切换至 "中华医学电子期刊资源库"
高级检索
中华口腔医学研究杂志(电子版)

中华口腔医学研究杂志(电子版) ›› 2019, Vol. 13 ›› Issue (05) : 311 -316. doi: 10.3877/cma.j.issn.1674-1366.2019.05.009

所属专题： 口腔医学； 文献；

综述

交联剂在抑制基质金属蛋白酶与提高粘接耐久性领域的研究进展
鄢晓媛1, 陈玥1, 李轲1, 郑适泽2, 战德松3, 付佳乐3,†()   
  1. 1. 中国医科大学口腔医学院，沈阳　110002
    2. 吉林大学口腔医学院，长春　130021
    3. 中国医科大学口腔医学院口腔材料学教研室，中国医科大学附属口腔医院修复二科，沈阳　110002
  • 收稿日期:2019-05-09 出版日期:2019-10-01
  • 通信作者: 付佳乐

Research progress of crosslinkers in inhibiting matrix metalloproteinases and improving bonding durability

Xiaoyuan Yan1, Yue Chen1, Ke Li1, Shize Zheng2, Desong Zhan3, Jiale Fu3,†()   

  1. 1. School of Stomatology, China Medical University, Shenyang 110002, China
    2. School of Stomatology, Jilin University, Changchun 130021, China
    3. Department of Dental Materials Science, The 2nd Department of Prosthodontics, School & Hospital of Stomatology, China Medical University, Shenyang 110002, China
  • Received:2019-05-09 Published:2019-10-01
  • Corresponding author: Jiale Fu
  • About author:
    Corresponding author: Fu Jiale, Email:
  • Supported by:
    Innovation and Entrepreneurship Training Program for College Students of Liaoning Province(1111251703); New Teachers Fund of China Medical University(XZR20160015)
全文 ( ) 下载PDF ( ) 导出引用
引用本文：

鄢晓媛, 陈玥, 李轲, 郑适泽, 战德松, 付佳乐. 交联剂在抑制基质金属蛋白酶与提高粘接耐久性领域的研究进展[J]. 中华口腔医学研究杂志(电子版), 2019, 13(05): 311-316.

Xiaoyuan Yan, Yue Chen, Ke Li, Shize Zheng, Desong Zhan, Jiale Fu. Research progress of crosslinkers in inhibiting matrix metalloproteinases and improving bonding durability[J]. Chinese Journal of Stomatological Research(Electronic Edition), 2019, 13(05): 311-316.

基质金属蛋白酶（MMP）能够降解牙本质胶原纤维，是影响牙科粘接修复耐久性的重要因素。因此，抑制牙本质MMP的活性是提高粘接耐久性的关键。作为一种MMP抑制剂，交联剂不仅能够抑制MMP活性，还具备促进牙本质胶原纤维交联的作用，上述双重作用使交联剂能够提高牙本质粘接的耐久性。本文就常见交联剂在抑制MMP与提高牙本质粘接耐久性方面的研究进展进行综述。

关键词: 基质金属蛋白酶类, 酶抑制剂, 交联试剂, 牙本质粘接剂, 牙粘合, 粘接耐久性

The matrix metalloproteinases (MMPs) can degrade dentin collagen fibers, which plays an important role in affecting the bonding durability of dental restoration. Therefore, inhibiting the activity of dentin MMPs is the key to improve bonding durability. As inhibitors of MMPs, cross-linking agents can not only inhibit the activity of MMPs, but also promote the crosslinking of dentin collagen fibers. These two functions enable cross-linkers to improve dentin bonding. In this article, the research progress of common cross-linking agents in inhibiting MMPs and improving bonding durability of dentin was reviewed.

