Results 261 to 270 of about 54,326 (298)

SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins

Journal of Structural and Functional Genomics, 2004
SUMO (small ubiquitin-related modifier) modulates protein structure and function by covalently binding to the lysine side chains of the target proteins. Yeast cells contain two SUMO proteases, Ulp1 and Ulp2, that cleave sumoylated proteins in the cell.
Michael P, Malakhov, Michael R, Mattern, Oxana A, Malakhova, Mark, Drinker, Stephen D, Weeks, Tauseef R, Butt   +5 more
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PIAS proteins: pleiotropic interactors associated with SUMO

Cellular and Molecular Life Sciences, 2009
The interactions and functions of protein inhibitors of activated STAT (PIAS) proteins are not restricted to the signal transducers and activators of transcription (STATs), but PIAS1, -2, -3 and -4 interact with and regulate a variety of distinct proteins, especially transcription factors. Although the majority of PIAS-interacting proteins are prone to
Miia M, Rytinki, Sanna, Kaikkonen, Petri, Pehkonen, Tiina, Jääskeläinen, Jorma J, Palvimo   +4 more
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The SUMO activating enzyme subunit, SAE2, contributes SUMO protein bias for mitotic fidelity

2022
Abstract Mammalian cells possess three conjugatable SUMO variants: SUMO1 and the largely indistinguishable SUMO2 and SUMO3 (designated SUMO2/3). Some SUMOylated substrates are modified by both SUMO1 and SUMO2/3, while others show biased modifications towards SUMO1 or SUMO2/3.
Alexandra K. Walker, Alexander J. Lanz, Mohammed Jamshad, Alexander J. Garvin, Peter Wotherspoon, Benjamin F. Cooper, Timothy J. Knowles, Joanna R. Morris   +7 more
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Protein Complexes in SUMO Signaling

2007
SUMO is a small ubiquitin-related modifier implicated in control of various cellular processes including gene transcription, cell cycle, DNA repair and apoptosis. Here we describe details of the SUMO molecular machineries implicated in the formation of signaling networks that underlie the specificity in these biological processes.
Christina-Maria Hecker, Ivan Dikic
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Abstract 2184: SUMO-binding proteins as effectors and regulators of SUMO modification

Cancer Research, 2010
Abstract SUMOs (Small Ubiquitin-related Modifiers) are reversibly conjugated to other proteins in the cell, thereby regulating a wide range of essential functions. Many of the functions regulated by SUMOylation are intimately tied to processes directly relevant to cancer, including maintenance of genome integrity and cell cycle ...
Catherine M. Guzzo, Ijeoma Uzoma, Heng Zhu, Eric Cox, Seth Blackshaw, Michael J. Matunis   +5 more
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Abstract B69: SUMO-binding proteins as effectors and regulators of SUMO modification

Cancer Research, 2009
Abstract SUMOs (Small Ubiquitin-related Modifiers) are reversibly conjugated to other proteins in the cell, thereby regulating a wide range of essential functions. Many of the functions regulated by SUMOylation are intimately tied to processes directly relevant to cancer, including maintenance of genome integrity and cell cycle ...
Catherine M. Guzzo, Ijeoma Uzoma, Heng Zhu, Eric Cox, Seth Blackshaw, Michael J. Matunis   +5 more
openaire   +1 more source

Identification of SUMO Target Proteins by Quantitative Proteomics

2009
The identification of target proteins for small ubiquitin-like modifiers (SUMOs) is a critical step towards a detailed understanding of the cellular functions of SUMOs. Substrate protein identification for SUMOs is hampered by the low abundance of SUMO targets, the finding that only a small fraction of these target proteins is sumoylated, and the high ...
Andersen, Jens S, Matic, Ivan, Vertegaal, Alfred C O   +2 more
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SUMO as a Solubility Tag and In Vivo Cleavage of SUMO Fusion Proteins with Ulp1

2014
Expression of proteins in E. coli is often plagued by insolubility of the protein of interest. A solution to this problem is the expression of proteins as fusions to solubility tags such as the SUMO protein. SUMO fusion proteins can be cleaved to remove the SUMO moiety using SUMO-specific proteases such as Ulp1. Here, we describe the use of vectors for
Dennis, Kuo, Minghua, Nie, Albert J, Courey   +2 more
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Identification of SUMO-Conjugated Proteins and their SUMO Attachment Sites Using Proteomic Mass Spectrometry

2009
The covalent modification of cellular factors by the small ubiquitin-like modifier (SUMO) has emerged as a key regulatory pathway for many biological processes. One recent advance in the field of SUMO modification that has provided important insights into SUMO-mediated regulatory networks is the ability to use proteomic mass spectrometry to identify ...
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SUMO modification of proteins other than transcription factors

Seminars in Cell & Developmental Biology, 2004
A wide range of eukaryotic proteins has been shown to be sumoylated. Most, but not all of these proteins are nuclear. In all cases documented so far, sumoylation has been shown to occur on lysine residues. In general these are located within the consensus sequence psiKxE, although there are some exceptions to this.
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