Anticancer potentiality and mode of action of low-carbohydrate proteins and peptides from mushrooms
Severe side effects of chemotherapy as well as drug resistance highlight the ongoing need to discover novel natural bioactive compounds with anticancer potentiality. Mushroom-derived proteins are among the naturally occurring compounds that have been the subject of a body of research on their potent...
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| Published in | Applied microbiology and biotechnology Vol. 104; no. 16; pp. 6855 - 6871 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Berlin/Heidelberg
Springer Berlin Heidelberg
01.08.2020
Springer Springer Nature B.V |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Severe side effects of chemotherapy as well as drug resistance highlight the ongoing need to discover novel natural bioactive compounds with anticancer potentiality. Mushroom-derived proteins are among the naturally occurring compounds that have been the subject of a body of research on their potentiality in cancer therapy. The greatest attention in relevant review articles has been paid to well-known mushroom-derived glycoproteins such as lectins and protein-bound polysaccharide complexes such as polysaccharide-K (PSK) or krestin and polysaccharopeptide (PSP), which contain substantial amounts of carbohydrates (50–90%). These complex compounds exert their anticancer activity mainly by binding to cell membranes leading to extrinsic (death receptor) apoptosis or intrinsic (mitochondrial) apoptotic pathways. However, several other research studies have reported pure, well-characterized, proteins or peptides from mushrooms, which are carbohydrate-free or have very low amounts of carbohydrate. These proteins may fall into four categories including fungal immunomodulatory proteins, ubiquitin-like proteins, enzymes, and unclassified proteins. Well-defined chemical structure, elucidated full amino acid or N-terminal sequences, purity, and having some distinct and specific pathways compared to glycoproteins have made these low-carbohydrate proteins attractive for cancer research. The aim of this review was therefore to improve the current understanding of mushroom-derived low-carbohydrate proteins and to consolidate the existing knowledge of the most promising mushroom species from which low-carbohydrate proteins have been derived, characterized, and examined for their anticancer activity. In addition, molecular targets and mechanisms of action of these proteins have been discussed.
Key points
• Mushroom-derived
low-carbohydrate
proteins lack or have low carbohydrate.
• Low-carbohydrate proteins show potent anticancer activities in vitro and in vivo.
• There are specific pathways for low-carbohydrate proteins to inhibit cancer cells
. |
|---|---|
| AbstractList | Severe side effects of chemotherapy as well as drug resistance highlight the ongoing need to discover novel natural bioactive compounds with anticancer potentiality. Mushroom-derived proteins are among the naturally occurring compounds that have been the subject of a body of research on their potentiality in cancer therapy. The greatest attention in relevant review articles has been paid to well-known mushroom-derived glycoproteins such as lectins and protein-bound polysaccharide complexes such as polysaccharide-K (PSK) or krestin and polysaccharopeptide (PSP), which contain substantial amounts of carbohydrates (50-90%). These complex compounds exert their anticancer activity mainly by binding to cell membranes leading to extrinsic (death receptor) apoptosis or intrinsic (mitochondrial) apoptotic pathways. However, several other research studies have reported pure, well-characterized, proteins or peptides from mushrooms, which are carbohydrate-free or have very low amounts of carbohydrate. These proteins may fall into four categories including fungal immunomodulatory proteins, ubiquitin-like proteins, enzymes, and unclassified proteins. Well-defined chemical structure, elucidated full amino acid or N-terminal sequences, purity, and having some distinct and specific pathways compared to glycoproteins have made these low-carbohydrate proteins attractive for cancer research. The aim of this review was therefore to improve the current understanding of mushroom-derived low-carbohydrate proteins and to consolidate the existing knowledge of the most promising mushroom species from which low-carbohydrate proteins have been derived, characterized, and examined for their anticancer activity. In addition, molecular targets and mechanisms of action of these proteins have been discussed. Key points • Mushroom-derived low-carbohydrate proteins lack or have low carbohydrate. • Low-carbohydrate proteins show potent anticancer activities in vitro and in vivo. • There are specific pathways for low-carbohydrate proteins to inhibit cancer cells.Severe side effects of chemotherapy as well as drug resistance highlight the ongoing need to discover novel natural bioactive compounds with anticancer potentiality. Mushroom-derived proteins are among the naturally occurring compounds that have been the subject of a body of research on their potentiality in cancer therapy. The greatest attention in relevant review articles has been paid to well-known mushroom-derived glycoproteins such as lectins and protein-bound polysaccharide complexes such as polysaccharide-K (PSK) or krestin and polysaccharopeptide (PSP), which contain substantial amounts of carbohydrates (50-90%). These complex compounds exert their anticancer activity mainly by binding to cell membranes leading to extrinsic (death receptor) apoptosis or intrinsic (mitochondrial) apoptotic pathways. However, several other research studies have reported pure, well-characterized, proteins or peptides from mushrooms, which are carbohydrate-free or have very low amounts of carbohydrate. These proteins may fall into four categories including fungal immunomodulatory proteins, ubiquitin-like proteins, enzymes, and unclassified proteins. Well-defined chemical structure, elucidated full amino acid or N-terminal sequences, purity, and having some distinct and specific pathways compared to glycoproteins have made these low-carbohydrate proteins attractive for cancer research. The aim of this review was therefore to improve the current understanding of mushroom-derived low-carbohydrate proteins and to consolidate the existing knowledge of the most promising mushroom species from which low-carbohydrate proteins have been derived, characterized, and examined for their anticancer activity. In addition, molecular targets and mechanisms of action of these proteins have been discussed. Key points • Mushroom-derived low-carbohydrate proteins lack or have low carbohydrate. • Low-carbohydrate proteins show potent anticancer activities in vitro and in vivo. • There are specific pathways for low-carbohydrate proteins to inhibit cancer cells. Severe side effects of chemotherapy as well as drug resistance highlight the ongoing need to discover novel natural bioactive compounds with anticancer potentiality. Mushroom-derived proteins are among the naturally occurring compounds that have been the subject of a body of research on their potentiality in cancer therapy. The greatest attention in relevant review articles has been paid to well-known mushroom-derived glycoproteins such as lectins and protein-bound polysaccharide complexes such as polysaccharide-K (PSK) or krestin and polysaccharopeptide (PSP), which contain substantial amounts of carbohydrates (50–90%). These complex compounds exert their anticancer activity mainly by binding to cell membranes leading to extrinsic (death receptor) apoptosis or intrinsic (mitochondrial) apoptotic pathways. However, several other