Auswahl der wissenschaftlichen Literatur zum Thema „Domain-motif interaction“
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Zeitschriftenartikel zum Thema "Domain-motif interaction"
Pang, Erli, und Kui Lin. „Yeast protein–protein interaction binding sites: prediction from the motif–motif, motif–domain and domain–domain levels“. Molecular BioSystems 6, Nr. 11 (2010): 2164. http://dx.doi.org/10.1039/c0mb00038h.
Der volle Inhalt der QuelleMillard, Peter S., Konrad Weber, Birthe B. Kragelund und Meike Burow. „Specificity of MYB interactions relies on motifs in ordered and disordered contexts“. Nucleic Acids Research 47, Nr. 18 (10.08.2019): 9592–608. http://dx.doi.org/10.1093/nar/gkz691.
Der volle Inhalt der QuelleLim, Jia Jia, Youngjin Lee, Tue Tu Ly, Jung Youn Kang, Jung-Gyu Lee, Jun Yop An, Hyung-Seop Youn et al. „Structural insights into the interaction of p97 N-terminus domain and VBM in rhomboid protease, RHBDL4“. Biochemical Journal 473, Nr. 18 (12.09.2016): 2863–80. http://dx.doi.org/10.1042/bcj20160237.
Der volle Inhalt der QuelleNielsen, Anders Lade, Poul Jørgensen, Thierry Lerouge, Margarita Cerviño, Pierre Chambon und Régine Losson. „Nizp1, a Novel Multitype Zinc Finger Protein That Interacts with the NSD1 Histone Lysine Methyltransferase through a Unique C2HR Motif“. Molecular and Cellular Biology 24, Nr. 12 (15.06.2004): 5184–96. http://dx.doi.org/10.1128/mcb.24.12.5184-5196.2004.
Der volle Inhalt der QuelleBardwell, V. J., und R. Treisman. „The POZ domain: a conserved protein-protein interaction motif.“ Genes & Development 8, Nr. 14 (15.07.1994): 1664–77. http://dx.doi.org/10.1101/gad.8.14.1664.
Der volle Inhalt der QuelleHe, Bin, und Elizabeth M. Wilson. „Electrostatic Modulation in Steroid Receptor Recruitment of LXXLL and FXXLF Motifs“. Molecular and Cellular Biology 23, Nr. 6 (15.03.2003): 2135–50. http://dx.doi.org/10.1128/mcb.23.6.2135-2150.2003.
Der volle Inhalt der QuellePascoe, Heath G., Stephen Gutowski, Hua Chen, Chad A. Brautigam, Zhe Chen, Paul C. Sternweis und Xuewu Zhang. „Secondary PDZ domain-binding site on class B plexins enhances the affinity for PDZ–RhoGEF“. Proceedings of the National Academy of Sciences 112, Nr. 48 (16.11.2015): 14852–57. http://dx.doi.org/10.1073/pnas.1508931112.
Der volle Inhalt der QuelleLitvinov, Rustem I., Marco Mravic, Hua Zhu, John W. Weisel, William F. DeGrado und Joel S. Bennett. „Unique transmembrane domain interactions differentially modulate integrin αvβ3 and αIIbβ3 function“. Proceedings of the National Academy of Sciences 116, Nr. 25 (03.06.2019): 12295–300. http://dx.doi.org/10.1073/pnas.1904867116.
Der volle Inhalt der QuelleBrady, Troy L., Peter G. Fuerst, Robert A. Dick, Clarice Schmidt und Daniel F. Voytas. „Retrotransposon Target Site Selection by Imitation of a Cellular Protein“. Molecular and Cellular Biology 28, Nr. 4 (17.12.2007): 1230–39. http://dx.doi.org/10.1128/mcb.01502-07.
Der volle Inhalt der QuelleGurung, Raju, Darlami Om, Rabin Pun, Soonsil Hyun und Dongyun Shin. „Recent Progress in Modulation of WD40-Repeat Domain 5 Protein (WDR5): Inhibitors and Degraders“. Cancers 15, Nr. 15 (01.08.2023): 3910. http://dx.doi.org/10.3390/cancers15153910.