Key words: Matrix metalloproteinases, Enzyme inhibitors, Cross-linking reagents, Dentin bonding agents, Dental bonding, Bonding durability
[1]
Tjäderhane L, Larjava H, Sorsa T, et al. The activation and function of host matrix metalloproteinases in dentin matrix breakdown in caries lesions[J]. J Dent Res，1998，77(8): 1622-1629. DOI: 10.1177/00220345980770081001.
[2]
Tezvergil-Mutluay A, Mutluay M, Seseogullari-Dirihan R, et al. Effect of phosphoric acid on the degradation of human dentin matrix[J]. J Dent Res，2013，92(1): 87-91. DOI: 10.1177/0022034512466264.
[3]
Mazzoni A, Pashley DH, Nishitani Y, et al. Reactivation of inactivated endogenous proteolytic activities in phosphoric acid-etched dentine by etch-and-rinse adhesives[J]. Biomaterials，2006，27(25): 4470-4476. DOI: 10.1016/j.biomaterials.2006.01.040.
[4]
Frassetto A, Breschi L, Turco G, et al. Mechanisms of degradation of the hybrid layer in adhesive dentistry and therapeutic agents to improve bond durability--A literature review[J]. Dent Mater，2016，32(2): e41-e53. DOI: 10.1016/j.dental.2015.11.007.
[5]
Sabatini C, Pashley DH. Mechanisms regulating the degradation of dentin matrices by endogenous dentin proteases and their role in dental adhesion. A review[J]. Am J Dent，2014，27(4): 203-214.
[6]
孙素，肖玉鸿.基质金属蛋白酶介导牙本质粘接界面的生物降解及其拮抗剂的研究进展[J/CD].中华口腔医学研究杂志（电子版），2015，9(4): 333-336. DOI: 10.3877/cma.j.issn.1674-1366.2015.04.017.
[7]
贾玲玲，万乾炳.基质金属蛋白酶抑制剂的研究进展[J].华西口腔医学杂志，2017，35(2): 208-214. DOI: 10.7518/hxkq.2017.02.019.
[8]
Tjäderhane L, Nascimento FD, Breschi L, et al. Strategies to prevent hydrolytic degradation of the hybrid layer-A review[J]. Dent Mater，2013，29(10): 999-1011. DOI: 10.1016/j.dental.2013.07.016.
[9]
Bedran-Russo AK, Pauli GF, Chen SN, et al. Dentin biomodification：strategies，renewable resources and clinical applications[J]. Dent Mater，2014，30(1): 62-76. DOI: 10.1016/j.dental.2013.10.012.
[10]
Priyadarshini BM, Lu TB, Fawzy AS. Effect of photoactivated riboflavin on the biodegradation-resistance of root-dentin collagen[J]. J Photochem Photobiol B，2017，177: 18-23. DOI: 10.1016/j.jphotobiol.2017.10.012.
[11]
Jain K, Beri L, Kunjir K, et al. Comparative evaluation of the effect of 10% sodium ascorbate，10% hesperidin，1% riboflavin 5 phosphate，collagen cross-linkers，on the pushout bond strength of fiber postluted to radicular dentin：In vitro study[J]. J Conserv Dent，2018，21(1): 95-99. DOI: 10.4103/jcd.Jcd_116_17.
[12]
Cova A, Breschi L, Nato F, et al. Effect of UVA-activated riboflavin on dentin bonding[J]. J Dent Res，2011，90(12): 1439-1445. DOI: 10.1177/0022034511423397.
[13]
Daood U, Matinlinna JP, Fawzy AS. Synergistic effects of VE-TPGS and riboflavin in crosslinking of dentine[J]. Dent Mater，2019，35(2): 356-367. DOI: 10.1016/j.dental.2018.11.031.
[14]
Hiraishi N, Sono R, Sofiqul I, et al. In vitro evaluation of plant-derived agents to preserve dentin collagen[J]. Dent Mater，2013，29(10): 1048-1054. DOI: 10.1016/j.dental.2013.07.015.