research studies have reported pure, well-characterized, proteins or peptides from mushrooms, which are carbohydrate-free or have very low amounts of carbohydrate. These proteins may fall into four categories including fungal immunomodulatory proteins, ubiquitin-like proteins, enzymes, and unclassified proteins. Well-defined chemical structure, elucidated full amino acid or N-terminal sequences, purity, and having some distinct and specific pathways compared to glycoproteins have made these low-carbohydrate proteins attractive for cancer research. The aim of this review was therefore to improve the current understanding of mushroom-derived low-carbohydrate proteins and to consolidate the existing knowledge of the most promising mushroom species from which low-carbohydrate proteins have been derived, characterized, and examined for their anticancer activity. In addition, molecular targets and mechanisms of action of these proteins have been discussed. Key points • Mushroom-derived low-carbohydrate proteins lack or have low carbohydrate. • Low-carbohydrate proteins show potent anticancer activities in vitro and in vivo. • There are specific pathways for low-carbohydrate proteins to inhibit cancer cells . Severe side effects of chemotherapy as well as drug resistance highlight the ongoing need to discover novel natural bioactive compounds with anticancer potentiality. Mushroom-derived proteins are among the naturally occurring compounds that have been the subject of a body of research on their potentiality in cancer therapy. The greatest attention in relevant review articles has been paid to well-known mushroom-derived glycoproteins such as lectins and protein-bound polysaccharide complexes such as polysaccharide-K (PSK) or krestin and polysaccharopeptide (PSP), which contain substantial amounts of carbohydrates (50–90%). These complex compounds exert their anticancer activity mainly by binding to cell membranes leading to extrinsic (death receptor) apoptosis or intrinsic (mitochondrial) apoptotic pathways. However, several other research studies have reported pure, well-characterized, proteins or peptides from mushrooms, which are carbohydrate-free or have very low amounts of carbohydrate. These proteins may fall into four categories including fungal immunomodulatory proteins, ubiquitin-like proteins, enzymes, and unclassified proteins. Well-defined chemical structure, elucidated full amino acid or N-terminal sequences, purity, and having some distinct and specific pathways compared to glycoproteins have made these low-carbohydrate proteins attractive for cancer research. The aim of this review was therefore to improve the current understanding of mushroom-derived low-carbohydrate proteins and to consolidate the existing knowledge of the most promising mushroom species from which low-carbohydrate proteins have been derived, characterized, and examined for their anticancer activity. In addition, molecular targets and mechanisms of action of these proteins have been discussed.Key points• Mushroom-derived low-carbohydrate proteins lack or have low carbohydrate.• Low-carbohydrate proteins show potent anticancer activities in vitro and in vivo.• There are specific pathways for low-carbohydrate proteins to inhibit cancer cells. Severe side effects of chemotherapy as well as drug resistance highlight the ongoing need to discover novel natural bioactive compounds with anticancer potentiality. Mushroom-derived proteins are among the naturally occurring compounds that have been the subject of a body of research on their potentiality in cancer therapy. The greatest attention in relevant review articles has been paid to well-known mushroom-derived glycoproteins such as lectins and protein-bound polysaccharide complexes such as polysaccharide-K (PSK) or krestin and polysaccharopeptide (PSP), which contain substantial amounts of carbohydrates (50-90%). These complex compounds exert their anticancer activity mainly by binding to cell membranes leading to extrinsic (death receptor) apoptosis or intrinsic (mitochondrial) apoptotic pathways. However, several other research studies have reported pure, well-characterized, proteins or peptides from mushrooms, which are carbohydrate-free or have very low amounts of carbohydrate. These proteins may fall into four categories including fungal immunomodulatory proteins, ubiquitin-like proteins, enzymes, and unclassified proteins. Well-defined chemical structure, elucidated full amino acid or N-terminal sequences, purity, and having some distinct and specific pathways compared to glycoproteins have made these low-carbohydrate proteins attractive for cancer research. The aim of this review was therefore to improve the current understanding of mushroom-derived low-carbohydrate proteins and to consolidate the existing knowledge of the most promising mushroom species from which low-carbohydrate proteins have been derived, characterized, and examined for their anticancer activity. In addition, molecular targets and mechanisms of action of these proteins have been discussed.Key points |
| Audience | Academic |
| Author | Mohammadnejad, Safoora Rezvani, Vala Pourianfar, Hamid R. Madjid Ansari, Alireza Farahmand, Leila |
| Author_xml | – sequence: 1 givenname: Vala surname: Rezvani fullname: Rezvani, Vala organization: Industrial Fungi Biotechnology Research Department, Research Institute for Industrial Biotechnology, Academic Center for Education, Culture and Research (ACECR) – sequence: 2 givenname: Hamid R. surname: Pourianfar fullname: Pourianfar, Hamid R. email: pourianfar@acecr.ac.ir, pourianfarh@gmail.com organization: Industrial Fungi Biotechnology Research Department, Research Institute for Industrial Biotechnology, Academic Center for Education, Culture and Research (ACECR) – sequence: 3 givenname: Safoora surname: Mohammadnejad fullname: Mohammadnejad, Safoora organization: Industrial Fungi Biotechnology Research Department, Research Institute for Industrial Biotechnology, Academic Center for Education, Culture and Research (ACECR) – sequence: 4 givenname: Alireza surname: Madjid Ansari fullname: Madjid Ansari, Alireza organization: Integrative Oncology Department, Breast Cancer Research Center, Moatamed Cancer Institute, ACECR – sequence: 5 givenname: Leila orcidid: 0000-0003-3541-7618 surname: Farahmand fullname: Farahmand, Leila email: laylafarahmand@gmail.com organization: Recombinant Proteins Department, Breast Cancer Research Center, Moatamed Cancer Institute, ACECR |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32556413$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1615/intjmedmushrooms.v17.i11.30 10.1042/bj3230557 10.1016/S0006-291X(02)00301-7 10.7314/APJCP.2014.15.12.5055 10.1038/srep30010 10.1039/c8fo00604k 10.2174/092986610791498966 10.1080/13880209.2017.1325913 10.1111/j.1365-2567.2009.03099.x 10.1016/j.bbamcr.2012.12.013 10.1016/j.foodchem.2004.01.015 10.1139/o00-087 10.1016/j.peptides.2003.11.012 10.1016/j.fct.2012.02.013 10.1016/j.pep.2012.01.015 10.1080/10408390591034445 10.1186/s12929-017-0328-x 10.1016/j.foodchem.2011.03.085 10.1038/ja.2011.112 10.1006/bbrc.1999.1571 10.1006/bbrc.2001.6036 10.3389/fphar.2016.00217 10.1002/jsfa.2887 10.1155/2015/735087 10.1371/journal.pone.0181748 10.1016/S0196-9781(03)00190-6 10.1016/j.phymed.2008.07.004 10.1139/o03-067 10.3892/or.2011.1593 10.1074/mcp.M113.030619 10.1208/s12248-014-9687-3 10.1016/S0196-9781(02)00073-6 10.4196/kjpp.2009.13.1.49 10.1016/j.peptides.2004.03.008 10.4014/jmb.0911.11022 10.1016/j.ijbiomac.2017.01.043 10.2174/138920310790274662 10.1615/IntJMedMushrooms.v18.i9.20 10.1007/978-3-319-14595-2_16 10.1615/IntJMedMushrooms.2018028430 10.1080/09540105.2019.1686467 10.1373/clinchem.2012.185389 10.1055/s-0036-1596829 10.1021/jf4031184 