Der volle Inhalt der QuelleDissertationen zum Thema "Domain-motif interaction"
Vivona, Sandro. „VAMP7: a model system to study the Longin Domain-SNARE motif“. Doctoral thesis, Università degli studi di Padova, 2009. http://hdl.handle.net/11577/3421900.
Der volle Inhalt der QuelleLe cellule eucariote sono caratterizzate da un complesso sistema di membrane, che offre svariate compartimentazioni con diverse condizioni chimico-fisiche. Se da una parte tale sistema permette la realizzazione di un’ampia gamma di processi biochimici, dall’altra richiede un altrettanto complesso sistema di interscambio atto al suo mantenimento. Tale interscambio è assicurato dal trafficking di vescicole che originano da un compartimento donatore e riversano il loro contenuto in un compartimento accettore attraverso un processo che richiede la fusione delle membrane lipidiche. Tale processo si fonda sull’organizzazione di complessi macromolecolari a cui contribuiscono varie famiglie proteiche ben conservate attraverso l’evoluzione eucariotica. La famiglia delle SNARE è una di queste. Le SNAREs sono considerate i motori della fusione di membrane. La loro capacità di formare complessi specifici in trans tra le due memrane su cui risiedono fornisce il contributo energetico necessario a indurre la fusione degli strati lipidici. Tali complessi consistono in un intreccio di quattro eliche chiamate SNARE motifs, domini di circa 60-70 amino acidi che definiscono tutte le SNAREs. Oltre allo SNARE motif, le SNAREs contengono spesso domini accessori a funzione regolativa. Uno di questi è il Longin Domain (LD). Il LD non è limitato alle sole SNAREs e anzi si ritrova in altre famiglie proteiche tutte coinvolte in processi molecolari riguardanti il ciclo vitale di una vescicola. Nelle SNAREs, il LD definisce una famiglia chiamata Longins, suddivisa a sua volta nelle proteine Ykt6, Sec22b e VAMP7. Il LD consiste di circa 120 aminoacidi organizzati in una struttura spaziale globulare che comprende un piano di cinque foglietti ? (?1- ?5), complessati da un’alfa elica (?1) su un lato e da altre due eliche (?2-?3) sull’altro. In Ykt6 e Sec22b si è dimostrata la possibilità che il LD si ripieghi sullo SNARE motif e lo coordini su una sua superficie idrofobica compresa tra ?1 e ?3. Questo meccanismo si è dimostrato in grado di prevenire la formazione di complessi SNARE non specifici. Tuttavia ben poco si conosce ad oggi sulla natura di questa interazione in termini dinamici, a differenza di quanto invece si sa per un analogo meccanismo osservato nella famiglia SNARE delle Sintaxine. In altri temrini non è dato sapere se nelle Longine questo meccanismo implica una conformazione stabilmente “chiusa” di LD e SNARE, o se piuttosto esso si realizza come un equilibrio dinamico tra conformazioni aperte e chiuse. Una serie di motivi, tra cui l’assenza di dati diretti per questo fenomeno in VAMP7 e la possibilità di usufruire di sue varianti naturali, ci hanno spinto a scegliere VAMP7 come sistema modello per fornire le risposte ai suddetti interrogativi. I nostri dati suggeriscono per le Longine una conformazione stabilmente chiusa, ma non omogenea e capace di cambi conformazionali molto rapidi. Questo lavoro complementa bene quanto già noto per le sintaxine e fornisce dunque la possibilità di comprendere meglio i meccanismi regolativi gneralmente adottati nella fusione vescicolare.
COSTA, STEFANO. „PepspotDB: una banca dati per l'immagazzinamento e l'analisi di esperimenti basati sulla tecnologia degli array di peptidi“. Doctoral thesis, Università degli Studi di Roma "Tor Vergata", 2009. http://hdl.handle.net/2108/984.