[15]
Sabatini C, Scheffel DL, Scheffel RH, et al. Inhibition of endogenous human dentin MMPs by Gluma[J]. Dent Mater，2014，30(7): 752-758. DOI: 10.1016/j.dental.2014.04.006.
[16]
Seseogullari-Dirihan R, Mutluay MM, Pashley DH, et al. Is the inactivation of dentin proteases by crosslinkers reversible？[J]. Dent Mater，2017，33(2): e62-e68. DOI: 10.1016/j.dental.2016.09.036.
[17]
Migneault I, Dartiguenave C, Bertrand MJ, et al. Glutaraldehyde：behavior in aqueous solution，reaction with proteins，and application to enzyme crosslinking[J]. Biotechniques，2004，37(5): 790-796，798-802. DOI: 10.2144/04375rv01.
[18]
Chen C, Mao C, Sun J, et al. Glutaraldehyde-induced remineralization improves the mechanical properties and biostability of dentin collagen[J]. Mater Sci Eng C Mater Biol Appl，2016，67: 657-665. DOI: 10.1016/j.msec.2016.05.076.
[19]
Hass V, Luque-Martinez IV, Gutierrez MF, et al. Collagen cross-linkers on dentin bonding：Stability of the adhesive interfaces，degree of conversion of the adhesive，cytotoxicity and in situ MMP inhibition[J]. Dent Mater，2016，32(6): 732-741. DOI: 10.1016/j.dental.2016.03.008.
[20]
Singh P, Nagpal R, Singh UP, et al. Effect of carbodiimide on the structural stability of resin/dentin interface[J]. J Conserv Dent，2016，19(6): 501-509. DOI: 10.4103/0972-0707.194020.
[21]
Tezvergil-Mutluay A, Mutluay MM, Agee KA, et al. Carbodiimide cross-linking inactivates soluble and matrix-bound MMPs，in vitro[J]. J Dent Res，2012，91(2): 192-196. DOI: 10.1177/0022034511427705.
[22]
Seseogullari-Dirihan R, Mutluay MM, Tjäderhane L, et al. Effect of pH on dentin protease inactivation by carbodiimide[J]. Eur J Oral Sci，2017，125(4): 288-293. DOI: 10.1111/eos.12354.
[23]
Scheffel DL, Hebling J, Scheffel RH, et al. Stabilization of dentin matrix after cross-linking treatments，in vitro[J]. Dent Mater，2014，30(2): 227-233. DOI: 10.1016/j.dental.2013.11.007.
[24]
Mazzoni A, Angeloni V, Comba A, et al. Cross-linking effect on dentin bond strength and MMPs activity[J]. Dent Mater，2018，34(2): 288-295. DOI: 10.1016/j.dental.2017.11.009.
[25]
Mazzoni A, Apolonio FM, Saboia VP, et al. Carbodiimide inactivation of MMPs and effect on dentin bonding[J]. J Dent Res，2014，93(3): 263-268. DOI: 10.1177/0022034513516465.
[26]
Shafiei F, Firouzmandi M, Zamanpour M. The effect of two cross-linking agents on dentin bond strength of resin-modified glass ionomer[J]. Eur J Dent，2017，11(4): 486-490. DOI: 10.4103/ejd.ejd_258_17.
[27]
Maravic T, Breschi L, Comba A, et al. Experimental use of an acrolein-based primer as collagen cross-linker for dentine bonding[J]. J Dent，2018，68: 85-90. DOI: 10.1016/j.jdent.2017.11.006.
[28]
Balalaie A, Rezvani MB, Mohammadi Basir M. Dual function of proanthocyanidins as both MMP inhibitor and crosslinker in dentin biomodification：A literature review[J]. Dent Mater J，2018，37(2): 173-182. DOI: 10.4012/dmj.2017-062.
