Results 201 to 210 of about 50,255 (242)

Screening and Validation of Functional Residues of the Antimicrobial Peptide <i>Pp</i>Rcys1. [PDF]

Biomolecules
Tao M, Fei Z, Sun A, Yu G, Ye H, Shi H, Zhang W, Wang J.   +7 more
europepmc   +1 more source

Regulation of the microprocessor by post-translational modifications. [PDF]

Front Cell Dev Biol
Leong KW, Chong MMW.
europepmc   +1 more source

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PIAS proteins promote SUMO-1 conjugation to STAT1

Blood, 2003
AbstractSignal transducer and activator of transcription 1 (STAT1) is a critical mediator of interferon-γ (IFN-γ)–induced transcription that is regulated through posttranslational modifications and through transacting proteins such as protein inhibitor of activated STAT1 (PIAS1). PIAS proteins have been shown to function as E3-type small ubiquitin-like
Daniela, Ungureanu, Sari, Vanhatupa, Noora, Kotaja, Jie, Yang, Saara, Aittomaki, Olli A, Jänne, Jorma J, Palvimo, Olli, Silvennoinen   +7 more
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Cell cycle-dependent SUMO-1 conjugation to nuclear mitotic apparatus protein (NuMA)

Biochemical and Biophysical Research Communications, 2014
Covalent conjugation of proteins with small ubiquitin-like modifier 1 (SUMO-1) plays a critical role in a variety of cellular functions including cell cycle control, replication, and transcriptional regulation. Nuclear mitotic apparatus protein (NuMA) localizes to spindle poles during mitosis, and is an essential component in the formation and ...
Jae Sung, Seo, Ha Na, Kim, Sun-Jick, Kim, Jiyoung, Bang, Eun-A, Kim, Ki Sa, Sung, Hyun-Joo, Yoon, Hae Yong, Yoo, Cheol Yong, Choi   +8 more
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TOPORS Functions As A SUMO-1 E3 Ligase for Chromatin-Modifying Proteins

Journal of Proteome Research, 2007
TOPORS is the first example of a protein with both ubiquitin and SUMO-1 E3 ligase activity and has been implicated as a tumor suppressor in several different malignancies. To gain insight into the cellular role of TOPORS, a proteomic screen was performed to identify candidate sumoylation substrates.
Pooja, Pungaliya, Diptee, Kulkarni, Hye-Jin, Park, Henderson, Marshall, Haiyan, Zheng, Henry, Lackland, Ahamed, Saleem, Eric H, Rubin   +7 more
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SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation

Journal of Cell Science, 1999
ABSTRACT PML is a nuclear phosphoprotein that was first identified as part of a translocated chromosomal fusion product associated with acute promyelocytic leukaemia (APL). PML localises to distinct nuclear multi-protein complexes termed ND10, Kr bodies, PML nuclear bodies and PML oncogenic domains (PODs), which are disrupted in APL and ...
E, Duprez, A J, Saurin, J M, Desterro, V, Lallemand-Breitenbach, K, Howe, M N, Boddy, E, Solomon, H, de Thé, R T, Hay, P S, Freemont   +9 more
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SUMO-1 is Associated with a Subset of Lysosomes in Glial Protein Aggregate Diseases

Neurotoxicity Research, 2012
Oligodendroglial inclusion bodies characterize a subset of neurodegenerative diseases. Multiple system atrophy (MSA) is characterized by α-synuclein glial cytoplasmic inclusions and progressive supranuclear palsy (PSP) is associated with glial tau inclusions.
Wong, Mathew B, Goodwin, Jacob, Norazit, Anwar, Meedeniya, Adrian CB, Richter-Landsberg, Christiane, Gai, Wei Ping, Pountney, Dean L   +6 more
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Heteronuclear nuclear magnetic resonance assignments, structure and dynamics of SUMO-1, a human ubiquitin-like protein

International Journal of Biological Macromolecules, 2001
The structure of a ubiquitin-like protein, small ubiquitin-related modifier-1 (SUMO-1), was earlier determined using homonuclear nuclear magnetic resonance (NMR) spectroscopy, since the spectral quality of the protein was not suitable for heteronuclear NMR data collection.
C, Jin, T, Shiyanova, Z, Shen, X, Liao
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The Vaccinia Virus E3L Protein Interacts with SUMO-1 and Ribosomal Protein L23a in a Yeast Two Hybrid Assay

Virus Genes, 2000
We report the results of a two-hybrid study which identified clones from a HeLa cDNA library that interact with the vaccinia virus protein E3L. These clones encode the nuclear protein SUMO-1 (also known as PIC-1, sentrin or GMP-1); the cytoplasmic ribosomal protein L23a; and a small peptide sequence of unknown significance.
Rogan, S, Heaphy, S
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PIAS proteins are involved in the SUMO-1 modification, intracellular translocation and transcriptional repressive activity of RET finger protein

Experimental Cell Research, 2005
Ret finger protein (RFP) is a nuclear protein that is highly expressed in testis and in various tumor cell lines. RFP functions as a transcriptional repressor and associates with Enhancer of Polycomb 1 (EPC1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex.
Tetsuo, Matsuura, Yohei, Shimono, Kumi, Kawai, Hideki, Murakami, Takeshi, Urano, Yasumasa, Niwa, Hidemi, Goto, Masahide, Takahashi   +7 more
openaire   +2 more sources