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101.
大孔树脂在三七叶皂苷脱色中的应用研究 总被引:4,自引:0,他引:4
目的:解决三七叶总皂苷提取中的脱色工艺技术。方法:组合大孔树脂法。结果:应用组合大孔吸附树脂,在碱性条件下多级脱色,较好地解决了三七叶总皂苷脱色困难,并实施了大规模产业化。 相似文献
102.
氟罗沙星的体内外试验相关性研究 总被引:4,自引:1,他引:3
本文研究了新型喹诺酮类药物氟罗沙星体外溶出与体内吸收之间的相关性。实验表明,本品口服吸收在血清中达峰时间较快,作用持久,消除半衰期为9.60hr。在人工胃液中溶出速率较快,在血清达峰之前,体内吸收与体外溶出量之间呈现良好的相关性。 相似文献
103.
二步冷冻保存同种异体骨-ACL-骨移植后排斥反应的影响 总被引:3,自引:0,他引:3
目的 :探讨新鲜异体和二步冷冻保存同种异体骨 前交叉韧带 (ACL) 骨移植后排斥反应的差异。方法 :将 6 0只新西兰兔和 6 0只日本大耳兔分别随机分成自体骨 ACL 骨移植组、新鲜异体骨 ACL 骨移植组和二步冷冻保存同种异体骨 ACL 骨移植组 ,分别于术前及术后 1周、2周、3周、4周各采血 2ml测定血清中白细胞介素 2 (IL 2 )水平 ,术后 4周、12周切取移植关节 ,作苏木精 -伊红染色。结果 :光镜下检查显示 ,自体移植组和二步冷冻保存移植组均未见明显炎性细胞浸润 ,胶原排列规则 ,分化成熟。新鲜异体移植组有大量淋巴细胞浸润 ,其IL 2水平明显高于自体移植组和二步冷冻保存同种异体移植组且高于术前水平 (P <0 .0 1)。结论 :二步冷冻减轻了同种异体骨 ACL 骨移植后排斥反应 ,移植后其组织学改变同自体移植相似 相似文献
104.
目的 :观察氨中毒损伤上呼吸道的症状及治疗效果。方法 :回顾分析急性氨中毒致上呼吸道损伤1 67例的临床资料。结果 :患者均愈后良好 ,无因上呼吸道损伤而死亡的病例 ,有少数患者遗留声嘶及慢性咽炎。结论 :在急性氨中毒致上呼吸道损伤患者的救治过程中合理应用糖皮质激素、酸性雾化液及抗生素至关重要。 相似文献
105.
激光光凝联合玻璃体腔注气治疗玻璃体切割术后再发黄斑孔 总被引:1,自引:0,他引:1
目的 探讨激光光凝联合玻璃体腔注气治疗玻璃体切割术后再发与未愈黄斑孔的疗效。方法 应用COHERENT Omni多波长激光光凝黄斑裂孔底部的视网膜色素上皮层。随后眼内注入20%C3F80.5~0.8ml并置换出玻璃体腔液体。治疗后每天坚持俯卧位。结果 19只眼中16只眼黄斑孔愈合,成功率为84.2%,视力提高15只眼,占78.9%,未出现严重的并发症。结论 应用激光光凝联合眼内注气治疗玻璃体切割术后再发与未愈黄斑孔具有方法简单、费用低、疗效确定、大部分患者无须住院等优点。 相似文献
106.
昆明种小鼠56只,在两个海拔高度上(300m和5000m)各分为两个组(对照组和复合组),分别给予相应的处理因素后,检测其血浆ANP水平和游泳时间。结果表明,小鼠在海拔5000m生活48h后,其血浆ANP较海拔300m小鼠降低52.87%,而其游泳时间则增长91.59%;在两个海拔高度上,复合组血浆ANP都较对照组降低,而游泳时间都长于对照组.提示复合方案提高高原劳动能力的机理,可能与降低体内血浆ANP水平有关。 相似文献
107.
Is neurogenesis reparative after status epilepticus? 总被引:1,自引:0,他引:1
108.
本文报道人精液抑制素的制备及其生物学特性。收集的新鲜人精液经乙醇沉淀和丙酮冲洗,获得的粗提物经Sephadex G100处理,产生具有高活性抑制素hP2组分。应用hP2测定使去势雄性大鼠增高的血清FSH水平降低。其生物特性:hP2的生物活性按单位重量计算为粗提物的10倍以上,包含16种氨基酸,通过SDS-PAGE计算分子量为11,500道尔顿。 相似文献
109.