[29]
Liu RR, Fang M, Zhang L, et al. Anti-proteolytic capacity and bonding durability of proanthocyanidin-biomodified demineralized dentin matrix[J]. Int J Oral Sci，2014，6(3): 168-174. DOI: 10.1038/ijos.2014.22.
[30]
Epasinghe DJ, Yiu CK, Burrow MF, et al. The inhibitory effect of proanthocyanidin on soluble and collagen-bound proteases[J]. J Dent，2013，41(9): 832-839. DOI: 10.1016/j.jdent.2013.06.002.
[31]
Hass V, Luque-Martinez I, Muñoz MA, et al. The effect of proanthocyanidin-containing 10% phosphoric acid on bonding properties and MMP inhibition[J]. Dent Mater，2016，32(3): 468-475. DOI: 10.1016/j.dental.2015.12.007.
[32]
刘瑞瑞，方明，赵三军，等.原花青素对树脂-牙本质粘接界面耐冷热循环老化作用的影响[J].中华口腔医学杂志，2012，47(5): 268-272. DOI: 10.3760/cma.j.issn.1002-0098.2012.05.004.
[33]
Parise Gré C, Pedrollo Lise D, Ayres AP, et al. Do collagen cross-linkers improve dentin′s bonding receptiveness？[J]. Dent Mater，2018，34(11): 1679-1689. DOI: 10.1016/j.dental.2018.08.303.
[34]
Hechler B, Yao X, Wang Y. Proanthocyanidins alter adhesive/dentin bonding strengths when included in a bonding system[J]. Am J Dent，2012，25(5): 276-280.
[35]
Savickiene N, Jekabsone A, Raudone L, et al. Efficacy of Proanthocyanidins from Pelargonium sidoides Root Extract in Reducing P.gingivalis Viability While Preserving Oral Commensal S.salivarius[J]. Materials（Basel），2018，11(9): 1499. DOI: 10.3390/ma11091499.
[36]
慈向科，陈丽培，欧晓艳.葡萄籽原花青素对牙龈卟啉单胞菌内毒素的影响[J].上海口腔医学，2015，24(4): 433-436.
[37]
Kim GE, Leme-Kraus AA, Phansalkar R, et al. Effect of Bioactive Primers on Bacterial-Induced Secondary Caries at the Tooth-Resin Interface[J]. Oper Dent，2017，42(2): 196-202. DOI: 10.2341/16-107-L.
[38]
Silva AP, Gonçalves RS, Borges AF, et al. Effectiveness of plant-derived proanthocyanidins on demineralization on enamel and dentin under artificial cariogenic challenge[J]. J Appl Oral Sci，2015，23(3): 302-309. DOI: 10.1590/1678-775720140304.
[39]
Varoni EM, Vijayakumar S, Canciani E, et al. Chitosan-Based Trilayer Scaffold for Multitissue Periodontal Regeneration[J]. J Dent Res，2018，97(3): 303-311. DOI: 10.1177/0022034517736255.
[40]
Qian Y, Song JL, Sun P, et al. Lactobacillus casei Strain Shirota Enhances the In Vitro Antiproliferative Effect of Geniposide in Human Oral Squamous Carcinoma HSC-3 Cells[J]. Molecules，2018，23(5): 1069. DOI: 10.3390/molecules23051069.
[41]
Shindo S, Hosokawa Y, Hosokawa I, et al. Genipin inhibits MMP-1 and MMP-3 release from TNF-a-stimulated human periodontal ligament cells[J]. Biochimie，2014，107 Pt B: 391-395. DOI: 10.1016/j.biochi.2014.10.008.
[42]
王玉睿，沙鑫家，轩昆，等.京尼平预处理对牙本质-树脂粘结面即刻和老化后粘结强度的影响[J].牙体牙髓牙周病学杂志，2014，24(9): 526-529. DOI: 10.3969/j.issn.1005-2593.2014.09.007.
[43]
谢丹丹，麦穗，吴倩，等.氧化海藻酸钠预处理提高树脂牙本质粘接的耐久性[J/CD].中华口腔医学研究杂志（电子版），2018，12(6): 329-334. DOI: 10.3877/cma.j.issn.1674-1366.2018.06.001.
[44]
Buzalaf MA, Kato MT, Hannas AR. The role of matrix metalloproteinases in dental erosion[J]. Adv Dent Res，2012，24(2): 72-76. DOI: 10.1177/0022034512455029.