Der volle Inhalt der QuelleThe mapping of the “interactome” (i.e. the network comprising all possible physical protein-protein interactions naturally occurring within a cell or an organism) of living organisms is a key asset to promote the advancement of Systems Biology. Notwithstanding the numerous insights we have gained from the study of protein-protein interaction networks, currently available interactomes present several shortcomings, one of the more crucial being the lack of information regarding the regions involved in the interactions. Especially important in this respect are several families of conserved protein domains (e. g. SH2, SH3, WW, EVH1) that mediate protein-protein interactions by binding to short linear motifs. Our group has recently devised a strategy based on peptide array technology to study on a large scale the target recognition specificity of domains binding to short peptides. Our approach consists of an experimental and a computational part: 1) the domains are profiled by testing them with ad hoc designed peptide arrays; 2) Neural Network based predictors are trained for each of the profiled domains and the predictions are combined in a Bayesian framework with information coming from multiple orthogonal sources to obtain an integrated interaction confidence score. The approach has been applied to the identification of all human protein-protein interactions mediated by SH2 domains. To support the projects employing our approach, we have developed a brand new database-centered application, called PepspotDB, specifically designed to facilitate the storage and analysis of molecular interaction assays exploiting peptide array technology. We hope that PepspotDB will grow enough to become a prominent resource for the storage, analysis and retrieval of peptide chip data. PepspotDB comes with a traditional relational database, where experimental results, computational predictions and data imported from the literature or other external sources are stored, a rich web application, providing a user-friendly, yet powerful, interface to the database, and a set of tools to automatically process raw experimental data, identify promising candidate binders and visualize sequence logos. At the time of writing, PepspotDB contains more than 5 million records, comprising about 80 experiments and 55,548 domain-peptide interactions involving 70 SH2 domains and 7,972 unique peptides. These numbers are bound to more than double as new experiments involving other domain families are completed. Scientists studying protein-protein interactions mediated by domains recognizing linear peptides may find PepspotDB a precious resource to foster their own research.
Berardi, A. „STRUCTURAL INSIGHTS INTO THE INTERACTION BETWEEN THE TANDEM PHD FINGER DOMAIN P5C5 OF NSD1 AND THE ZINC FINGER MOTIF C2HR OF NIZP1“. Doctoral thesis, Università degli Studi di Milano, 2014. http://hdl.handle.net/2434/247139.
Der volle Inhalt der QuelleReh, Juliane, Annett Stange, Anne Götz, Marlene Rönitz, Arend Große und Dirk Lindemann. „An N-terminal domain helical motif of Prototype Foamy Virus Gag with dual functions essential for particle egress and viral infectivity“. Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2014. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-127152.
Der volle Inhalt der QuelleReh, Juliane, Annett Stange, Anne Götz, Marlene Rönitz, Arend Große und Dirk Lindemann. „An N-terminal domain helical motif of Prototype Foamy Virus Gag with dual functions essential for particle egress and viral infectivity“. BioMed Central, 2013. https://tud.qucosa.de/id/qucosa%3A27282.
Der volle Inhalt der QuelleJané, Palli Pau. „Quantification des affinités PBM/PDZ et de leurs sites modulateurs par des approches expérimentales et informatiques à haut débit“. Electronic Thesis or Diss., Strasbourg, 2020. http://www.theses.fr/2020STRAJ051.
Der volle Inhalt der QuelleThis thesis focuses on PDZ domains, a family of globular domains that bind to conserved PDZ-Binding Motifs (called henceforth PBMs) generally situated at the extreme C-terminus of their partner proteins. Domain-motif networks are often modulated by reversible post-translational modifications (PTMs). We used synthetized PBMs to reproduce different conditions, such as a wild-type, acetylation or phosphorylation, addition of extra exosites or residue mimication of PTM in the literature. These peptides were used for interaction studies using the holdup assay, an assay originally developed in our laboratory. We evaluated the impact of diverse modifications of the PBM/PDZ interactions, which led to a global change of the PDZ-binding capability. These results provided quantitative information on the biological effects that such modifications may have in the context of full-length proteins
Biasutto, Antonio. „Structural insights into human SNF2/SWI2 chromatin remodeler SMARCAD1 and its role in DNA repair“. Thesis, University of Oxford, 2016. https://ora.ox.ac.uk/objects/uuid:efc019ba-41ee-4dbd-adfb-2786017e91aa.