10.1016/j.biochi.2013.10.016 10.1016/j.bbrc.2003.10.201 10.1016/j.bbrc.2004.09.132 10.1021/jf970551h 10.1039/c7fo00895c 10.1016/j.drudis.2018.09.014 10.1016/j.peptides.2004.03.007 10.1246/bcsj.37.747 10.1016/j.procbio.2009.12.010 10.21873/anticanres.11146 10.1155/2019/3139689 10.7717/peerj.4940 10.1016/j.foodchem.2017.09.149 10.3892/ijmm.2013.1553 10.1016/j.gene.2017.10.080 10.1016/j.jfda.2017.12.010 10.1177/101042831770691 10.2174/187152109789760216 10.1186/s13568-017-0346-9 10.1002/mnfr.201200316 10.1007/s11694-019-00222-4 10.1055/s-2003-38492 10.1615/IntJMedMushrooms.2018026264 10.1016/S0959-8049(18)30629-4 10.1111/j.1399-3011.2005.00266.x 10.3892/or.2016.4830 10.1111/j.1432-1033.1995.tb20256.x 10.3322/caac.21492 10.1016/j.bbagen.2007.07.014 10.1016/j.jep.2015.08.042 10.1006/bbrc.2001.5279 10.1139/o06-033 10.1021/bi00427a056 10.1016/j.jmii.2015.07.013 10.1002/psc.382 10.1016/s0196-9781(03)00136-0 10.1021/jf4030272 10.1016/j.lfs.2003.06.023 10.5897/BMBR11.027 10.1007/s00253-008-1639-3 10.1016/j.phymed.2010.07.004 10.1007/s10528-010-9347-y 10.15446/rev.colomb.biote.v16n2.38747 10.2174/0929867003374705 10.1021/acs.jafc.6b00539 10.1039/c7fo00244k 10.1155/2014/417461 10.1155/2018/7271509 10.1016/j.carbpol.2016.08.059 10.1021/jf034556s 10.1006/bbrc.2001.6037 10.1093/ecam/neq057 10.1016/j.peptides.2004.03.013 10.1007/s00726-010-0791-0 10.1007/s11427-011-4153-2 10.3390/ijms13056246 10.1107/S1744309112051755 10.1016/j.fct.2012.10.014 10.3892/ol.2016.5106 10.1038/nrc1994 10.2323/jgam.56.231 10.1006/bbrc.2001.5816 10.1016/j.bbrc.2003.12.139 10.1016/j.biopha.2004.02.004 10.3390/ijms19102986 10.1016/j.ijbiomac.2016.11.004 10.1021/jf500316f |
| ContentType | Journal Article |
| Copyright | Springer-Verlag GmbH Germany, part of Springer Nature 2020 COPYRIGHT 2020 Springer Springer-Verlag GmbH Germany, part of Springer Nature 2020. Copyright Springer Nature B.V. Aug 2020 |
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| Issue | 16 |
| Keywords | Anticancer Chemical structure Mushroom Mode of action Low-carbohydrate protein |
| Language | English |
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| PublicationDate | 2020-08-01 |
| PublicationDateYYYYMMDD | 2020-08-01 |
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| PublicationDecade | 2020 |
| PublicationPlace | Berlin/Heidelberg |
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| PublicationTitle | Applied microbiology and biotechnology |
| PublicationTitleAbbrev | Appl Microbiol Biotechnol |
| PublicationTitleAlternate | Appl Microbiol Biotechnol |
| PublicationYear | 2020 |
| Publisher | Springer Berlin Heidelberg Springer Springer Nature B.V |
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| References | Moradi, Soltani, Ansari, Sardari (CR49) 2009; 8 De Mejía, Prisecaru (CR12) 2005; 45 Ng, Lam, Wang (CR56) 2003; 69 CR39 CR38 Ann, Lun, Zhang, Liu, Li, Zhong, Wang, Cao, Ning, Huang (CR1) 2014; 15 CR36 CR35 CR34 Li, Zheng, Zhou (CR40) 2019; 24 Gerber (CR17) 2008; 77 Xu, Kong, Chen, Guo, Bai, Lu, Li, Zhou (CR103) 2016; 64 Shao, Mao, Li, Li, Wang, Zhou (CR71) 2019; 30 Gao, Padhiar, Wang, Zhang, Zhong, Liu, Kang, Wang, Li, Huang (CR15) 2017; 642 Hu, Zhang, Zhang, Wang, Ng (CR26) 2011; 18 Ngai, Ng (CR59) 2003; 73 Palacios, Lozano, Moro, D’Arrigo, Rostagno, Martínez, García-Lafuente, Guillamón, Villares (CR62) 2011; 128 Sumkhemthong, Suksomtip, Chanvorachote, Chaotham (CR74) 2016; 82 CR45 Marqus, Pirogova, Piva (CR47) 2017; 24 CR43 CR42 Ng, Wong, Wang (CR57) 2010; 11 Watanabe, Nakanishi, Komatsu, Sakabe, Terakawa (CR95) 1964; 37 Yuan, Ma, Zhao, Zhao, Gao, Wang, Song, Zhang, Hu, Xiao (CR110) 2017; 8 Guzmán-Rodríguez, Ochoa-Zarzosa, López-Gómez, López-Meza (CR22) 2015; 2015 Lam, Ng (CR31) 2001; 285 Guo, Wang, Liu, Chen, Chanda, Pahiar, Li, Zhang, Ning, Huang, Cao, Zhong (CR21) 2018; 20 Zhao, Zhao, Li, Zhang, Wang, Ng (CR115) 2009; 20 Liu, Chen, Wang, Ng (CR44) 2015; 17 Prateep, Sumkhemthong, Suksomtip, Chanvorachote, Chaotham (CR66) 2017; 55 Ye, Ng (CR107) 2002; 293 Pan, Wong, Fang, Chan, Ye, Ng (CR63) 2012; 1833 Hsu, Hsu, Lin, Kao, Lin (CR25) 1997; 15 Muszyńska, Grzywacz-Kisielewska, Kała, Gdula-Argasińska (CR51) 2017; 243 Wong, Ng, Jiang, Liu, Sze, Zhang (CR97) 2010; 17 Ghadirian, Ansari, Farahmand, Sanati, Mesbah Moosavi (CR18) 2018; 92 CR53 CR52 Zhang, Liu, Ng, Chen, Qiao, Liu (CR114) 2014; 99 Guan, Wang, Ng (CR20) 2007; 1770 Ngai, Ng (CR58) 2003; 25 Sheu, Po-Jung, Ai-Lin, Chen, Chin (CR72) 2004; 87 Tsao, Kuan, Wang, Sheu (CR78) 2013; 61 Usmani, Bedi, Samuel, Singh, Kalra, Kumar, Ahuja, Sharma, Gautam, Raghava (CR80) 2017; 12 Muñoz, Orozco, Gartner (CR50) 2014; 16 Wang, Ng (CR89) 2004; 324 Sun, Hu, Li (CR75) 2017; 97 Zhang, Zhao, Wang, Ng (CR113) 2013; 33 Lavanya, Subhashini (CR33) 2013; 9 Darvishi, Farahmand, Eslami-S, Majidzadeh-A (CR11) 2017; 38 Wang, Ng (CR82) 2000; 78 Pushparajah, Fatima, Chong, Gambule, Chan, Ng, Tan, Fung, Lee, Tan, Lim (CR67) 2016; 6 Ye, Ng (CR108) 2002; 8 Zhang, Wang, Zhang, Ng, Wang (CR111) 2009; 45 Bray, Ferlay, Soerjomataram, Siegel, Torre, Jemal (CR5) 2018; 68 Rakashanda, Rana, Rafiq, Masood, Amin (CR68) 2012; 7 Liang, Li, Zhou, Zhang, Liu, Zhou, Sun (CR41) 2011; 27 Mohammadnejad, Pourianfar, Drakhshan, Jabaleh, Rezayi (CR48) 2019; 13 Yap, Tan, Ng, Tan, Fung (CR106) 2018; 6 Kino, Yamashita, Yamaoka, Watanabe, Tanaka, Ko, Shimizu, Tsunoo (CR29) 1989; 264 CR77 Kinghorn, De Blanco, Lucas, Rakotondraibe, Orjala, Soejarto, Oberlies, Pearce, Wani, Stockwell, Burdette, Swanson, Fuchs, Phelps, Xu, Zhang, Shen (CR28) 2016; 36 CR76 CR116 Chen, Jiang, Jin, Yin, Yu, Lan, Cui, Liang, Wong, Guo, Sun (CR7) 2012; 56 Ko, Hsu, Lin, Kao, Lin (CR30) 1994; 228 Dan, Liu, Wong, Ng (CR10) 2016; 7 Ng, Wang (CR54) 2004; 25 Li, Wen, Liu, Zhou, Chen (CR37) 2012; 82 Reis, Martins, Barros, Ferreira (CR70) 2012; 50 CR2 CR4 Wang, Ng (CR81) 1999; 264 Wang, Su, Bao, Cong, Chen, Li, Zhou (CR93) 2012; 10 Wu, Cao, Wu, Lin, Xie (CR98) 2009; 21 Wang, Wan, Gao, Zhong, Sha, Liu, Zhang, Tian, Ruan, Cao, Huang (CR94) 2016; 36 CR84 Ngai, Wang, Ng (CR60) 2003; 24 CR83 Lv, Kong, Yao, Zhang, Leng, Bian, Balzarini, Damme, Bao (CR46) 2009; 16 Wang, Ng (CR85) 2003; 81 Tung, Lin, Wang, Chen, Sheu, Lu (CR79) 2018; 26 Wang, Ng (CR90) 2006; 84 Yap, Fung, Ng, Tan, Tan (CR105) 2015; 174 Wong, Wang, Ng (CR96) 2008; 81 Yao, Yu, Ooi, Ng, Chang, Sun, Ooi (CR104) 1998; 46 Ooi, Liu (CR61) 2000; 7 Zhou, Han, Zhang, Zhang, Ng, Liu (CR117) 2017; 7 Raval, Purohit, Singh, Maheshwari, Saraf (CR69) 2015 Ng, Lam, Chan (CR55) 2002; 23 Wang, Ng (CR87) 2003; 24 Chang, Hsiao, Wu, Ou, Lin, Lue, Ko (CR6) 2013; 61 Chu, Sun, Ko, Ku, Lin, Lee, Liao, Pan, Lu, Lue (CR9) 2015; 50 CR99 Cheng, Zhao, Chen, Yu, Wang, Cheng, Zhu (CR8) 2013; 12 Hu, Du, Ma, Pei, Ma, Yuan, Nakata, Yang (CR27) 2018; 9 Wang, Ng (CR86) 2003; 312 CR92 CR91 Gao, Wáng, Wāng, Wu, Chen, Yang, Bao (CR16) 2019; 2019 Grzywacz, Gdula-Argasińska, Kała, Opoka, Muszyńska (CR19) 2016; 18 Wu, Wang, Ng (CR101) 2011; 65 Sheu, Chien, Wang, Chang, Shyu (CR73) 2007; 87 Bao, Bai, Gao, Wu, Wang (CR3) 2018; 20 Zhang, Zhang, Hu, Wang, Ng (CR112) 2010; 48 Patterson, Maresso, Hawk (CR65) 2013; 59 CR24 CR23 Xia, Chu, Ng (CR102) 2005; 66 Park, Na, Jung, Park, Kim (CR64) 2009; 13 CR100 Lam, Ng, Wang (CR32) 2001; 289 Ding, Seow, Huang, Liew, Lim, Kuo, Chua (CR14) 2009; 128 Wang, Ng (CR88) 2004; 25 Di (CR13) 2015; 17 CR109 10707_CR100 HX Wang (10707_CR85) 2003; 81 DE Gerber (10707_CR17) 2008; 77 HX Wang (10707_CR89) 2004; 324 10707_CR109 HX Wang (10707_CR87) 2003; 24 BT Park (10707_CR64) 2009; 13 DD Hu (10707_CR26) 2011; 18 HX Wang (10707_CR86) 2003; 312 YW Lam (10707_CR32) 2001; 289 SL Patterson (10707_CR65) 2013; 59 GQ Zhang (10707_CR111) 2009; 45 XY Ye (10707_CR108) 2002; 8 S Rakashanda (10707_CR68) 2012; 7 TB Ng (10707_CR57) 2010; 11 CH Tung (10707_CR79) 2018; 26 JJ Guzmán-Rodríguez (10707_CR22) 