[45]
Bae JY, Choi JS, Choi YJ, et al. （-）Epigallocatechin gallate hampers collagen destruction and collagenase activation in ultraviolet-B-irradiated human dermal fibroblasts：involvement of mitogen-activated protein kinase[J]. Food Chem Toxicol，2008，46(4): 1298-1307. DOI: 10.1016/j.fct.2007.09.112.
[46]
Zarella BL, Buzalaf MA, Kato MT, et al. Cytotoxicity and effect on protease activity of copolymer extracts containing catechin[J]. Arch Oral Biol，2016，65: 66-71. DOI: 10.1016/j.archoralbio.2016.01.017.
[47]
Vidal CM, Aguiar TR, Phansalkar R, et al. Galloyl moieties enhance the dentin biomodification potential of plant-derived catechins[J]. Acta Biomater，2014，10(7): 3288-3294. DOI: 10.1016/j.actbio.2014.03.036.
[48]
孙秋榕，古丽莎，武诗语，等.表没食子儿茶素没食子酸酯对脱矿牙本质粘接面改性的研究[J].中华口腔医学杂志，2016，51(3): 148-153. DOI: 10.3760/cma.j.issn.1002-0098.2016.03.005.
[49]
Yang H, Guo J, Deng D, et al. Effect of adjunctive application of epigallocatechin-3-gallate and ethanol-wet bonding on adhesive-dentin bonds[J]. J Dent，2016，44: 44-49. DOI: 10.1016/j.jdent.2015.12.001.
[50]
Fialho MPN, Hass V, Nogueira RP, et al. Effect of epigallocatechin-3- gallate solutions on bond durability at the adhesive interface in caries-affected dentin[J]. J Mech Behav Biomed Mater，2019，91: 398-405. DOI: 10.1016/j.jmbbm.2018.11.022.
[51]
Carvalho C, Fernandes FP, Freitas Vda P, et al. Effect of green tea extract on bonding durability of an etch-and-rinse adhesive system to caries-affected dentin[J]. J Appl Oral Sci，2016，24(3): 211-217. DOI: 10.1590/1678-775720150518.
[52]
Khamverdi Z, Rezaei-Soufi L, Rostamzadeh T. The Effect of Epigallocatechin Gallate on the Dentin Bond Durability of Two Self-etch Adhesives[J]. J Dent （Shiraz），2015，16(2): 68-74.
[53]
Yallapu MM, Jaggi M, Chauhan S. Curcumin Nanomedicine：A Road to Cancer Therapeutics[J]. Current pharmaceutical design，2013，19(11): 1994-2010.
[54]
Farhood B, Mortezaee K, Goradel NH, et al. Curcumin as an anti-inflammatory agent：Implications to radiotherapy and chemotherapy[J]. J Cell Physiol，2019，234(5): 5728-5740. DOI: 10.1002/jcp.27442.
[55]
Seseogullari-Dirihan R, Apollonio F, Mazzoni A, et al. Use of crosslinkers to inactivate dentin MMPs[J]. Dent Mater，2016，32(3): 423-432. DOI: 10.1016/j.dental.2015.12.012.
[56]
Seseogullari-Dirihan R, Mutluay MM, Vallittu P, et al. Effect of pretreatment with collagen crosslinkers on dentin protease activity[J]. Dent Mater，2015，31(8): 941-947. DOI: 10.1016/j.dental.2015.05.002.
[57]
贾斌，董颖韬，苗莉，等.姜黄素对人牙周膜干细胞增殖及炎症因子表达的影响[J].牙体牙髓牙周病学杂志，2018，28(3): 131-135. DOI: 10.15956/j.cnki.chin.j.conserv.dent.2018.03.002.
[58]
卞雨晴，马一丹，代东跃，等.单宁酸的生物学特征及在医学和口腔医学领域的应用价值[J].中国组织工程研究，2019，23(2): 284-290. DOI: 10.3969/j.issn.2095-4344.1516.
[59]
荆才，罗志军，胡鹏刚，等.反萃取降低高纯单宁酸生产中没食子酸残留量的应用[J].中国酿造，2017，36(3): 156-159. DOI: 10.11882/j.issn.0254-5071.2017.03.031.
[60]
