PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9085937-2 1997 Thus, the mature IFN-alpha2a protein product is characterized by a lysine residue at position 23 (AAA) and a histidine at position 34 (CAA), IFN-alpha2b has an arginine at position 23 (AGA) and histidine at position 34 (CAT), and IFN-alpha2c has arginine residues at both positions 23 (AGA) and 34 (CGT). Lysine 67-73 interferon alpha 2 Homo sapiens 17-27 9758677-1 1998 Palmitoyl derivatives of interferon alpha2b (p-IFNalpha) were prepared by covalent attachment of the fatty acid to lysine residues in the protein through a reaction with N-hydroxysuccinimide palmitate ester. Lysine 115-121 interferon alpha 2 Homo sapiens 25-43 1692865-4 1990 Although a corresponding sequence of amino acids in the IFN-beta molecule was localized to the region 134-139 and shows only a 66% homology with the assumed IFN-alpha 2 binding site, lysine at position 132 in IFN-alpha 2 and at position 134 in IFN-beta seems to be crucial for establishment of the common epitope. Lysine 183-189 interferon alpha 2 Homo sapiens 157-168 1692865-4 1990 Although a corresponding sequence of amino acids in the IFN-beta molecule was localized to the region 134-139 and shows only a 66% homology with the assumed IFN-alpha 2 binding site, lysine at position 132 in IFN-alpha 2 and at position 134 in IFN-beta seems to be crucial for establishment of the common epitope. Lysine 183-189 interferon alpha 2 Homo sapiens 209-220 20108989-6 2010 The branched, 40 kDa PEG chain of peginterferon-alpha-2a is covalently attached via stable amide bonds to lysine residues of interferon-alpha-2a, and circulates as an intact molecule. Lysine 106-112 interferon alpha 2 Homo sapiens 37-56 34497374-4 2021 In this study, we report that IFN-alpha2b enhances the histone deacetylase 3 (HDAC3)-mediated de-2-hydroxyisobutyrylation of histone H4 lysine 8 (H4K8) on HBV cccDNA minichromosome to restrict the cccDNA transcription in liver. Lysine 136-142 interferon alpha 2 Homo sapiens 30-41 2077397-3 1990 An IFN-alpha analogue in which arginine and lysine residues 121 and 122 were replaced by 2 leucines was generated by site-directed in vitro mutagenesis of the IFN-alpha 4 gene; at equivalent concentrations of antiviral activity, this analogue was 10-fold less effective in NK stimulation. Lysine 44-50 interferon alpha 2 Homo sapiens 3-12 15656592-3 2005 Previous studies showed that it is possible to extend the circulating half-life of IFN-alpha2 by modifying lysine residues of the protein with amine-reactive poly(ethylene glycol) (PEG) reagents. Lysine 107-113 interferon alpha 2 Homo sapiens 83-93 18937499-5 2008 In particular, residue 120 (Arg in IFN-alpha2; Lys in IFN-alpha2/alpha1) appears to be a "hot-spot" residue: substitution by alanine significantly decreased biological activity, and the charge-reversal mutation of residue 120 to Glu caused drastic loss of antiviral and antiproliferative activity for both IFN-alpha2 and IFN-alpha2/alpha1. Lysine 47-50 interferon alpha 2 Homo sapiens 35-45 18937499-5 2008 In particular, residue 120 (Arg in IFN-alpha2; Lys in IFN-alpha2/alpha1) appears to be a "hot-spot" residue: substitution by alanine significantly decreased biological activity, and the charge-reversal mutation of residue 120 to Glu caused drastic loss of antiviral and antiproliferative activity for both IFN-alpha2 and IFN-alpha2/alpha1. Lysine 47-50 interferon alpha 2 Homo sapiens 54-64 18937499-5 2008 In particular, residue 120 (Arg in IFN-alpha2; Lys in IFN-alpha2/alpha1) appears to be a "hot-spot" residue: substitution by alanine significantly decreased biological activity, and the charge-reversal mutation of residue 120 to Glu caused drastic loss of antiviral and antiproliferative activity for both IFN-alpha2 and IFN-alpha2/alpha1. Lysine 47-50 interferon alpha 2 Homo sapiens 54-64 18937499-5 2008 In particular, residue 120 (Arg in IFN-alpha2; Lys in IFN-alpha2/alpha1) appears to be a "hot-spot" residue: substitution by alanine significantly decreased biological activity, and the charge-reversal mutation of residue 120 to Glu caused drastic loss of antiviral and antiproliferative activity for both IFN-alpha2 and IFN-alpha2/alpha1. Lysine 47-50 interferon alpha 2 Homo sapiens 54-64 18020402-3 2008 It is possible to extend the circulating half-life of IFN-alpha2 by random modification of lysine residues in the protein with polyethylene glycol (PEG); however, such preparations have heterogeneous structures and low specific activities, and may not provide optimal therapeutic benefits to patients. Lysine 91-97 interferon alpha 2 Homo sapiens 54-64 15656592-4 2005 However, amine-PEGylated IFN-alpha2 comprises a heterogeneous product mixture with low specific activity due to the large number and critical locations of lysine residues in IFN-alpha2. Lysine 155-161 interferon alpha 2 Homo sapiens 25-35 15656592-4 2005 However, amine-PEGylated IFN-alpha2 comprises a heterogeneous product mixture with low specific activity due to the large number and critical locations of lysine residues in IFN-alpha2. Lysine 155-161 interferon alpha 2 Homo sapiens 174-184 15646642-7 2004 Interferon alpha-2a is monopegylated at four major positional lysine (Lys) residues. Lysine 62-68 interferon alpha 2 Homo sapiens 0-19 15646642-7 2004 Interferon alpha-2a is monopegylated at four major positional lysine (Lys) residues. Lysine 70-73 interferon alpha 2 Homo sapiens 0-19