PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23523789-6 2013 Importantly, we showed that the closely spaced N-terminal cysteine residues of Id3 interacted with the arsenic derivative phenylarsine oxide (PAO) and were essential for the arsenite-induced cytoplasmic accumulation, suggesting that arsenite induces the CRM1-dependent nuclear export of Id3 via binding to the N-terminal cysteines. Cysteine 58-66 exportin 1 Homo sapiens 254-258 12374846-8 2002 In addition, we prove that the inhibition is through direct interaction of the compound with Cys-539 of CRM1. Cysteine 93-96 exportin 1 Homo sapiens 104-108 28467801-3 2017 Selinexor forms a covalent bond with exportin-1 at cysteine-528, and blocks its ability to export cargos. Cysteine 51-59 exportin 1 Homo sapiens 37-47 27634897-6 2016 However, introduction of a homozygous mutation at the drug"s target site, the cysteine 528 residue inside the XPO1 cargo-binding pocket, by genetic engineering, confers resistance to selinexor. Cysteine 78-86 exportin 1 Homo sapiens 110-114 25579209-6 2015 These results validate XPO1 as the prime target of selinexor in cells and identify the selectivity of this drug toward the cysteine 528 residue of XPO1. Cysteine 123-131 exportin 1 Homo sapiens 147-151 15574331-4 2004 Residues critical for NES recognition are identified adjacent to the cysteine residue targeted by leptomycin B (LMB), a specific CRM1 inhibitor. Cysteine 69-77 exportin 1 Homo sapiens 129-133 10430904-0 1999 Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region. Cysteine 71-79 exportin 1 Homo sapiens 25-29 10430904-7 1999 Inhibition by N-ethylmaleimide (NEM), an alkylating agent, of CRM1-mediated nuclear export probably was caused by covalent binding of the electrophilic structure in NEM to the sulfhydryl group of Cys-529, because the crm1-K1 mutant showed the normal rate for the export of Rev nuclear export signal-bearing proteins in the presence of not only LMB but also NEM. Cysteine 196-199 exportin 1 Homo sapiens 62-66 10430904-7 1999 Inhibition by N-ethylmaleimide (NEM), an alkylating agent, of CRM1-mediated nuclear export probably was caused by covalent binding of the electrophilic structure in NEM to the sulfhydryl group of Cys-529, because the crm1-K1 mutant showed the normal rate for the export of Rev nuclear export signal-bearing proteins in the presence of not only LMB but also NEM. Cysteine 196-199 exportin 1 Homo sapiens 217-221 10430904-8 1999 These results show that the single cysteine residue determines LMB sensitivity and is selectively alkylated by LMB, leading to CRM1 inactivation. Cysteine 35-43 exportin 1 Homo sapiens 127-131 33682791-2 2021 Structural analysis of several inhibitor compounds bound to CRM1 revealed that their mechanism of action relies on the covalent modification of a critical cysteine residue (Cys528 in the human receptor) located in the nuclear export signal-binding cleft. Cysteine 155-163 exportin 1 Homo sapiens 60-64 28412356-2 2017 Leptomycin B (LMB), the first specific inhibitor of CRM1 identified, binds covalently to cysteine 528 in the nuclear export signal binding region of CRM1 leading to the inhibition of protein nuclear export. Cysteine 89-97 exportin 1 Homo sapiens 52-56 28412356-2 2017 Leptomycin B (LMB), the first specific inhibitor of CRM1 identified, binds covalently to cysteine 528 in the nuclear export signal binding region of CRM1 leading to the inhibition of protein nuclear export. Cysteine 89-97 exportin 1 Homo sapiens 149-153 26654943-1 2016 Selective Inhibitor of Nuclear Export (SINE) compounds are a family of small-molecules that inhibit nuclear export through covalent binding to cysteine 528 (Cys528) in the cargo-binding pocket of Exportin 1 (XPO1/CRM1) and promote cancer cell death. Cysteine 143-151 exportin 1 Homo sapiens 196-206 26654943-1 2016 Selective Inhibitor of Nuclear Export (SINE) compounds are a family of small-molecules that inhibit nuclear export through covalent binding to cysteine 528 (Cys528) in the cargo-binding pocket of Exportin 1 (XPO1/CRM1) and promote cancer cell death. Cysteine 143-151 exportin 1 Homo sapiens 208-212 26654943-1 2016 Selective Inhibitor of Nuclear Export (SINE) compounds are a family of small-molecules that inhibit nuclear export through covalent binding to cysteine 528 (Cys528) in the cargo-binding pocket of Exportin 1 (XPO1/CRM1) and promote cancer cell death. Cysteine 143-151 exportin 1 Homo sapiens 213-217 20457605-3 2010 Like leptomycin B (LMB), an established fungal CRM1-inhibitor, 15d-PGJ(2) reacts with a conserved cysteine residue in the CRM1 sequence. Cysteine 98-106 exportin 1 Homo sapiens 47-51 20457605-3 2010 Like leptomycin B (LMB), an established fungal CRM1-inhibitor, 15d-PGJ(2) reacts with a conserved cysteine residue in the CRM1 sequence. Cysteine 98-106 exportin 1 Homo sapiens 122-126 19812309-5 2009 Analysis by mass spectrometry and involving the use of S-nitrosylation mimetic mutations indicated that modification at either of two specific cysteines of CRM1 was sufficient to abolish the CRM1-NES association. Cysteine 143-152 exportin 1 Homo sapiens 156-160 19812309-5 2009 Analysis by mass spectrometry and involving the use of S-nitrosylation mimetic mutations indicated that modification at either of two specific cysteines of CRM1 was sufficient to abolish the CRM1-NES association. Cysteine 143-152 exportin 1 Homo sapiens 191-195