edkins - The Networking of Chaperones by Co-chaperones , 2015 - Springerhttps://link.springer.com/chapter/10.1007/978-3-319-11731-7_11 Mirror-image ligand discovery enabled by single-shot fast-flow synthesis of D-proteins AJ Callahan, S Gandhesiri , TL Travaline - Nature , 2024 - nature.comhttps://www.nature.com/articles/s41467-024-45634-z CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome A Chakraborty, AL Edkins - The Networking of Chaperones by Co , 2022 - Springerhttps://link.springer.com/chapter/10.1007/978-3-031-14740-1_12

• Marke: Biosynth