Boruziniat A, Babazadeh M, Gifani M, et al. Effect of Tannic Acid Application on Durability of Bond of Etch and Rinse Adhesive Resins[J]. Journal of Dental Materials and Techniques，2017，6(3): 125-130. DOI: 10.22038/jdmt.2017.9014.
[61]
Bedran-Russo AK, Yoo KJ, Ema KC, et al. Mechanical properties of tannic-acid-treated dentin matrix[J]. J Dent Res，2009，88(9): 807-811. DOI: 10.1177/0022034509342556.
[62]
徐国发，郑适萍，张建博，等.单宁酸在不同PH缓冲液条件下的含量变化[J].云南中医药杂志，2015，36(6): 88-90.
[63]
Bhargava P, Verma VK, Malik S, et al. Hesperidin regresses cardiac hypertrophy by virtue of PPAR-gamma agonistic，anti-inflammatory，antiapoptotic，and antioxidant properties[J]. J Biochem Mol Toxicol，2019，33(5): e22283. DOI: 10.1002/jbt.22283.
[64]
Hiraishi N, Maruno T, Tochio N, et al. Hesperidin interaction to collagen detected by physico-chemical techniques[J]. Dent Mater，2017，33(1): 33-42. DOI: 10.1016/j.dental.2016.09.035.
[65]
Liu Z, Li F, Zhang L, et al. The effect of active components from citrus fruits on dentin MMPs[J]. Arch Oral Biol，2017，83: 111-117. DOI: 10.1016/j.archoralbio.2017.07.006.
[66]
Islam MS, Hiraishi N, Nassar M, et al. Effect of hesperidin incorporation into a self-etching primer on durability of dentin bond[J]. Dent Mater，2014，30(11): 1205-1212. DOI: 10.1016/j.dental.2014.08.371.
[67]
王践云，金娟，叶文靖，等.新型天然交联剂氧化海藻酸钠制备及其性能研究[J].化学试剂，2009，31(2): 97-100. DOI: 10.3969/j.issn.0258-3283.2009.02.005.
[1] 王青青, 耿翠芝, 苏晓雨, 彭玉晓, 秦明祎, 刘风侠. 乳腺癌芳香化酶抑制剂相关肌肉骨骼不良反应的研究进展[J]. 中华乳腺病杂志(电子版), 2023, 17(04): 243-249.
[2] 杨继鑫, 李南林. 细胞周期蛋白依赖激酶4和6抑制剂研究进展[J]. 中华乳腺病杂志(电子版), 2021, 15(05): 315-319.
[3] 李兴, 李震, 肖方骏, 翁家贤, 潘建科, 何沛恒, 苏海涛. 微小RNA-27b-3p与基质金属蛋白酶13在人软骨细胞的对应关系[J]. 中华关节外科杂志(电子版), 2022, 16(04): 431-440.
[4] 林昌盛, 战军, 肖雪. 上皮性卵巢癌患者诊疗中基因检测及分子靶向药物治疗[J]. 中华妇幼临床医学杂志(电子版), 2023, 19(05): 505-510.
[5] 刘锐, 王树明. 丙戊酸钠抗休克作用及其相关机制的研究进展[J]. 中华损伤与修复杂志(电子版), 2022, 17(04): 359-362.
[6] 李咏生, 孙建国, 李梦侠, 重庆肺癌精准治疗协作组(CPLOG). 第三代EGFR-TKI耐药后诊疗策略专家共识[J]. 中华肺部疾病杂志(电子版), 2023, 16(02): 145-155.
[7] 沈冶中, 胡智刚, 吴黎明, 伍宏玲. EGFR-TKI联合放疗对NSCLC脑转移的临床分析[J]. 中华肺部疾病杂志(电子版), 2022, 15(06): 844-846.
[8] 陈俞坊, 王康, 吴文昊, 张厚丽, 周向东. EGFR敏感突变ⅠA期浸润性肺腺癌术后辅助靶向治疗预后分析[J]. 中华肺部疾病杂志(电子版), 2022, 15(06): 776-781.
[9] 饶汕, 陈瑞, 吕晶. EGFR-TKI化疗后NSCLC肺叶切除术的疗效分析[J]. 中华肺部疾病杂志(电子版), 2022, 15(05): 700-702.
[10] 甘开梅, 黄剑. 肺癌干细胞对EGFR-TKI耐药影响的研究进展[J]. 中华细胞与干细胞杂志(电子版), 2023, 13(01): 36-44.
[11] 杨秀君, 崔梦莹, 张丹, 曲仙智, 苗云皓, 盛基尧, 郑戈, 刘水, 张学文. 信迪利单抗联合仑伐替尼成功转化治疗不可切除肝癌一例[J]. 中华肝脏外科手术学电子杂志, 2023, 12(05): 581-584.
[12] 佘重阳, 卢弘. Janus激酶抑制剂在幼年特发性关节炎相关葡萄膜炎治疗中的研究进展[J]. 中华眼科医学杂志(电子版), 2023, 13(02): 104-108.
[13] 黄晴, 赵瑞珩, 钱惠英. PCI-24781诱导SKOV-3细胞凋亡及相关机制的研究[J]. 中华临床医师杂志(电子版), 2022, 16(08): 775-781.
[14] 马文文, 呼敏, 王贵红, 高健. miR-103a-2、miR-122和vaspin在非酒精性脂肪性肝病合并HBV感染中的表达及意义[J]. 中华临床医师杂志(电子版), 2022, 16(02): 170-174.
[15] 李娜, 李军, 郭李平, 王海雄. 血管紧张素受体脑啡肽酶抑制剂在心律失常患者中的应用[J]. 中华心脏与心律电子杂志, 2023, 11(01): 39-44.
阅读次数
全文


摘要

版权所有 中华医学会 中华医学电子音像出版社有限责任公司  京ICP备14006079号-1  网络出版服务许可证：(署)网出证(京)字第075号