Der volle Inhalt der QuelleStein, Amelie. „Peptime-mediated interactions in high-resolution 3-dimensional structures“. Doctoral thesis, Universitat Pompeu Fabra, 2010. http://hdl.handle.net/10803/7218.
Der volle Inhalt der QuelleLos procesos moleculares subyacentes a la mayoría de funciones biológicas implican la participación directa de una infinidad de proteínas y múltiples interacciones entre ellas. En esta tesis estudiamos un tipo particular de estas interacciones, de carácter transitorio y altamente específicas, dónde un dominio globular en una proteína reconoce un corto péptido lineal en otra (DMIs). En concreto, identificamos múltiples casos de DMIs en estructuras tridimensionales (3D) de alta resolución y analizamos las bases moleculares de su especificidad. Además, derivamos parámetros estructurales globales que nos permiten identificar nuevos casos de DMIs. Así mismo, y como caso práctico, combinamos el motivo de fosforilación propio de la quinasa humana Aurora A con diversas clases de información contextual para predecir y validar 90 nuevos substratos. Por último, incorporamos las caracterizadas DMIs en nuestra base de datos de interacciones en 3D (3did) con el fin de diseminar nuestros resultados entre la comunidad científica.
Liu, Shao-Hsuan, und 劉劭萱. „Characterization of the Interaction between Serine 269 Phosphorylated Aquaporin-2 PDZ Motif and Sipa1l1 Domain“. Thesis, 2016. http://ndltd.ncl.edu.tw/handle/13827132453844395362.
Der volle Inhalt der Quelle國立臺灣大學
生物化學暨分子生物學研究所
104
Vasopressin regulates the amount of the water channel protein aquaporin-2 (AQP2) in the apical plasma membrane via enhancing exocytosis and/or reducing endocytosis of AQP2-containing vesicles to and from the apical plasma membrane of the kidney collecting duct cells. Previous studies suggest that vasopressin induces AQP2 phosphorylation at serine 269 (S269), which enhances retention of AQP2 in the apical plasma membrane. We previously identified Sipa1l1, a PDZ domain-containing protein that regulates apical retention of serine 269-phosphorylated AQP2. Sipa1l1 reduces its interaction with the serine 269 phosphorylated AQP2 PDZ motif. To directly measure this PDZ interaction, we expressed and purified the Sipa1l1 PDZ domain with fusion tags glutathione-S-transferase, thioredoxin, 6x His, and maltose binding protein. Surface plasmon resonance binding experiments showed weaker binding of the serine 269 phosphorylated AQP2 peptide to the Sipa1l1 PDZ compared with the serine 269 non-phosphorylated AQP2 peptide. Models of the Sipa1l1 PDZ domain-AQP2 PDZ motif complex showed phosphorylation at serine 269 of the AQP2 PDZ domain reduces its interaction with the Sipa1l1 PDZ domain.
Cieplak-Rotowska, Maja. „Biophysical and molecular biology studies of proteins involved in gene silencing“. Doctoral thesis, 2017. https://depotuw.ceon.pl/handle/item/2368.