2015; 2015 10707_CR52 A Grzywacz (10707_CR19) 2016; 18 10707_CR53 H Lv (10707_CR46) 2009; 16 A Prateep (10707_CR66) 2017; 55 R Zhou (10707_CR117) 2017; 7 RY Zhang (10707_CR112) 2010; 48 F Sheu (10707_CR72) 2004; 87 KD Shao (10707_CR71) 2019; 30 HYY Yap (10707_CR105) 2015; 174 HX Wang (10707_CR82) 2000; 78 I Palacios (10707_CR62) 2011; 128 HC Hsu (10707_CR25) 1997; 15 Y Gao (10707_CR15) 2017; 642 Y Wu (10707_CR101) 2011; 65 B Darvishi (10707_CR11) 2017; 38 L Di (10707_CR13) 2015; 17 JH Wong (10707_CR96) 2008; 81 10707_CR83 10707_CR84 GP Guan (10707_CR20) 2007; 1770 PHK Ngai (10707_CR58) 2003; 25 XH Ann (10707_CR1) 2014; 15 Y Gao (10707_CR16) 2019; 2019 PY Chu (10707_CR9) 2015; 50 QZ Li (10707_CR40) 2019; 24 AG Muñoz (10707_CR50) 2014; 16 L Xia (10707_CR102) 2005; 66 Y Watanabe (10707_CR95) 1964; 37 H Xu (10707_CR103) 2016; 64 DP Bao (10707_CR3) 2018; 20 S Moradi (10707_CR49) 2009; 8 10707_CR76 10707_CR77 S Marqus (10707_CR47) 2017; 24 Y Chang (10707_CR6) 2013; 61 HYY Yap (10707_CR106) 2018; 6 L Wu (10707_CR98) 2009; 21 10707_CR4 R Ghadirian (10707_CR18) 2018; 92 HL Cheng (10707_CR8) 2013; 12 WL Pan (10707_CR63) 2012; 1833 10707_CR2 B Muszyńska (10707_CR51) 2017; 243 TB Ng (10707_CR55) 2002; 23 SK Lam (10707_CR31) 2001; 285 10707_CR23 10707_CR24 J Lavanya (10707_CR33) 2013; 9 V Pushparajah (10707_CR67) 2016; 6 Y Sun (10707_CR75) 2017; 97 XY Ye (10707_CR107) 2002; 293 YW Tsao (10707_CR78) 2013; 61 Q Hu (10707_CR27) 2018; 9 10707_CR91 PH Ngai (10707_CR60) 2003; 24 TB Ng (10707_CR56) 2003; 69 10707_CR99 10707_CR92 AD Kinghorn (10707_CR28) 2016; 36 Y Ding (10707_CR14) 2009; 128 HX Wang (10707_CR88) 2004; 25 HX Wang (10707_CR81) 1999; 264 F Li (10707_CR37) 2012; 82 VEC Ooi (10707_CR61) 2000; 7 JL Ko (10707_CR30) 1994; 228 FS Reis (10707_CR70) 2012; 50 B Yuan (10707_CR110) 2017; 8 R Zhang (10707_CR113) 2013; 33 10707_CR42 10707_CR43 S Zhao (10707_CR115) 2009; 20 SS Usmani (10707_CR80) 2017; 12 Y Chen (10707_CR7) 2012; 56 10707_CR45 F Sheu (10707_CR73) 2007; 87 C Liang (10707_CR41) 2011; 27 Q Liu (10707_CR44) 2015; 17 XF Wang (10707_CR93) 2012; 10 QZ Yao (10707_CR104) 1998; 46 S Sumkhemthong (10707_CR74) 2016; 82 PHK Ngai (10707_CR59) 2003; 73 K Kino (10707_CR29) 1989; 264 10707_CR116 X Guo (10707_CR21) 2018; 20 F Bray (10707_CR5) 2018; 68 TB Ng (10707_CR54) 2004; 25 VH Raval (10707_CR69) 2015 X Dan (10707_CR10) 2016; 7 EG De Mejía (10707_CR12) 2005; 45 J Wang (10707_CR94) 2016; 36 10707_CR38 JH Wong (10707_CR97) 2010; 17 10707_CR39 10707_CR34 10707_CR35 S Mohammadnejad (10707_CR48) 2019; 13 10707_CR36 Y Zhang (10707_CR114) 2014; 99 HX Wang (10707_CR90) 2006; 84 |
| References_xml | – ident: CR45 – volume: 17 start-page: 1037 year: 2015 end-page: 1045 ident: CR44 article-title: Isolation and characterization of a ubiquitin-like ribonuclease from the cultured deep root mushroom, (higher Basidiomycetes) publication-title: Int J Med Mushrooms doi: 10.1615/intjmedmushrooms.v17.i11.30 – volume: 15 start-page: 557 year: 1997 end-page: 565 ident: CR25 article-title: FIP-vvo, a new fungal immunomodulatory protein isolated from publication-title: Biochem J doi: 10.1042/bj3230557 – volume: 293 start-page: 857 year: 2002 end-page: 861 ident: CR107 article-title: A novel and potent ribonuclease from fruiting bodies of the mushroom publication-title: Biochem Biophys Res Commun doi: 10.1016/S0006-291X(02)00301-7 – volume: 15 start-page: 5055 year: 2014 end-page: 5061 ident: CR1 article-title: Expression and characterization of protein latcripin-3, an antioxidant and antitumor molecule from publication-title: Asian Pac J Cancer Prev doi: 10.7314/APJCP.2014.15.12.5055 – volume: 6 start-page: 30010 year: 2016 ident: CR67 article-title: Characterization of a new fungal immunomodulatory protein from tiger milk mushroom, publication-title: Sci Rep doi: 10.1038/srep30010 – ident: CR39 – volume: 9 start-page: 3764 year: 2018 end-page: 3775 ident: CR27 article-title: Purification, identification and functional characterization of an immunomodulatory protein from publication-title: Food Funct doi: 10.1039/c8fo00604k – volume: 17 start-page: 1040 year: 2010 end-page: 1047 ident: CR97 article-title: Purification and characterization of a laccase with inhibitory activity toward HIV-1 reverse transcriptase and tumor cells from an edible mushroom ( ) publication-title: Protein Pept Lett doi: 10.2174/092986610791498966 – volume: 55 start-page: 1792 year: 2017 end-page: 1799 ident: CR66 article-title: Peptides extracted from edible mushroom: induces apoptosis in human lung cancer cells publication-title: Pharm Biol doi: 10.1080/13880209.2017.1325913 – ident: CR77 – volume: 128 start-page: e881 year: 2009 end-page: e894 ident: CR14 article-title: Coadministration of the fungal immunomodulatory protein FIP-Fve and a tumor-associated antigen enhanced antitumor immunity publication-title: Immunology doi: 10.1111/j.1365-2567.2009.03099.x – volume: 1833 start-page: 987 year: 2012 end-page: 996 ident: CR63 article-title: Differential inhibitory potencies and mechanisms of the type I ribosome inactivating protein marmorin on estrogen receptor (ER) positive and ER-negative breast cancer cells publication-title: Biochim Biophys Acta doi: 10.1016/j.bbamcr.2012.12.013 – ident: CR42 – volume: 87 start-page: 593 year: 2004 end-page: 600 ident: CR72 article-title: Isolation and characterization of an immunomodulatory protein (APP) from the Jew’s ear mushroom publication-title: Food Chem doi: 10.1016/j.foodchem.2004.01.015 – volume: 78 start-page: 699 year: 2000 end-page: 702 ident: CR82 article-title: Flammulin: A novel ribosome-inactivating protein from fruiting bodies of the winter mushroom publication-title: Biochem Cell Biol doi: 10.1139/o00-087 – ident: CR92 – volume: 25 start-page: 11 year: 2003 end-page: 17 ident: CR58 article-title: A ribonuclease with antimicrobial, antimitogenic and antiproliferative activities from the edible mushroom publication-title: Peptides doi: 10.1016/j.peptides.2003.11.012 – volume: 50 start-page: 1201 year: 2012 end-page: 1207 ident: CR70 article-title: Antioxidant properties and phenolic profile of the most widely appreciated cultivated mushrooms: a comparative study between and samples publication-title: Food Chem Toxicol doi: 10.1016/j.fct.2012.02.013 – volume: 82 start-page: 339 year: 2012 end-page: 344 ident: CR37 article-title: Gene cloning and recombinant expression of a novel fungal immunomodulatory protein from publication-title: Protein Expr Purif doi: 10.1016/j.pep.2012.01.015 – volume: 45 start-page: 425 year: 2005 end-page: 445 ident: CR12 article-title: Lectins as bioactive plant proteins: a potential in cancer treatment publication-title: Crit Rev Food Sci Nutr doi: 10.1080/10408390591034445 – volume: 24 start-page: 21 year: 2017 ident: CR47 article-title: Evaluation of the use of therapeutic peptides for cancer treatment publication-title: J Biomed Sci doi: 10.1186/s12929-017-0328-x – volume: 128 start-page: 674 year: 2011 end-page: 678 ident: CR62 article-title: Antioxidant properties of phenolic compounds occurring in edible mushrooms publication-title: Food Chem doi: 10.1016/j.foodchem.2011.03.085 – ident: CR36 – volume: 65 start-page: 67 year: 2011 end-page: 72 ident: CR101 article-title: Purification and characterization of a novel RNase with antiproliferative activity from the mushroom publication-title: J Antibiot doi: 10.1038/ja.2011.112 – volume: 21 start-page: 371 year: 2009 end-page: 376 ident: CR98 article-title: YP3: a novel plant virus inhibitory protein from mushroom publication-title: Nat Prod Res Dev – ident: CR109 – ident: CR100 – ident: CR91 – volume: 264 start-page: 714 year: 1999 end-page: 718 ident: CR81 article-title: Isolation of a new ribonuclease from fresh fruiting bodies of the straw mushroom publication-title: