Results 201 to 210 of about 13,489 (251)

POEMS Syndrome: 2026 Update on Diagnosis, Risk‐Stratification, and Management

American Journal of Hematology, EarlyView.
ABSTRACT Disease Overview POEMS syndrome is a life‐threatening syndrome due to an underlying plasma cell neoplasm. The major criteria for the syndrome are polyneuropathy, clonal plasma cell disorder (PCD), sclerotic bone lesions, elevated vascular endothelial growth factor, and the presence of Castleman disease.
Angela Dispenzieri
wiley   +1 more source

Cardiovascular Toxicity Associated With Bispecific Antibodies in Hematological Malignancies: A Comprehensive Pharmacovigilance Analysis

American Journal of Hematology, EarlyView.
ABSTRACT Cardiovascular adverse events (CVAEs) associated with bispecific T‐cell engaging antibodies (BsAbs) have not been systematically investigated across approved agents. In this disproportionality analysis of FAERS (December 2014–September 2025), reports listing BsAbs as the primary suspected drug (n = 7647) were compared with all other drugs in ...
Malak Munir, Ahmed Sayed, Dae Hyun Lee, Sanam Ghazi, Mustafa M. Houmsse, Saad Badat, Abdul Moeed, Avirup Guha, Daniel Addison, Narendranath Epperla   +9 more
wiley   +1 more source

Effectiveness of intermittent hypoxia on muscle recovery in rats: A systematic review

Animal Models and Experimental Medicine, EarlyView.
This systematic review of animal studies evaluated intermittent hypobaric hypoxia (IHH), cold exposure, and their combinations, with or without exercise, on skeletal muscle recovery. IHH enhanced muscle regeneration, reduced fibrosis, improved contractile force, and maintained oxidative capacity, while cold exposure increased mitochondrial activity but
Sebastian Philippe Hansen Quiblier, María García‐Arrabé, Diego Domínguez‐Balmaseda, Guillermo García‐Pérez‐de‐Sevilla   +3 more
wiley   +1 more source

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20S proteasome biogenesis

Biochimie, 2001
26S proteasomes are multi-subunit protease complexes responsible for the turnover of short-lived proteins. Proteasomal degradation starts with the autocatalytic maturation of the 20S core particle. Here, we summarize different models of proteasome assembly.
E, Krüger, P M, Kloetzel, C, Enenkel
openaire   +2 more sources

Autocatalytic processing of the 20S proteasome

Nature, 1996
The Ntn (N-terminal nucleophile) hydrolases are enzymes with an unusual four-layer alpha + beta fold. The amino-terminal residue (cysteine, serine or threonine) of the mature protein is the catalytic nucleophile, and its side chain is activated for nucleophilic attack by transfer of its proton to the free N terminus, although other active-site residues
Seemüller, E., Lupas, A. ; https://orcid.org/0000-0002-1959-4836, Baumeister, W.   +2 more
openaire   +4 more sources

In vitro Activation of the 20S Proteasome

Enzyme and Protein, 2017
The effect of chemical compounds like sodium dodecyl sulfate (SDS), fatty acid esters of glycerol, carnitine and coenzyme A, phospholipids, histones, polylysines as well as homobifunctional chemical cross-linkers on the various proteolytic activities of mammalian proteasomes have been tested. Most of the reagents enhance these activities, and some, e.g.
B, Dahlmann, B, Becher, A, Sobek, C, Ehlers, F, Kopp, L, Kuehn   +5 more
openaire   +2 more sources

Purification of 20S Proteasomes

2003
Proteasomes are large multicatalytic proteinases located in the nuclei and cytoplasm of all eukaryotic cells. Proteasomes are composed of four heptameric rings stacked to form a hollow cylinder (length 16–20 nm, diameter 11–12 nm). The outer two rings are composed of α-subunits, while β-subunits, which contain the active sites, comprise the inner two ...
J R, Beyette, T, Hubbell, J J, Monaco
openaire   +2 more sources

Structure and assembly of the 20S proteasome

Cellular and Molecular Life Sciences CMLS, 1998
The barrel-shaped 20S proteasome is one of the two components of a larger 26S particle, the multicatalytic 2000-kDa protease complex. The proteolytic sites are located in the inner chamber of the 20S particle and are only accessible via narrow entrances.
W L, Gerards, W W, de Jong, W, Boelens, H, Bloemendal   +3 more
openaire   +2 more sources

Purification of the Eukaryotic 20S Proteasome

Current Protocols in Protein Science, 2001
AbstractThe 20S proteasome is the catalytic core of the major extralysosomal proteolytic system of the cell. Combination of the 20S proteasome with a complex of regulatory proteins forms the 26S proteasome, which in turn is responsible for the recognition and degradation of ubiquitin‐protein conjugates.
S, Wilk, W E, Chen
openaire   +2 more sources

Structural Features of 26S and 20S Proteasomes

Enzyme and Protein, 2017
The 26S proteasome is the central protease of the ubiquitindependent pathway of protein degradation and has a highly conserved structure from slime molds to humans. The elongated molecule which has a molecular mass of approximately 2,000 kD is formed by a barrel-shaped 20S core complex and two polar 19S complexes. The 20S complex has C2 symmetry and is
Lupas, A. ; https://orcid.org/0000-0002-1959-4836, Koster, A., Baumeister, W.   +2 more
openaire   +4 more sources