Jeffrey E. Fletcher Marcy Hubert Steven J. Wieland Qi-Hua Gong Ming-Shi Jiang 《Toxicon》1996,34(11-12)
Myonecrosis induced in vivo by cardiotoxin, melittin, and Asp49 and Lys49 phospholipase A2 (PLA2) myotoxins involves rapid lysis of the sarcolemma, myofibril clumping, and hypercontraction of sarcomeres. In contrast, skeletal muscle necrosis induced by crotamine and myotoxin a is much slower, consisting of mitochondrial and sarcoplasmic reticulum swelling, myofibril degeneration, and lack of sarcolemma or transverse tubule damage. The mechanisms contributing to the myonecrosis induced by these peptides were evaluated. Two cardiotoxins and two Lys49 PLA2 myotoxins lysed primary cultures of human skeletal muscle within 24 hr at a concentration of 0.25 μM, while melittin, crotamine, and myotoxin a, and an Asp49 PLA2 myotoxin were non-cytolytic at concentrations up to 5.0 μM, suggesting that cytolysis is not a good measure of myotoxicity. Crotamine and the Lys49 PLA2 myotoxin altered Ca2+ ion flux in human heavy sarcoplasmic reticulum by opening the ryanodine receptor. Whole-cell patch-clamp studies demonstrated that administrating crotamine intracellularly increased Na+ currents. Free fatty acids, liberated by activation of tissue phospholipase C or by the PLA2 activity of the myotoxins, were monitored for crotamine, myotoxin a and a Lys49 PLA2 myotoxin in cell cultures in which the lipids had been radiolabeled. Only the Lys49 myotoxin produced significant amounts of fatty acid in cell cultures, supporting a potential role for fatty acid production only in the mechanism of sarcolemma-destroying myotoxins. These findings, coupled with those in the literature, support a hypothesis in which the myotoxins and/or products of lipase activity (e.g. fatty acids) are acting at a site existing on both the Na+ channel and a protein involved in Ca2+ release and probably serving a modulatory function for ion regulation. Based on the similarities in mechanisms between the toxins and fatty acids, the most likely site would be a fatty acid binding site on the protein (either similar to that on fatty acid binding proteins, or an acylated cysteine residue) or in the membrane. 相似文献
110.
Proteolytic Processing Mechanisms in the Biosynthesis of Neuroendocrine Peptides: The Subtilisin-like Proprotein Convertases 总被引:1,自引:0,他引:1
Yves Rouill Stephen J. Duguay Kaare Lund Machi Furuta Qiuming Gong Gregory Lipkind Anthony A. Oliva Jr. Shu Jin Chan Donald F. Steiner 《Frontiers in neuroendocrinology》1995,16(4)
The recent discovery of a novel family of precursor processing endoproteases has greatly accelerated progress in understanding the complex mechanisms underlying the maturation of prohormones, neuropeptides, and many other precursor-derived proteins. At least six members of this family have been found thus far in mammalian species, several having alternatively spliced isoforms, and related enzymes have been identified in many invertebrates, including molluscs, insects, nematodes, and coelenterates. The proprotein convertases are all dependent on calcium for activity and all possess highly conserved subtilisin-like domains with the characteristic catalytic triad of this serine protease (ordered Asp, His, and Ser along the polypeptide chain). Two members of this family, PC2(SPC2) and PC1/PC3(SPC3), appear to play a preeminent role in neuroendocrine precursor processing. Both convertases are expressed only in the brain and in the extended neuroendocrine system, while another important family member—furin/PACE (SPC1)—is expressed more ubiquitously, in almost all tissues, and at high levels in liver. SPC2 and SPC3 exhibit acidic pH optima and other properties which enhance their activity in the acidic, calcium-enriched environment of the dense-core secretory granules of the regulated pathway in neuroendocrine cells, while furin has a neutral pH optimum and is localized predominantly to the trans Golgi network where it is retained by a C-terminal transmembrane domain. Furin processes a wide variety of precursors in the constitutive pathway, such as those of growth factors, receptors, coagulation factors, and viral glycoproteins. Recent findings on the processing of proopiomelanocortin, proinsulin, proglucagon, and several other neuroendocrine precursors by SPC2 and SPC3 are discussed, along with information on the structure, properties, evolution, developmental expression, and regulation or the convertases. An inherited defect in the fat/fat mouse which affects the processing of proinsulin, and probably also many other prohormones, due to a point mutation in carboxypeptidase E has recently been identified and has begun to provide new insights into the functional integration of the individual processing steps. 相似文献