Biochem Biophys Res Commun doi: 10.1006/bbrc.1999.1571 – volume: 289 start-page: 744 year: 2001 end-page: 749 ident: CR32 article-title: Antiproliferative and antimitogenic activities in a peptide from puffball mushroom publication-title: Biochem Biophys Res Commun doi: 10.1006/bbrc.2001.6036 – volume: 7 start-page: 217 year: 2016 ident: CR10 article-title: A ribonuclease isolated from wild suppressed autophagy and triggered apoptosis in colorectal cancer cells publication-title: Front Pharmacol doi: 10.3389/fphar.2016.00217 – volume: 87 start-page: 1550 year: 2007 end-page: 1558 ident: CR73 article-title: New protein PCiP from edible golden oyster mushroom ( ) activating murine macrophages and splenocytes publication-title: J Sci Food Agric doi: 10.1002/jsfa.2887 – volume: 2015 start-page: 735087 year: 2015 end-page: 735011 ident: CR22 article-title: Plant antimicrobial peptides as potential anticancer agents publication-title: Biomed Res Int doi: 10.1155/2015/735087 – volume: 12 year: 2017 ident: CR80 article-title: THPdb: database of FDA-approved peptide and protein therapeutics publication-title: PLoS One doi: 10.1371/journal.pone.0181748 – volume: 24 start-page: 973 year: 2003 end-page: 977 ident: CR87 article-title: Isolation of a ribonuclease from fruiting bodies of the wild mushroom publication-title: Peptides doi: 10.1016/S0196-9781(03)00190-6 – volume: 16 start-page: 198 year: 2009 end-page: 205 ident: CR46 article-title: Nebrodeolysin, a novel hemolytic protein from mushroom with apoptosis-inducing and anti-HIV-1 effects publication-title: Phytomedicine doi: 10.1016/j.phymed.2008.07.004 – volume: 81 start-page: 373 year: 2003 end-page: 377 ident: CR85 article-title: A novel ribonuclease from the veiled lady mushroom publication-title: Biochem Cell Biol doi: 10.1139/o03-067 – volume: 27 start-page: 1079 year: 2011 end-page: 1089 ident: CR41 article-title: Recombinant Lz-8 from induces endoplasmic reticulum stress-mediated autophagic cell death in SGC-7901 human gastric cancer cells publication-title: Oncol Rep doi: 10.3892/or.2011.1593 – volume: 12 start-page: 2236 year: 2013 end-page: 2248 ident: CR8 article-title: Cloning and characterization of the glycoside hydrolases that remove xylosyl groups from 7-β-xylosyl-10-deacetyltaxol and its analogues publication-title: Mol Cell Proteomics doi: 10.1074/mcp.M113.030619 – volume: 17 start-page: 134 year: 2015 end-page: 143 ident: CR13 article-title: Strategic approaches to optimizing peptide ADME properties publication-title: AAPS J doi: 10.1208/s12248-014-9687-3 – volume: 23 start-page: 1361 year: 2002 end-page: 1365 ident: CR55 article-title: A ubiquitin-like peptide from the mushroom exhibits relatively potent translation-inhibitory and ribonuclease activities publication-title: Peptides doi: 10.1016/S0196-9781(02)00073-6 – ident: CR38 – volume: 13 start-page: 49 year: 2009 end-page: 54 ident: CR64 article-title: Antifungal and anticancer activities of a protein from the mushroom publication-title: Korean J Physiol Pharmacol doi: 10.4196/kjpp.2009.13.1.49 – ident: CR52 – volume: 25 start-page: 935 year: 2004 end-page: 939 ident: CR88 article-title: Isolation of a new ribonuclease from fruiting bodies of the silver plate mushroom publication-title: Peptides doi: 10.1016/j.peptides.2004.03.008 – volume: 20 start-page: 693 year: 2009 end-page: 699 ident: CR115 article-title: An antiproliferative ribonuclease from fruiting bodies of the wild mushroom publication-title: J Microbiol Biotechnol doi: 10.4014/jmb.0911.11022 – volume: 97 start-page: 323 year: 2017 end-page: 330 ident: CR75 article-title: Antioxidant, antitumor and immunostimulatory activities of the polypeptide from mycelium publication-title: Int J Biol Macromol doi: 10.1016/j.ijbiomac.2017.01.043 – volume: 11 start-page: 37 year: 2010 end-page: 53 ident: CR57 article-title: Recent progress in research on ribosome inactivating proteins publication-title: Curr Protein Pept Sci doi: 10.2174/138920310790274662 – volume: 18 start-page: 769 year: 2016 end-page: 779 ident: CR19 article-title: Anti-inflammatory activity of biomass extracts of the bay mushroom, (Agaricomycetes), in RAW 264.7 cells publication-title: Int J Med Mushrooms doi: 10.1615/IntJMedMushrooms.v18.i9.20 – start-page: 421 year: 2015 end-page: 449 ident: CR69 article-title: Extracellular proteases from halophilic and haloalkaliphilic bacteria: occurrence and biochemical properties publication-title: Halophiles, Sustainable doi: 10.1007/978-3-319-14595-2_16 – volume: 20 start-page: 1163 year: 2018 end-page: 1172 ident: CR21 article-title: Expression and antitumor function of latcripin-4 RCC and ANK domain protein on HepG2 from the shiitake medicinal mushroom, C91-3 (Agaricomycetes), transcriptome publication-title: Int J Med Mushrooms doi: 10.1615/IntJMedMushrooms.2018028430 – volume: 30 start-page: 1253 year: 2019 end-page: 1270 ident: CR71 article-title: Characterization of a novel fungal immunomodulatory protein, FIP-SJ75 shuffled from , and publication-title: Food Agric Immunol doi: 10.1080/09540105.2019.1686467 – ident: CR83 – volume: 59 start-page: 94 year: 2013 end-page: 101 ident: CR65 article-title: Cancer chemoprevention: successes and failures publication-title: Clin Chem doi: 10.1373/clinchem.2012.185389 – volume: 82 start-page: S1 year: 2016 end-page: S381 ident: CR74 article-title: Anticancer activity of peptide extracted from edible mushroom; in human lung cancer cells publication-title: Planta Med doi: 10.1055/s-0036-1596829 – ident: CR24 – volume: 61 start-page: 9828 year: 2013 end-page: 9838 ident: CR78 article-title: Characterization of a novel maitake ( ) protein that activates natural killer and dendritic cells and enhances antitumor immunity in mice publication-title: J Agric Food Chem doi: 10.1021/jf4031184 – volume: 99 start-page: 28 year: 2014 end-page: 37 ident: CR114 article-title: Purification and characterization of a novel antitumor protein with antioxidant and deoxyribonuclease activity from edible mushroom publication-title: Biochimie doi: 10.1016/j.biochi.2013.10.016 – volume: 312 start-page: 965 year: 2003 end-page: 968 ident: CR86 article-title: A ribonuclease with distinctive features from the wild green-headed mushroom publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2003.10.201 – volume: 324 start-page: 855 year: 2004 end-page: 859 ident: CR89 article-title: Purification of a novel ribonuclease from dried fruiting bodies of the edible wild mushroom publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2004.09.132 – volume: 46 start-page: 788 year: 1998 end-page: 792 ident: CR104 article-title: Isolation and characterization of a type 1 ribosome-inactivating protein from fruiting bodies of the edible mushroom ( ) publication-title: J Agric Food Chem doi: 10.1021/jf970551h – volume: 8 start-page: 3553 year: 2017 end-page: 3562 ident: CR110 article-title: and inhibitory effects of a protein on colon cancer cells publication-title: Food Funct doi: 10.1039/c7fo00895c – ident: CR4 – volume: 24 start-page: 307 year: 2019 end-page: 314 ident: CR40 article-title: Fungal immunomodulatory proteins: characteristic, potential antitumor activities and their molecular mechanisms publication-title: Drug Discov Today doi: 10.1016/j.drudis.2018.09.014 – volume: 10 start-page: 1 year: 2012 end-page: 12 ident: CR93 article-title: Immunomodulatory effects of fungal proteins publication-title: Curr Top Nutraceut R – volume: 25 start-page: 929 year: 2004 end-page: 933 ident: CR54 article-title: Flammin and velin: new ribosome inactivating polypeptides from the mushroom publication-title: Peptides doi: 10.1016/j.peptides.2004.03.007 – volume: 37 start-page: 747 year: 1964 end-page: 750 ident: CR95 article-title: Flammulin, an antitumor substance