Der volle Inhalt der QuelleNiniejsza praca doktorska dotyczy biofizycznych podstaw oddziaływania między białkami zaangażowanymi w wyciszanie ekspresji genów przez mikro-RNA (miRNA), a mianowicie pomiędzy białkiem CNOT1 a domeną wyciszającą białka GW182. W procesie wyciszania ekspresji genów przez miRNA, cząsteczki te wiążą się z białkiem Argonaute i naprowadzają je na cząsteczkę mRNA, która ma ulec wyciszeniu. Z białkiem Argonaute oddziałuje białko GW182, które z kolei wiąże się z kompleksem deadenylaz CCR4-NOT. Kompleks ten deadenyluje mRNA oraz może także blokować jego translację, co łącznie prowadzi do wyciszenia ekspresji danego genu. Z kolei w wyciszaniu mRNA zawierających sekwencje bogate w adeninę i urydynę, rolę miRNA wraz z Argonaute i GW182 pełni białko o nazwie tristetraprolina, które odgrywa kluczową rolę w procesach odpowiedzi na stany zapalne. Oddziaływania pomiędzy składnikami tego skomplikowanego układu białek o wielkich masach cząsteczkowych są jeszcze stosunkowo słabo poznane. W szczególności, nieznane były miejsca odpowiedzialne za tworzenie kompleksu pomiędzy GW182 a CCR4-NOT. Doświadczenia z zakresu biologii molekularnej pozwoliły na identyfikację miejsc wiążących CCR4-NOT w sekwencji domeny wyciszającej białka GW182. Jedno z nich ma kluczowy wpływ na deadenylację, a drugie - kluczowy wpływ na oddziaływanie z kompleksem CCR4-NOT za pośrednictwem jego centralnej podjednostki CNOT1. Badania biofizyczne metodą wymiany wodór-deuter sprzężoną ze spektrometrią mas pozwoliły z kolei na identyfikację miejsca oddziaływania GW182 na białku CNOT1 (we fragmencie 800-999), które, niespodziewanie, okazało się bardzo dobrze pokrywać z miejscem oddziaływania CNOT1(800-999) z tristetraproliną. Eksperymenty biochemiczne wykazały, że białka te konkurują o miejsce oddziaływania na CNOT1(800-999). Białka GW182 i tristetraprolina oddziałują z CNOT1 wykorzystując ten sam motyw sekwencji, RLPXφ, w bardzo podobny, jednak nie identyczny sposób. Sekwencja ta prawdopodobnie działa jako tzw. krótki motyw liniowy (z ang. short linear motif, SLiM). Zatem te dwa szlaki kontroli nad ekspresją genów krzyżują się. W pracy zbadano także dynamikę strukturalną białka CNOT1(800-999) oraz domeny wyciszającej białka GW182. Wykazano eksperymentalnie, że białko GW182 ma nieustrukturyzowany charakter, oprócz domeny wiążącej RNA (RRM), która ma strukturę bardzo dynamiczną. Natomiast białko CNOT1(800-999) charakteryzuje się stabilną, ściśle upakowaną strukturą. Przeprowadzone badania doprowadziły do odkrycia miejsc oddziaływania pomiędzy natywnie nieustrukturyzowaną domeną wyciszającą GW182, a helikalnym fragmentem białka CNOT1(800 999), przyczyniając się do zrozumienia molekularnych mechanizmów rozpoznawania w kompleksach białkowych odpowiedzialnych za regulację ekspresji genów w różnych procesach komórkowych.
Buchteile zum Thema "Domain-motif interaction"
Littlewood, Trevor D., und Gerard I. Evan. „Introduction“. In Helix-Loop-Helix Transcription Factors, 1–5. Oxford University PressOxford, 1998. http://dx.doi.org/10.1093/oso/9780198502487.003.0001.
Der volle Inhalt der QuellePieler, Tomas. „Interaction of 5S RNA -with TFIIIA“. In RNA-Protein Interactions, 178–91. Oxford University PressOxford, 1995. http://dx.doi.org/10.1093/oso/9780199635054.003.0008.
Der volle Inhalt der QuelleKonferenzberichte zum Thema "Domain-motif interaction"
Hongbiao Liu und J. Liu. „Prediction of Domain Interactive Motif Pairs“. In 2005 IEEE Engineering in Medicine and Biology 27th Annual Conference. IEEE, 2005. http://dx.doi.org/10.1109/iembs.2005.1616309.
Der volle Inhalt der QuelleBorges, Heraldo, Antonio Castro, Rafaelli Coutinho, Fabio Porto, Esther Pacitti und Eduardo Ogasawara. „STMotif Explorer: A Tool for Spatiotemporal Motif Analysis“. In Anais Estendidos do Simpósio Brasileiro de Banco de Dados. Sociedade Brasileira de Computação - SBC, 2023. http://dx.doi.org/10.5753/sbbd_estendido.2023.233371.
Der volle Inhalt der QuelleCho, Hongkwan, Abdul Sheikh und Daria A. Narmoneva. „Non-Specific Endothelial Cell Interactions With the Substrate Result in Cell Activation and Angiogenesis In Vitro“. In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19094.
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