以TPCP工艺开发690 MPa级超低碳贝氏体钢

采用Mn-Ni-Cu-B系合金，在4200mm轧机上实行Ⅲ型控轧，以ACC装置进行轧后冷却，开发出超低碳贝氏体钢（ULCB）50mm厚板，其抗拉强度达到70kg级，低温冲击性能优良，这为开发80kg级ULCB钢打下了基础。     

工程机械用高强度钢板控轧控冷工艺的开发

为开发强度级别为６８５ＭＰａ的高强钢板的控轧控冷工艺,研究了终轧温度,未再结晶区累积压下量,终冷温度,冷却速度等工艺参数对钢的显微组织和力学性能的影响。实验结果表明,在控轧控冷条件下,钢的室温显微组织由铁素体和贝氏体组成,贝氏体主要以粒状贝氏体为主,此外,晶粒细化是提高钢的强度和韧性的最有效的手段。     

厚板的控制轧制和控制冷却

厚板控轧控冷的目的是赋予其优良的韧性。控轧是在合金成分合适的前提下选择板坯的加热条件和轧制条件，使钢晶粒细化，提高韧性。控制冷却增大了相变组织强化的比重。从韧性观点来看，最理想的是在控制冷却的同时使铁素体晶粒细化，同时控制贝氏体和珠光体的弥散状态，防止生成岛状马氏体。控制冷却技术与控制轧制相结合，可以有效地用于钢的强韧性处理。经过控制冷却的厚钢板，显微组织均匀，明显细化，韧性提高，并可提高抗脆裂性和抗氢脆能力。今后用控制冷却生产厚板的比重将越来越大。     

DH36级高强度船板轧制技术开发

为适应造船业发展的需要,生产市场所需的高强度船板,天钢中厚板厂利用3500mm双机架轧机和ACC层流冷却系统等自身设备能力的优势,进行了DH36级高强度船板轧制技术的开发,试轧了16mm和30mm两个规格的DH36级高强度船板。采用了合理的成分设计和控轧控冷技术,对加入不同合金元素的船板分析比较了试轧制的过程与结果,证明Nb系高强船板钢轧制工艺制度较优,为工业生产提供了依据。     

Nb微合金化16MnK钢板的生产

Q345级钢的传统生产工艺是采用钒微合金处理，提高强度，达到所需性能。本文结合济钢16MnK钢板的生产探讨Nb微合金化Q345B钢的生产工艺及控轧工艺对性能的影响。     

控轧技术在H型钢生产中的应用

根据钢板的控轧经验，结合H型钢轧制的特点分析控轧在轧制中运用的具体问题，制定H型钢控轧工艺方案。介绍了实际应用情况，并提出改进的措施。     

轧制工艺对Nb微合金H型钢性能的影响

采用透射电镜、电解法对铌（Nb）微合金H型钢析出相进行分析,利用显微镜研究加热温度对奥氏体晶粒度的影响,以及通过轧制试验研究未再结晶区压下率和终轧温度对试验钢性能的影响,制定出微合金H型钢控轧工艺。该工艺应用于微合金H型钢工业生产,其实际晶粒度11级,屈服强度为400~420 MPa,-20℃横向夏比冲击功大于45 J,产品性能满足日标H型钢要求。     

高建筑用Q345GJC-Z35特厚钢板的研制

 利用250mm连铸坯料,在3800mm宽厚板轧机上针对Q345GJC-Z35钢种进行了厚50～80mm钢板的TMCP工艺试验,确定了相应的热轧及控冷工艺条件。结果表明：采用碳的质量分数低于0.11%添加微量复合铌、钒、钛元素,按照2阶段控制,当轧到成品钢板厚度的2～3倍时开始待温,精轧开轧温度小于860℃,终轧温度为820～860℃,生产的Q345GJC-Z35高强度厚板的性能完全超出国家标准GB19879—2005要求,而且其钢板的平均断面收缩率都大于50%,远高于Z35钢板的技术要求。实现了钢板很好的强韧性匹配,工艺上不用后续热处理,减少了工艺流程,节约了成本。     

层流冷却在南钢中厚板卷厂的应用

轧后快冷，配合成份优化和控制轧制，可以使钢材获得良好的强韧性和焊接性能。本文介绍了南钢申厚板卷生产线上轧后控冷系统的选型、布置、结构特点、工艺特点和应用。该系统具有维护简单、控制灵活、冷却均匀、冷却能力强的特点，使南钢具备生产综合性能良好的钢板和钢卷的能力。并已经成功生产出X65管线钢和D36高强船板等高附加值产品。     

控轧控冷低碳Mn─Nb─RE钢中微细粒子沉淀强化

测定了控轧控冷低碳Ｍｎ─Ｎｂ─ＲＥ钢中析出相微细粒子化学成分、直径及形状因子；研究了控冷冷却速度对微细粒子直径、形状因子及屈服强度增量的影响和控轧控冷铌钢屈服强度增量与微细粒子平均直径的关系；探讨了析出相微细粒子的强化作用机理。     

