3.2.2.22 ? x * 13000, SDS-PAGE 749545 3.2.2.22 ? x * 13000, SDS-PAGE, x * 10964.6, mass spectrometry 710473 3.2.2.22 ? x * 26000, SDS-PAGE 666621 3.2.2.22 ? x * 27000, SDS-PAGE 715779, 749545 3.2.2.22 ? x * 28000, A chain, + x * 29000, B chain, SDS-PAGE 684025 3.2.2.22 ? x * 28000, SDS-PAGE 731115 3.2.2.22 ? x * 28000, subunit A1, SDS-PAGE 732120 3.2.2.22 ? x * 29000, A chain, + x * 28000, B chain, SDS-PAGE 683912 3.2.2.22 ? x * 29000, SDS-PAGE 731196 3.2.2.22 ? x * 29094, calculated from amino acid sequence 731196 3.2.2.22 ? x * 29310, MALDI-TOF, recombinant protein 750789 3.2.2.22 ? x * 29770, calculated from sequence 749801 3.2.2.22 ? x * 30000, SDS-PAGE 683792, 701053, 706937, 731333 3.2.2.22 ? x * 30000-35000, recombinant SNA-I, SNA-IV, SNA-V, and SNLRP, SDS-PAGE 664818 3.2.2.22 ? x * 32000, SDS-PAGE 731786 3.2.2.22 ? x * 32500, mature enzyme, SDS-PAGE 716963 3.2.2.22 ? x * 35000, precursor, SDS-PAGE 716963 3.2.2.22 ? x * 36000 714784 3.2.2.22 ? x * 36000, SDS-PAGE 749545 3.2.2.22 ? x * 61000, SDS-PAGE 749545 3.2.2.22 ? x * 62912, MALDI-TOF mass spectrometry 732952 3.2.2.22 ? x * 62925, MALDI-TOF 683403 3.2.2.22 dimer - 664562 3.2.2.22 dimer (alphabeta) structure 664166 3.2.2.22 dimer 1 * 21000, SDS-PAGE 646927 3.2.2.22 dimer 1 * 27000 + 1 * 33000, SDS-PAGE 646908 3.2.2.22 dimer 1 * 28478, ML-I subunit A + 1 * 28981, ML-I subunits B, sequence calculation 664027 3.2.2.22 dimer 1 * 29000, A-chain, + 1 * 32000, B-chain, SDS-PAGE 664265 3.2.2.22 dimer 1 * 30000, recombinant B-subunit, the enzyme forms a heterodimer comprising subunits A and B, the latter is the carbohydrate-binding subunit 664168 3.2.2.22 dimer 1 * 30500 + 1 * 33500, A-chain and B-chain, SDS-PAGE 646905 3.2.2.22 dimer 1 * 30500 + 1 * 34500, cinnamomin, A- and B-chain, SDS-PAGE 646911, 646922 3.2.2.22 dimer 1 * 33000 + 1 * 30000, cinnamomin, SDS-PAGE 646902 3.2.2.22 dimer 2 * 30000, recombinant abricin A-chain, SDS-PAGE 664245 3.2.2.22 dimer heterodimer formed by a catalytic subunit A and a carbohydrate binding subunit B 664034, 664150, 664730, 666379 3.2.2.22 dimer heterodimer formed by a catalytic subunit A, RTA and a carbohydrate binding subunit B, RTB 664819 3.2.2.22 dimer heterodimer formed by a catalytic subunit A, RTA, and a carbohydrate binding subunit B, RTB 664033, 664103, 664730, 665780 3.2.2.22 dimer heterodimer formed by a catalytic subunit A, the A-chain, and a carbohydrate binding subunit B, the B-chain 663782 3.2.2.22 dimer heterodimer, subunits A and B, RTA and RTB, are derived from a single precursor protein, structure comparison and analysis 664180 3.2.2.22 dimer subunit A and subunit B connected by a disulfide bridge 666976 3.2.2.22 dimer type III RIP isozyme RIP1 forms dimers and ressembles type II RIPs concerning its subunit structure 665864 3.2.2.22 dimer type III RIP isozyme RIP2 forms dimers and ressembles type II RIPs concerning its subunit structure 665864 3.2.2.22 heterodimer 1 * 29000 + 1 * 31000, SDS-PAGE 731509 3.2.2.22 heterodimer 1 * 40000 + 1 * 22000, chain B and chain A, SDS-PAGE -, 716962 3.2.2.22 monomer - 664089, 666818 3.2.2.22 monomer 1 * 10000, SDS-PAGE 695817 3.2.2.22 monomer 1 * 22500, camphorin, SDS-PAGE 646902 3.2.2.22 monomer 1 * 25000, SDS-PAGE 751814 3.2.2.22 monomer 1 * 27000, SDS-PAGE 646919 3.2.2.22 monomer 1 * 27700, SDS-PAGE 646900 3.2.2.22 monomer 1 * 28000, SDS-PAGE 683218 3.2.2.22 monomer 1 * 30200, SDS-PAGE 646900 3.2.2.22 monomer 1 * 30200, SO-R1, SDS-PAGE 646899 3.2.2.22 monomer 1 * 30200-31600, 7 major saporins, SDS-PAGE 646899 3.2.2.22 monomer 1 * 30700, momorchochin-S, SDS-PAGE 646897 3.2.2.22 monomer 1 * 30900, SO-R2, SO-R3, and SO-S%, SDS-PAGE 646899 3.2.2.22 monomer 1 * 31600, SO-L1, SO-L2, and SO-S6, SDS-PAGE 646899 3.2.2.22 monomer 1 * 35000, SDS-PAGE, 1 * 34600, calculated for mature protein, 1 * 62000, calculated for full-length protein including