publication-title: Bull Chem Soc Jpn doi: 10.1246/bcsj.37.747 – volume: 45 start-page: 627 year: 2009 end-page: 633 ident: CR111 article-title: Purification and characterization of a novel laccase from the edible mushroom publication-title: Process Biochem doi: 10.1016/j.procbio.2009.12.010 – ident: CR35 – volume: 36 start-page: 5623 year: 2016 end-page: 5638 ident: CR28 article-title: Discovery of anticancer agents of diverse natural origin publication-title: Anticancer Res doi: 10.21873/anticanres.11146 – ident: CR84 – volume: 2019 start-page: 15 year: 2019 ident: CR16 article-title: Protective function of novel fungal immunomodulatory proteins Fip-lti1 and Fip-lti2 from in concanavalin A-induced liver oxidative injury publication-title: Oxidative Med Cell Longev doi: 10.1155/2019/3139689 – volume: 6 year: 2018 ident: CR106 article-title: Molecular attributes and apoptosis-inducing activities of a putative serine protease isolated from Tiger Milk mushroom ( ) sclerotium against breast cancer cells publication-title: PeerJ doi: 10.7717/peerj.4940 – volume: 243 start-page: 373 year: 2017 end-page: 381 ident: CR51 article-title: Anti-inflammatory properties of edible mushrooms: A review publication-title: Food Chem doi: 10.1016/j.foodchem.2017.09.149 – volume: 33 start-page: 209 year: 2013 end-page: 214 ident: CR113 article-title: A novel ribonuclease with antiproliferative activity toward leukemia and lymphoma cells and HIV-1 reverse transcriptase inhibitory activity from the mushroom, publication-title: Int J Mol Med doi: 10.3892/ijmm.2013.1553 – volume: 642 start-page: 212 year: 2017 end-page: 219 ident: CR15 article-title: Recombinant latcripin 11 of C91-3 suppresses the proliferation of various cancer cells publication-title: Gene doi: 10.1016/j.gene.2017.10.080 – volume: 26 start-page: 1005 year: 2018 end-page: 1014 ident: CR79 article-title: Application of thermal stability difference to remove flammutoxin in fungal immunomodulatory protein, FIP-fve, extract from publication-title: J Food Drug Anal doi: 10.1016/j.jfda.2017.12.010 – volume: 38 start-page: 1 year: 2017 end-page: 10 ident: CR11 article-title: NF-κB as the main node of resistance to receptor tyrosine kinase inhibitors in triple-negative breast cancer publication-title: Tumor Biol doi: 10.1177/101042831770691 – ident: CR116 – volume: 8 start-page: 327 year: 2009 end-page: 344 ident: CR49 article-title: Peptidomimetics and their applications in antifungal drug design publication-title: Anti-Infective Agents Med Chem doi: 10.2174/187152109789760216 – volume: 7 start-page: 47 year: 2017 ident: CR117 article-title: Purification and characterization of a novel ubiquitin-like antitumor protein with hemagglutinating and deoxyribonuclease activities from the edible mushroom publication-title: AMB Express doi: 10.1186/s13568-017-0346-9 – volume: 56 start-page: 1729 year: 2012 end-page: 1738 ident: CR7 article-title: Purification and characterization of an antitumor protein with deoxyribonuclease activity from edible mushroom publication-title: Food Res doi: 10.1002/mnfr.201200316 – volume: 13 start-page: 3015 year: 2019 end-page: 3024 ident: CR48 article-title: Potent antiproliferative and pro-apoptotic effects of a soluble protein fraction from culinary-medicinal mushroom on cancer cells publication-title: J Food Meas Charact doi: 10.1007/s11694-019-00222-4 – volume: 69 start-page: 212 year: 2003 end-page: 217 ident: CR56 article-title: Calcaelin, a new protein with translation inhibiting, antiproliferative and antimitogenic activities from the mosaic puffball mushroom publication-title: Planta Med doi: 10.1055/s-2003-38492 – ident: CR99 – volume: 20 start-page: 537 year: 2018 end-page: 548 ident: CR3 article-title: Computational insights into the molecular mechanism of the high immunomodulatory activity of LZ-8 protein isolated from the lingzhi or reishi medicinal mushroom (Agaricomycetes) publication-title: Int J Med Mushrooms doi: 10.1615/IntJMedMushrooms.2018026264 – volume: 92 start-page: S135 year: 2018 ident: CR18 article-title: A proteomics approach in evaluating extremely low frequency electromagnetic field-induced apoptosis in breast cancer cells publication-title: Eur J Cancer doi: 10.1016/S0959-8049(18)30629-4 – volume: 66 start-page: 1 year: 2005 end-page: 8 ident: CR102 article-title: A low-molecular mass ribonuclease from the brown oyster mushroom publication-title: J Pept Res doi: 10.1111/j.1399-3011.2005.00266.x – ident: CR43 – ident: CR2 – ident: CR53 – volume: 36 start-page: 441 year: 2016 end-page: 447 ident: CR94 article-title: Latcripin-13 domain induces apoptosis and cell cycle arrest at the G1 phase in human lung carcinoma A549 cells publication-title: Oncol Rep doi: 10.3892/or.2016.4830 – volume: 228 start-page: 244 year: 1994 end-page: 249 ident: CR30 article-title: A new fungal immunomodulatory protein, FIP-fve isolated from the edible mushroom, and its complete amino acid sequence publication-title: Eur J Biochem doi: 10.1111/j.1432-1033.1995.tb20256.x – volume: 77 start-page: 311 year: 2008 end-page: 319 ident: CR17 article-title: Targeted therapies: a new generation of cancer treatments publication-title: Am Fam Physician – ident: CR23 – volume: 68 start-page: 394 year: 2018 end-page: 424 ident: CR5 article-title: Global cancer statistics 2018: Globocan estimates of incidence and mortality worldwide for 36 cancers in 185 countries publication-title: CA Cancer J Clin doi: 10.3322/caac.21492 – volume: 1770 start-page: 1593 year: 2007 end-page: 1597 ident: CR20 article-title: A novel ribonuclease with antiproliferative activity from fresh fruiting bodies of the edible mushroom publication-title: BBA-Gen Subjects doi: 10.1016/j.bbagen.2007.07.014 – volume: 174 start-page: 437 year: 2015 end-page: 451 ident: CR105 article-title: Shotgun proteomic analysis of tigermilk mushroom ( ) and the isolation of a cytotoxic fungal serine protease from its sclerotium publication-title: J Ethnopharmacol doi: 10.1016/j.jep.2015.08.042 – volume: 285 start-page: 1071 year: 2001 end-page: 1075 ident: CR31 article-title: Hypsin, a novel thermostable ribosome-inactivating protein with antifungal and antiproliferative activities from fruiting bodies of the edible mushroom publication-title: Biochem Biophys Res Commun doi: 10.1006/bbrc.2001.5279 – volume: 84 start-page: 178 year: 2006 end-page: 183 ident: CR90 article-title: A novel ribonuclease from fresh fruiting bodies of the portabella mushroom publication-title: Biochem Cell Biol doi: 10.1139/o06-033 – volume: 264 start-page: 472 year: 1989 end-page: 478 ident: CR29 article-title: Isolation and characterization of a new immunomodulatory protein, Ling Zhi-8 (LZ-8), from publication-title: J Biol Chem doi: 10.1021/bi00427a056 – volume: 50 start-page: 297 year: 2015 end-page: 306 ident: CR9 article-title: Oral fungal immunomodulatory protein- has influence on pulmonary inflammatory process and potential treatment for allergic airway disease: A mouse model publication-title: J Microbiol Immunol Infect doi: 10.1016/j.jmii.2015.07.013 – volume: 8 start-page: 235 year: 2002 end-page: 240 ident: CR108 article-title: A novel peptide with ribonuclease and translation-inhibitory activities from fruiting bodies of the oyster mushroom publication-title: J Pept Sci doi: 10.1002/psc.382 – volume: 24 start-page: 639 year: 2003 end-page: 645 ident: CR60 article-title: Purification and characterization of an ubiquitin-like peptide with macrophage stimulating, antiproliferative and ribonuclease activities from the mushroom publication-title: Peptides doi: 10.1016/s0196-9781(03)00136-0 – volume: 61 start-page: 12044 year: 2013 end-page: 12052 ident: CR6 article-title: Interruption of lung cancer cell migration and proliferation by fungal immunomodulatory