Author pages are created from data sourced from our academic publisher partnerships and public sources.
- Publications
- Influence
Insights into E3 ligase activity revealed by a SUMO–RanGAP1–Ubc9–Nup358 complex
- D. Reverter, C. D. Lima
- Physics, Medicine
- Nature
- 2 June 2005
SUMO-1 (for small ubiquitin-related modifier) belongs to the ubiquitin (Ub) and ubiquitin-like (Ubl) protein family. SUMO conjugation occurs on specific lysine residues within protein targets,… Expand
A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex.
- D. Reverter, C. D. Lima
- Biology, Medicine
- Structure
- 1 August 2004
Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear metabolism and cell cycle progression in yeast. X-ray structures of the human Senp2 catalytic protease… Expand
Structure of the Human SENP7 Catalytic Domain and Poly-SUMO Deconjugation Activities for SENP6 and SENP7*
- C. D. Lima, D. Reverter
- Biology, Medicine
- Journal of Biological Chemistry
- 14 November 2008
Small ubiquitin-like modifier (SUMO) proteases regulate the abundance and lifetime of SUMO-conjugated substrates by antagonizing reactions catalyzed by SUMO-conjugating enzymes. Six SUMO proteases… Expand
Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates
- D. Reverter, C. D. Lima
- Chemistry, Medicine
- Nature Structural &Molecular Biology
- 12 November 2006
SUMO processing and deconjugation are essential proteolytic activities for nuclear metabolism and cell-cycle progression in yeast and higher eukaryotes. To elucidate the mechanisms used during… Expand
SUMO-2 and PIAS1 Modulate Insoluble Mutant Huntingtin Protein Accumulation
- J. O’Rourke, Jaclyn R. Gareau, +21 authors L. Thompson
- Biology, Medicine
- Cell reports
- 18 July 2013
SUMMARY A key feature in Huntington disease (HD) is the accumulation of mutant Huntingtin (HTT) protein, which may be regulated by posttranslational modifications. Here, we define the primary sites… Expand
Determinants of Small Ubiquitin-like Modifier 1 (SUMO1) Protein Specificity, E3 Ligase, and SUMO-RanGAP1 Binding Activities of Nucleoporin RanBP2*
- Jaclyn R. Gareau, D. Reverter, C. D. Lima
- Biology, Medicine
- The Journal of Biological Chemistry
- 22 December 2011
Background: The RanBP2 internal repeat domain (IR1-M-IR2) catalyzes SUMO E3 ligase activity and binds SUMO1-RanGAP1/UBC9 at the nuclear pore complex. Results: Biochemistry and structures of… Expand
The structure of calcium-free human m-calpain: implications for calcium activation and function.
- D. Reverter, H. Sorimachi, W. Bode
- Chemistry, Medicine
- Trends in cardiovascular medicine
- 1 August 2001
The calpains form a growing family of structurally related intracellular multidomain cysteine proteinases containing a papain-related catalytic domain, whose activity depends on calcium. The calpains… Expand
Specific and Covalent Targeting of Conjugating and Deconjugating Enzymes of Ubiquitin-Like Proteins
- J. Hemelaar, A. Borodovsky, +9 authors H. Ovaa
- Biology, Medicine
- Molecular and Cellular Biology
- 1 January 2004
ABSTRACT Modification of proteins by ubiquitin (Ub)-like proteins (UBLs) plays an important role in many cellular processes, including cell cycle progression, nuclear transport, and autophagy.… Expand
Overexpression of Human Procarboxypeptidase A2 in Pichia pastoris and Detailed Characterization of Its Activation Pathway*
- D. Reverter, S. Ventura, V. Villegas, J. Vendrell, F. Avilés
- Biology, Medicine
- The Journal of Biological Chemistry
- 6 February 1998
The cDNA of human procarboxypeptidase A2 has been overexpressed in the methylotrophic yeastPichia pastoris and secreted into the culture medium by means of the α-mating factor signal sequence,… Expand
The three‐dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen
- I. Garcia-Saez, D. Reverter, J. Vendrell, F. Avilés, M. Coll
- Biology, Medicine
- The EMBO journal
- 1 December 1997
The three‐dimensional structure of human procarboxypeptidase A2 has been determined using X‐ray crystallography at 1.8 Å resolution. This is the first detailed structural report of a human pancreatic… Expand