PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34970534-1 2021 Lysyl oxidase-like 2 (LOXL2) is a metalloenzyme that catalyzes the oxidative deamination epsilon-amino group of lysine. Lysine 112-118 lysyl oxidase like 2 Homo sapiens 0-20 16096638-4 2005 Snail"s lysine residues 98 and 137 are essential for Snail stability, functional cooperation with LOXL2/3 and induction of EMT. Lysine 8-14 lysyl oxidase like 2 Homo sapiens 98-103 16023247-8 2005 We have found that Loxl2 is able to oxidize lysine residues of collagen, and behaves in that respect similarly to Lox. Lysine 44-50 lysyl oxidase like 2 Homo sapiens 19-24 34970534-1 2021 Lysyl oxidase-like 2 (LOXL2) is a metalloenzyme that catalyzes the oxidative deamination epsilon-amino group of lysine. Lysine 112-118 lysyl oxidase like 2 Homo sapiens 22-27 34944490-2 2021 LOXL2 catalyzes the oxidative deamination of lysine and hydroxylysine residues in extracellular matrix (ECM) proteins to promote crosslinking of these proteins, and thereby plays a major role in ECM remodeling. Lysine 45-51 lysyl oxidase like 2 Homo sapiens 0-5 25254241-1 2014 LOXL2 (lysyl oxidase-like 2), an enzyme that catalyzes oxidative deamination of lysine residue, is upregulated in esophageal squamous cell carcinoma (ESCC). Lysine 80-86 lysyl oxidase like 2 Homo sapiens 0-5 30387148-1 2019 Lysyl oxidase-like 2 (LOXL2) belongs to the family of lysyl oxidases, and as such promotes crosslinking of collagens and elastin by oxidative deamination of lysine residues. Lysine 157-163 lysyl oxidase like 2 Homo sapiens 0-20 30387148-1 2019 Lysyl oxidase-like 2 (LOXL2) belongs to the family of lysyl oxidases, and as such promotes crosslinking of collagens and elastin by oxidative deamination of lysine residues. Lysine 157-163 lysyl oxidase like 2 Homo sapiens 22-27 28872461-6 2017 Mechanistic studies revealed that trihydroxyphenolics induce auto-oxidation of a LOXL2/3-specific lysine (K731) in a time-dependent reaction that irreversibly inhibits LOXL2 and converts the trihydrophenolic to a previously undescribed metabolite that directly inhibits TbetaRI kinase. Lysine 98-104 lysyl oxidase like 2 Homo sapiens 81-86 28872461-6 2017 Mechanistic studies revealed that trihydroxyphenolics induce auto-oxidation of a LOXL2/3-specific lysine (K731) in a time-dependent reaction that irreversibly inhibits LOXL2 and converts the trihydrophenolic to a previously undescribed metabolite that directly inhibits TbetaRI kinase. Lysine 98-104 lysyl oxidase like 2 Homo sapiens 168-173 28670509-6 2015 Mechanistically, hydrogen peroxide is produced as a byproduct of LOXL2 when using an appropriate substrate, lysine. Lysine 108-114 lysyl oxidase like 2 Homo sapiens 65-70 24716982-1 2014 Lysyl oxidase-like 2 (LOXL2), a member of the lysyl oxidase (LOX) family, is a copper-dependent enzyme that catalyzes oxidative deamination of lysine residues on protein substrates. Lysine 143-149 lysyl oxidase like 2 Homo sapiens 0-20 24716982-1 2014 Lysyl oxidase-like 2 (LOXL2), a member of the lysyl oxidase (LOX) family, is a copper-dependent enzyme that catalyzes oxidative deamination of lysine residues on protein substrates. Lysine 143-149 lysyl oxidase like 2 Homo sapiens 22-27 35483499-8 2022 Of these, downregulation of the tumor metastatic microenvironment facilitator LOXL2, a copper-dependent enzyme catalyzing posttranslational oxidative deamination of peptidyl lysine, was of special interest. Lysine 174-180 lysyl oxidase like 2 Homo sapiens 78-83 32801097-1 2020 Lysyl oxidase-like 2 (LOXL2) is a copper-dependent amine oxidase that catalyzes the oxidative deamination of the epsilon-amino group of lysines/hydroxylysines on substrate proteins (collagen and elastin) to form aldehyde groups. Lysine 136-143 lysyl oxidase like 2 Homo sapiens 0-20 32801097-1 2020 Lysyl oxidase-like 2 (LOXL2) is a copper-dependent amine oxidase that catalyzes the oxidative deamination of the epsilon-amino group of lysines/hydroxylysines on substrate proteins (collagen and elastin) to form aldehyde groups. Lysine 136-143 lysyl oxidase like 2 Homo sapiens 22-27 31462706-1 2020 Oxidation of H3 at lysine 4 (H3K4ox) by lysyl oxidase-like 2 (LOXL2) generates an H3 modification with an unknown physiological function. Lysine 19-25 lysyl oxidase like 2 Homo sapiens 40-60 31462706-1 2020 Oxidation of H3 at lysine 4 (H3K4ox) by lysyl oxidase-like 2 (LOXL2) generates an H3 modification with an unknown physiological function. Lysine 19-25 lysyl oxidase like 2 Homo sapiens 62-67 28864775-1 2017 Lysyl oxidase-like-2 (LOXL2) is an enzyme secreted into the extracellular matrix that crosslinks collagens by mediating oxidative deamination of lysine residues. Lysine 145-151 lysyl oxidase like 2 Homo sapiens 0-20 28864775-1 2017 Lysyl oxidase-like-2 (LOXL2) is an enzyme secreted into the extracellular matrix that crosslinks collagens by mediating oxidative deamination of lysine residues. Lysine 145-151 lysyl oxidase like 2 Homo sapiens 22-27 25254241-1 2014 LOXL2 (lysyl oxidase-like 2), an enzyme that catalyzes oxidative deamination of lysine residue, is upregulated in esophageal squamous cell carcinoma (ESCC). Lysine 80-86 lysyl oxidase like 2 Homo sapiens 7-27 22483618-0 2012 Lysyl oxidase-like 2 deaminates lysine 4 in histone H3. Lysine 32-38 lysyl oxidase like 2 Homo sapiens 0-20 24014025-5 2013 Both forms of LOXL2 can oxidize lysine in solution. Lysine 32-38 lysyl oxidase like 2 Homo sapiens 14-19 22578539-2 2012 (2012) demonstrate that LOXL2 deaminates trimethylated histone 3 lysine 4 (H3K4me3), which uncovers a new chromatin modification and a new enzymatic mechanism with the potential to regulate additional lysine residues. Lysine 65-71 lysyl oxidase like 2 Homo sapiens 24-29 22578539-2 2012 (2012) demonstrate that LOXL2 deaminates trimethylated histone 3 lysine 4 (H3K4me3), which uncovers a new chromatin modification and a new enzymatic mechanism with the potential to regulate additional lysine residues. Lysine 201-207 lysyl oxidase like 2 Homo sapiens 24-29 20306300-1 2011 The lysyl oxidase-like 2 (LOXL2) protein is a human paralogue of lysyl oxidase (LOX) that functions as an amine oxidase for formation of lysine-derived cross-links found in collagen and elastin. Lysine 137-143 lysyl oxidase like 2 Homo sapiens 4-24 20306300-1 2011 The lysyl oxidase-like 2 (LOXL2) protein is a human paralogue of lysyl oxidase (LOX) that functions as an amine oxidase for formation of lysine-derived cross-links found in collagen and elastin. Lysine 137-143 lysyl oxidase like 2 Homo sapiens 26-31