Results 21 to 30 of about 31,654 (255)
Toxins, 2016 Endoglin (CD105) is an accessory component of the TGF-β receptor complex, which is expressed in a number of tissues and over-expressed in the endothelial cells of tumor neovasculature.
Begoña Barriuso +7 more
doaj +1 more source
Extensive evolution of cereal ribosome-inactivating proteins translates into unique structural features, activation mechanisms, and physiological roles [PDF]
, 2017 Ribosome-inactivating proteins (RIPs) are a class of cytotoxic enzymes that can depurinate rRNAs thereby inhibiting protein translation. Although these proteins have also been detected in bacteria, fungi, and even some insects, they are especially ...
De Zaeytijd, Jeroen, Van Damme, Els
core +2 more sources
British Journal of Haematology, 2000 Immunotoxins specific for the CD80 and CD86 antigens were prepared by linking three type 1 ribosome‐inactivating proteins (RIPs), namely bouganin, gelonin and saporin‐S6, to the monoclonal antibodies M24 (anti‐CD80) and 1G10 (anti‐CD86). These immunotoxins showed a specific cytotoxicity for the CD80/CD86‐expressing cell lines Raji and L428.
A. Bolognesi +8 more
semanticscholar +4 more sources
Acta Pharmaceutica Sinica B, 2020 Ricin is a highly toxic type 2 ribosome-inactivating protein (RIP) which is extracted from the seeds of castor beans. Ricin is considered a potential bioterror agent and no effective antidote for ricin exists so far.
Xu Zhao +7 more
doaj +1 more source
Ribosome-Inactivating and Related Proteins
Toxins, 2015 Ribosome-inactivating proteins (RIPs) are toxins that act as N-glycosidases (EC 3.2.2.22). They are mainly produced by plants and classified as type 1 RIPs and type 2 RIPs.
Joachim Schrot +2 more
doaj +1 more source
Evolution of plant ribosome-inactivating proteins [PDF]
, 2010 This contribution presents an updated analysis of the evolution of ribosome-inactivating proteins (RIPs) in plants. All evidence suggests that an ancestor of modern seed plants developed the RIP domain at least 300 million years ago.
Peumans, Willy J, Van Damme, Els
core +1 more source
Identification of the catalytic motif of the microbial ribosome inactivating cytotoxin colicin E3 [PDF]
, 2004 Colicin E3 is a cytotoxic ribonuclease that specifically cleaves 16S rRNA at the ribosomal A-site to abolish protein synthesis in sensitive Escherichia coli cells.
Bohm +30 more
core +2 more sources
X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein [PDF]
BMC Structural Biology, 2007 Abstract Background Protein sequence can be obtained through Edman degradation, mass spectrometry, or cDNA sequencing. High resolution X-ray crystallography can also be used to derive protein sequence information, but faces the difficulty in distinguishing the Asp/Asn, Glu/Gln, and Val/Thr pairs. Luffaculin 1 is a new
Hou, Xiaomin +5 more
openaire +2 more sources
Structural and Functional Investigation and Pharmacological Mechanism of Trichosanthin, a Type 1 Ribosome-Inactivating Protein [PDF]
Toxins, 2018 Trichosanthin (TCS) is an RNA N-glycosidase that depurinates adenine-4324 in the conserved α-sarcin/ricin loop (α-SRL) of rat 28 S ribosomal RNA (rRNA). TCS has only one chain, and is classified as type 1 ribosome-inactivating protein (RIP). Our structural studies revealed that TCS consists of two domains, with five conserved catalytic residues Tyr70 ...
Wei-Wei Shi, Kam-Bo Wong, Pang-Chui Shaw
openaire +3 more sources
Immunotoxins and Other Conjugates Containing Saporin-S6 for Cancer Therapy
Toxins, 2011 Ribosome-inactivating proteins (RIPs) are a family of plant toxins that permanently damage ribosomes and possibly other cellular substrates, thus causing cell death.
Andrea Bolognesi +3 more
doaj +1 more source