N-terminal leader sequence, pectin methylesterase inhibitor domain, pectin esterase domain and pectin esterase signature sequences 1 and 2 683188 3.2.2.22 monomer subunit A 666976 3.2.2.22 additional information 2 domains connected by a covalent linker 666976 3.2.2.22 additional information amino acid sequence analysis and comparison with other toxin sequences, overview 664168 3.2.2.22 additional information analysis of amino acid composition of A and B chain. The total helical content of ricin is 53.6% 683912 3.2.2.22 additional information comparison of binding properties of ricin B chain toward different mono- and disaccharide ligands, calculation of free energies of binding and analysis of epimeric specificity of the protein 683263 3.2.2.22 additional information isozyme structure analysis by ESI/Q-TOF mass spectrometric and circular dichroism analysis, structure-function relationship, influence of carbohydrate moieties, overview 709896 3.2.2.22 additional information MOD structure determination and comparison using the crystal structure of DELTAN5-MOD, PDB ID 2PQI, and by determination of the NMR solution structure of MOD, PDB ID 2k6H, detailed overview. MOD has shorter beta6 and alphaB segments, probably for accommodating easier substrate binding, and an alpha-helix instead of an antiparallel beta-sheet in the C-terminal domain, which is involved in binding ribosomal protein P2 in some RIPs, compared to type I and II RIPs. The P2 binding site on MOD is located at the N-terminal domain near the internal inactivation region 709537 3.2.2.22 additional information overall enzyme structure, overview 666675 3.2.2.22 additional information ricin interacts with the ER degradation enhancing alpha-mannosidase I-like protein EDEM responsible for redirecting aberrant proteins for ER-associated protein degradation and with Sec61alpha, and both kifunensin and puromycin enhance these interactions. Overexpression of EDEM strongly protects against ricin. In presence of kifunensin, EDEM promotes retranslocation of ricin from the ER to the cytosol 683859 3.2.2.22 additional information structure comparison and analysis 664180 3.2.2.22 additional information structure modeling of ME1 666826 3.2.2.22 additional information the 5'-flanking regions of the isozymes contains functional motifs involved in e.g. plant defense in SoRIP2 and with functions related to embryonic development in SoRIP1, overview 710293 3.2.2.22 additional information the A-chain exhibits the RNA N-glycosidase activity, while the B-chain mediates cell entry by binding to the target cell surface glycolipid receptor 664245 3.2.2.22 additional information the A1 chain of shiga-like toxin 1 binds to the human ribosomal proteins P0, P1, and P2. Removal of the C-terminal 17 amino acids of either protein P1 or P2 abolishes the interaction, whereas P0 still binds to the A1 domain even without its C-terminus 683786 3.2.2.22 additional information the heterodimeric enzyme consists of the catalytic ricin A chain, RTA, and the cabohydrate-binding B chain, RTB 666993 3.2.2.22 additional information the N-terminal amino acid sequence of the enzyme is identical with that of several superoxide dimutases 666621 3.2.2.22 additional information trichosanthin interacts with the C-terminal tail of eukaryotic ribosomal protein P2, involving residues K173, R174, and K177 of trichosanthin 683935 3.2.2.22 additional information tryptic peptides mapping, overview 710473 3.2.2.22 additional information volkensin binds strongly to asialofetuin, but does not show any affnity to fetuin, carboxypeptidase Y and transferrin 684025 3.2.2.22 pentamer one of two Stx liberated by Stx-producing Escherichia coli is composed of an A subunit monomer and a B subunit pentamer 707883 3.2.2.22 pentamer StxB 664166 3.2.2.22 polymer - 646930 3.2.2.22 tetramer - 731382