protein FIP-fve from publication-title: J Agric Food Chem doi: 10.1021/jf4030272 – volume: 73 start-page: 3363 year: 2003 end-page: 3374 ident: CR59 article-title: Lentin, a novel and potent antifungal protein from shitake mushroom with inhibitory effects on activity of human immunodeficiency virus-1 reverse transcriptase and proliferation of leukemia cells publication-title: Life Sci doi: 10.1016/j.lfs.2003.06.023 – volume: 7 start-page: 90 year: 2012 end-page: 101 ident: CR68 article-title: Role of proteases in cancer: A review publication-title: Biotech Mol Biol Rev doi: 10.5897/BMBR11.027 – ident: CR34 – volume: 81 start-page: 669 year: 2008 end-page: 674 ident: CR96 article-title: Marmorin, a new ribosome inactivating protein with antiproliferative and HIV-1 reverse transcriptase inhibitory activities from the mushroom publication-title: Appl Microbiol Biotechnol doi: 10.1007/s00253-008-1639-3 – ident: CR76 – volume: 18 start-page: 374 year: 2011 end-page: 379 ident: CR26 article-title: A laccase with antiproliferative activity against tumor cells from an edible mushroom, white common publication-title: Phytomedicine doi: 10.1016/j.phymed.2010.07.004 – volume: 48 start-page: 658 year: 2010 end-page: 668 ident: CR112 article-title: A novel ribonuclease with antiproliferative activity from fresh fruiting bodies of the edible mushroom publication-title: Biochem Genet doi: 10.1007/s10528-010-9347-y – volume: 9 start-page: 162 year: 2013 end-page: 176 ident: CR33 article-title: Therapeutic proteins and peptides from edible and medicinal mushrooms- review publication-title: Eur Sci J – volume: 16 start-page: 90 year: 2014 end-page: 95 ident: CR50 article-title: Finding of a novel fungal immunomodulatory protein coding sequence in publication-title: Rev Colomb Biotecnol doi: 10.15446/rev.colomb.biote.v16n2.38747 – volume: 7 start-page: 715 year: 2000 end-page: 729 ident: CR61 article-title: Immunomodulation and anti-cancer activity of polysaccharide protein complexes publication-title: Curr Med Chem doi: 10.2174/0929867003374705 – volume: 64 start-page: 2690 year: 2016 end-page: 2698 ident: CR103 article-title: Recombinant FIP-gat, a fungal immunomodulatory protein from , induces growth inhibition and cell death in breast cancer cells publication-title: J Agric Food Chem doi: 10.1021/acs.jafc.6b00539 – volume: 68 start-page: 394 year: 2018 ident: 10707_CR5 publication-title: CA Cancer J Clin doi: 10.3322/caac.21492 – volume: 64 start-page: 2690 year: 2016 ident: 10707_CR103 publication-title: J Agric Food Chem doi: 10.1021/acs.jafc.6b00539 – volume: 87 start-page: 1550 year: 2007 ident: 10707_CR73 publication-title: J Sci Food Agric doi: 10.1002/jsfa.2887 – ident: 10707_CR109 doi: 10.1039/c7fo00244k – volume: 66 start-page: 1 year: 2005 ident: 10707_CR102 publication-title: J Pept Res doi: 10.1111/j.1399-3011.2005.00266.x – ident: 10707_CR116 doi: 10.1155/2014/417461 – ident: 10707_CR2 doi: 10.1155/2018/7271509 – volume: 8 start-page: 327 year: 2009 ident: 10707_CR49 publication-title: Anti-Infective Agents Med Chem doi: 10.2174/187152109789760216 – volume: 7 start-page: 90 year: 2012 ident: 10707_CR68 publication-title: Biotech Mol Biol Rev doi: 10.5897/BMBR11.027 – volume: 7 start-page: 217 year: 2016 ident: 10707_CR10 publication-title: Front Pharmacol doi: 10.3389/fphar.2016.00217 – volume: 38 start-page: 1 year: 2017 ident: 10707_CR11 publication-title: Tumor Biol doi: 10.1177/101042831770691 – volume: 25 start-page: 11 year: 2003 ident: 10707_CR58 publication-title: Peptides doi: 10.1016/j.peptides.2003.11.012 – ident: 10707_CR77 doi: 10.1016/j.carbpol.2016.08.059 – volume: 289 start-page: 744 year: 2001 ident: 10707_CR32 publication-title: Biochem Biophys Res Commun doi: 10.1006/bbrc.2001.6036 – volume: 17 start-page: 134 year: 2015 ident: 10707_CR13 publication-title: AAPS J doi: 10.1208/s12248-014-9687-3 – volume: 7 start-page: 715 year: 2000 ident: 10707_CR61 publication-title: Curr Med Chem doi: 10.2174/0929867003374705 – volume: 9 start-page: 162 year: 2013 ident: 10707_CR33 publication-title: Eur Sci J – volume: 24 start-page: 21 year: 2017 ident: 10707_CR47 publication-title: J Biomed Sci doi: 10.1186/s12929-017-0328-x – ident: 10707_CR92 doi: 10.1021/jf034556s – volume: 11 start-page: 37 year: 2010 ident: 10707_CR57 publication-title: Curr Protein Pept Sci doi: 10.2174/138920310790274662 – volume: 24 start-page: 639 year: 2003 ident: 10707_CR60 publication-title: Peptides doi: 10.1016/s0196-9781(03)00136-0 – start-page: 421 volume-title: Halophiles, Sustainable year: 2015 ident: 10707_CR69 doi: 10.1007/978-3-319-14595-2_16 – volume: 65 start-page: 67 year: 2011 ident: 10707_CR101 publication-title: J Antibiot doi: 10.1038/ja.2011.112 – ident: 10707_CR83 doi: 10.1006/bbrc.2001.6037 – volume: 264 start-page: 472 year: 1989 ident: 10707_CR29 publication-title: J Biol Chem doi: 10.1021/bi00427a056 – volume: 9 start-page: 3764 year: 2018 ident: 10707_CR27 publication-title: Food Funct doi: 10.1039/c8fo00604k – volume: 2015 start-page: 735087 year: 2015 ident: 10707_CR22 publication-title: Biomed Res Int doi: 10.1155/2015/735087 – volume: 50 start-page: 1201 year: 2012 ident: 10707_CR70 publication-title: Food Chem Toxicol doi: 10.1016/j.fct.2012.02.013 – volume: 10 start-page: 1 year: 2012 ident: 10707_CR93 publication-title: Curr Top Nutraceut R – volume: 21 start-page: 371 year: 2009 ident: 10707_CR98 publication-title: Nat Prod Res Dev – volume: 8 start-page: 235 year: 2002 ident: 10707_CR108 publication-title: J Pept Sci doi: 10.1002/psc.382 – volume: 25 start-page: 929 year: 2004 ident: 10707_CR54 publication-title: Peptides doi: 10.1016/j.peptides.2004.03.007 – volume: 55 start-page: 1792 year: 2017 ident: 10707_CR66 publication-title: Pharm Biol doi: 10.1080/13880209.2017.1325913 – volume: 30 start-page: 1253 year: 2019 ident: 10707_CR71 publication-title: Food Agric Immunol doi: 10.1080/09540105.2019.1686467 – volume: 81 start-page: 373 year: 2003 ident: 10707_CR85 publication-title: Biochem Cell Biol doi: 10.1139/o03-067 – volume: 20 start-page: 1163 year: 2018 ident: 10707_CR21 publication-title: Int J Med Mushrooms doi: 10.1615/IntJMedMushrooms.2018028430 – volume: 78 start-page: 699 year: 2000 ident: 10707_CR82 publication-title: Biochem Cell Biol doi: 10.1139/o00-087 – ident: 10707_CR99 doi: 10.1093/ecam/neq057 – volume: 84 start-page: 178 year: 2006 ident: 10707_CR90 publication-title: Biochem Cell Biol doi: 10.1139/o06-033 – volume: 6 start-page: 30010 year: 2016 ident: 10707_CR67 publication-title: Sci Rep doi: 10.1038/srep30010 – volume: 69 start-page: 212 year: 2003 ident: 10707_CR56 publication-title: Planta Med doi: 10.1055/s-2003-38492 – volume: 77 start-page: 311 year: 2008 ident: 10707_CR17 publication-title: Am Fam Physician – volume: 24 start-page: 307 year: 2019 ident: 10707_CR40 publication-title: Drug Discov Today doi: 10.1016/j.drudis.2018.09.014 – ident: 10707_CR52 doi: 10.1016/j.peptides.2004.03.013 – volume: 20 start-page: 537 year: 2018 ident: 10707_CR3 publication-title: Int J Med Mushrooms doi: 10.1615/IntJMedMushrooms.2018026264 – ident: 10707_CR35 doi: 10.1007/s00726-010-0791-0 – volume: 12 start-page: 2236 year: 2013 ident: 10707_CR8 publication-title: Mol Cell Proteomics doi: 10.1074/mcp.M113.030619 – volume: 2019 start-page: 15 year: 2019 ident: 10707_CR16 publication-title: Oxidative Med Cell Longev doi: 10.1155/2019/3139689 – volume: 228 start-page: 244 year: 1994 ident: 10707_CR30 publication-title: Eur J Biochem doi: 10.1111/j.1432-1033.1995.tb20256.x – volume: 243 start-page: 373 year: 2017 ident: 10707_CR51 publication-title: Food Chem doi: 10.1016/j.foodchem.2017.09.149 – volume: 33 start-page: 209 year: 2013 ident: 10707_CR113 publication-title: Int J Mol Med doi: 10.3892/ijmm.2013.1553 – volume: 24 start-page: 973 year: 2003 ident: 10707_CR87 publication-title: Peptides doi: 10.1016/S0196-9781(03)00190-6 – volume: 13 start-page: 3015 year: 2019 ident: 10707_CR48 publication-title: J Food Meas Charact doi: 10.1007/s11694-019-00222-4 – volume: 37 start-page: 747 year: 1964 ident: 10707_CR95 publication-title: Bull Chem Soc Jpn doi: 10.1246/bcsj.37.747 – volume: 23 start-page: 1361 year: 2002 ident: 10707_CR55 publication-title: Peptides doi: 10.1016/S0196-9781(02)00073-6 – volume: 26 start-page: 1005 year: 2018 ident: 10707_CR79 publication-title: J Food Drug Anal doi: 10.1016/j.jfda.2017.12.010 – ident: 10707_CR34 doi: 10.1007/s11427-011-4153-2 – volume: 17 start-page: 1040 year: 2010 ident: 10707_CR97 publication-title: Protein Pept Lett doi: 10.2174/092986610791498966 – ident: 10707_CR42 doi: 10.3390/ijms13056246 – volume: 1833 start-page: 987 year: 2012 ident: 10707_CR63 publication-title: Biochim Biophys Acta doi: 10.1016/j.bbamcr.2012.12.013 – volume: 61 start-page: 9828 year: 2013 ident: 10707_CR78 publication-title: J Agric Food Chem doi: 10.1021/jf4031184 – volume: 59 start-page: 94 year: 2013 ident: 10707_CR65 publication-title: Clin Chem doi: 10.1373/clinchem.2012.185389 – volume: 25 start-page: 935 year: 2004 ident: 10707_CR88 publication-title: Peptides doi: 10.1016/j.peptides.2004.03.008 – volume: 15 start-page: 557 year: 1997 ident: 10707_CR25 publication-title: Biochem J doi: 10.1042/bj3230557 – volume: 87 start-page: 593 year: 2004 ident: 10707_CR72 publication-title: Food Chem doi: 10.1016/j.foodchem.2004.01.015 – volume: 16 start-page: 90 year: 2014 ident: 10707_CR50 publication-title: Rev Colomb Biotecnol doi: 10.15446/rev.colomb.biote.v16n2.38747 – ident: 10707_CR36 doi: 10.1107/S1744309112051755 – ident: 10707_CR38 – volume: 285 start-page: 1071 year: 2001 ident: 10707_CR31 publication-title: Biochem Biophys Res Commun doi: 10.1006/bbrc.2001.5279 – volume: 92 start-page: S135 year: 2018 ident: 10707_CR18 publication-title: Eur J Cancer doi: 10.1016/S0959-8049(18)30629-4 – volume: 20 start-page: 693 year: 2009 ident: 10707_CR115 publication-title: J Microbiol Biotechnol doi: 10.4014/jmb.0911.11022 – volume: 50 start-page: 297 year: 2015 ident: 10707_CR9 publication-title: J Microbiol Immunol Infect doi: 10.1016/j.jmii.2015.07.013 – ident: 10707_CR43 doi: 10.1016/j.fct.2012.10.014 – volume: 128 start-page: 674 year: 2011 ident: 10707_CR62 publication-title: Food Chem doi: 10.1016/j.foodchem.2011.03.085 – volume: 174 start-page: 437 year: 2015 ident: 10707_CR105 publication-title: J Ethnopharmacol doi: 10.1016/j.jep.2015.08.042 – volume: 18 start-page: 374 year: 2011 ident: 10707_CR26 publication-title: Phytomedicine doi: 10.1016/j.phymed.2010.07.004 – volume: 56 start-page: 1729 year: 2012 ident: 10707_CR7 publication-title: Food Res doi: 10.1002/mnfr.201200316 – volume: 16 start-page: 198 year: 2009 ident: 10707_CR46 publication-title: Phytomedicine doi: 10.1016/j.phymed.2008.07.004 – volume: 17 start-page: 1037 year: 2015 ident: 10707_CR44 publication-title: Int J Med Mushrooms doi: 10.1615/intjmedmushrooms.v17.i11.30 – volume: 264 start-page: 714 year: 1999 ident: 10707_CR81 publication-title: Biochem Biophys Res Commun doi: 10.1006/bbrc.1999.1571 – volume: 82 start-page: 339 year: 2012 ident: 10707_CR37 publication-title: Protein Expr Purif doi: 10.1016/j.pep.2012.01.015 – ident: 10707_CR76 doi: 10.3892/ol.2016.5106 – volume: 81 start-page: 669 year: 2008 ident: 10707_CR96 publication-title: Appl Microbiol Biotechnol doi: 10.1007/s00253-008-1639-3 – ident: 10707_CR24 doi: 10.1038/nrc1994 – volume: 642 start-page: 212 year: 2017 ident: 10707_CR15 publication-title: Gene doi: 10.1016/j.gene.2017.10.080 – ident: 10707_CR100 doi: 10.2323/jgam.56.231 – ident: 10707_CR53 doi: 10.1016/j.peptides.2004.03.013 – volume: 45 start-page: 627 year: 2009 ident: 10707_CR111 publication-title: Process Biochem doi: 10.1016/j.procbio.2009.12.010 – volume: 7 start-page: 47 year: 2017 ident: 10707_CR117 publication-title: AMB Express doi: 10.1186/s13568-017-0346-9 – volume: 73 start-page: 3363 year: 2003 ident: 10707_CR59 publication-title: Life Sci doi: 10.1016/j.lfs.2003.06.023 – volume: 27 start-page: 1079 year: 2011 ident: 10707_CR41 publication-title: Oncol Rep doi: 10.3892/or.2011.1593 – volume: 97 start-page: 323 year: 2017 ident: 10707_CR75 publication-title: Int J Biol Macromol doi: 10.1016/j.ijbiomac.2017.01.043 – volume: 82 start-page: S1 year: 2016 ident: 10707_CR74 publication-title: Planta Med doi: 10.1055/s-0036-1596829 – volume: 324 start-page: 855 year: 2004 ident: 10707_CR89 publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2004.09.132 – ident: 10707_CR84 doi: 10.1006/bbrc.2001.5816 – volume: 61 start-page: 12044 year: 2013 ident: 10707_CR6 publication-title: J Agric Food Chem doi: 10.1021/jf4030272 – volume: 6 year: 2018 ident: 10707_CR106 publication-title: PeerJ doi: 10.7717/peerj.4940 – volume: 48 start-page: 658 year: 2010 ident: 10707_CR112 publication-title: Biochem Genet doi: 10.1007/s10528-010-9347-y – volume: 15 start-page: 5055 year: 2014 ident: 10707_CR1 publication-title: Asian Pac J Cancer Prev doi: 10.7314/APJCP.2014.15.12.5055 – volume: 312 start-page: 965 year: 2003 ident: 10707_CR86 publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2003.10.201 – volume: 99 start-page: 28 year: 2014 ident: 10707_CR114 publication-title: Biochimie doi: 10.1016/j.biochi.2013.10.016 – ident: 10707_CR91 doi: 10.1016/j.bbrc.2003.12.139 – volume: 46 start-page: 788 year: 1998 ident: 10707_CR104 publication-title: J Agric Food Chem doi: 10.1021/jf970551h – volume: 1770 start-page: 1593 year: 2007 ident: 10707_CR20 publication-title: BBA-Gen Subjects doi: 10.1016/j.bbagen.2007.07.014 – volume: 8 start-page: 3553 year: 2017 ident: 10707_CR110 publication-title: Food Funct doi: 10.1039/c7fo00895c – volume: 18 start-page: 769 year: 2016 ident: 10707_CR19 publication-title: Int J Med Mushrooms doi: 10.1615/IntJMedMushrooms.v18.i9.20 – ident: 10707_CR23 doi: 10.1016/j.biopha.2004.02.004 – ident: 10707_CR4 doi: 10.3390/ijms19102986 – volume: 13 start-page: 49 year: 2009 ident: 10707_CR64 publication-title: Korean J Physiol Pharmacol doi: 10.4196/kjpp.2009.13.1.49 – ident: 10707_CR45 doi: 10.1016/j.ijbiomac.2016.11.004 – volume: 45 start-page: 425 year: 2005 ident: 10707_CR12 publication-title: Crit Rev Food Sci Nutr doi: 10.1080/10408390591034445 – volume: 36 start-page: 5623 year: 2016 ident: 10707_CR28 publication-title: Anticancer Res doi: 10.21873/anticanres.11146 – ident: 10707_CR39 doi: 10.1021/jf500316f – volume: 12 year: 2017 ident: 10707_CR80 publication-title: PLoS One doi: 10.1371/journal.pone.0181748 – volume: 36 start-page: 441 year: 2016 ident: 10707_CR94 publication-title: Oncol Rep doi: 10.3892/or.2016.4830 – volume: 128 start-page: e881 year: 2009 ident: 10707_CR14 publication-title: Immunology doi: 10.1111/j.1365-2567.2009.03099.x – volume: 293 start-page: 857 year: 2002 ident: 10707_CR107 publication-title: Biochem Biophys Res Commun doi: 10.1016/S0006-291X(02)00301-7 |
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| Snippet | Severe side effects of chemotherapy as well as drug resistance highlight the ongoing need to discover novel natural bioactive compounds with anticancer... |
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| Title | Anticancer potentiality and mode of action of low-carbohydrate proteins and peptides from mushrooms |
| URI | https://link.springer.com/article/10.1007/s00253-020-10707-8 https://www.ncbi.nlm.nih.gov/pubmed/32556413 https://www.proquest.com/docview/2425728887 https://www.proquest.com/docview/3195330445 https://www.proquest.com/docview/2415289586 https://www.proquest.com/docview/2552040514 |
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