BAG-1 modulates the chaperone activity of Hsp70/Hsc70

The 70 kDa heat shock family of molecular chaperones is essential to a variety of cellular processes, yet it is unclear how these proteins are regulated in vivo. We present evidence that the protein BAG-1 is a potential modulator of the molecular chaperones, Hsp70 and Hsc70. BAG-1 binds to the ATPase domain of Hsp70 and Hsc70, without requirement for their carboxy-terminal peptide-binding domain, and can be co-immunoprecipitated with Hsp/Hsc70 from cell lysates. Purified BAG-1 and Hsp/Hsc70 efficiently form heteromeric complexes in vitro. BAG-1 inhibits Hsp/Hsc70-mediated in vitro refolding of an unfolded protein substrate, whereas BAG-1 mutants that fail to bind Hsp/Hsc70 do not affect chaperone activity. The binding of BAG-1 to one of its known cellular targets, Bcl-2, in cell lysates was found to be dependent on ATP, consistent with the possible involvement of Hsp/Hsc70 in complex formation. Overexpression of BAG-1 also protected certain cell lines from heat shock-induced cell death. The identification of Hsp/Hsc70 as a partner protein for BAG-1 may explain the diverse interactions observed between BAG-1 and several other proteins, including Raf-1, steroid hormone receptors and certain tyrosine kinase growth factor receptors. The inhibitory effects of BAG-1 on Hsp/Hsc70 chaperone activity suggest that BAG-1 represents a novel type of chaperone regulatory proteins and thus suggest a link between cell signaling, cell death and the stress response.     

An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators

Heat Shock Protein 70 kDa (Hsp70) family molecular chaperones play critical roles in protein folding and trafficking in all eukaryotic cells. The mechanisms by which Hsp70 family chaperones are regulated, however, are only partly understood. BAG-1 binds the ATPase domains of Hsp70 and Hsc70, modulating their chaperone activity and functioning as a competitive antagonist of the co-chaperone Hip. We describe the identification of a family of BAG-1-related proteins from humans (BAG-2, BAG-3, BAG-4, BAG-5), the invertebrate Caenorhabditis elegans (BAG-1, BAG-2), and the fission yeast Schizosaccharomyces pombe (BAG-1A, BAG-1B). These proteins all contain a conserved approximately 45-amino acid region near their C termini (the BAG domain) that binds Hsc70/Hsp70, but they differ widely in their N-terminal domains. The human BAG-1, BAG-2, and BAG-3 proteins bind with high affinity (KD congruent with 1-10 nM) to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. The findings suggest opportunities for specification and diversification of Hsp70/Hsc70 chaperone functions through interactions with various BAG-family proteins.     

70钢氧化铁皮测定分析

模拟分析了70钢表面氧化层厚度、氧化层的基本构成以及氧化层与基体的结合强度，为准确定位高速线材的控冷工艺，优化酸洗，提高热轧盘条表面质量提供技术依据。     

Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein

A cDNA that codes for an Hsp70-interacting protein (HspBP1) was isolated from a human heart cDNA library using the yeast two-hybrid system. The derived amino acid sequence is unique and therefore represents a new regulator of Hsp70. Northern blots of RNA from human tissues indicate that HspBP1 mRNA has a size of approximately 1.7 kilobase pairs and is present in all tissues analyzed but is most abundant in heart and skeletal muscle. Western blot analysis revealed a protein of approximately 40 kilodaltons detected in cell extracts. The ATPase domain of Hsp70 demonstrated binding to HspBP1. Further experiments showed binding of HspBP1 to Hsp70 and Hsc70 in a total heart extract. HspBP1 (8 microM) inhibited approximately 90% of the Hsp40-activated Hsp70 ATPase activity. HspBP1 prevented ATP binding to Hsp70, and therefore this is the likely mechanism of inhibition. Hsp40-activated ATPase activity is essential for the renaturation activity of Hsp70; therefore, the effects of HspBP1 on renaturation of luciferase in a reticulocyte lysate and a defined system were examined. HspBP1 inhibited renaturation with half-maximal inhibition at 2 microM. These data indicate that we have identified a novel Hsp70-interacting protein that inhibits Hsp70 chaperone activity.     

Optimization of HPS 70W Applications

In February 1996 the Tennessee Department of Transportation, in cooperation with the Federal Highway Administration, the American Iron and Steel Institute, the U.S. Navy, and various steel plate manufacturers, agreed to design the first bridge in the United States to use HPS 485W (70W) steel. Since that time the department has constructed a second bridge using HPS 485W (70W) and has let to contract a third bridge that uses HPS 485W (70W) in both quenched and tempered and thermomechanical controlled processing HPS 485W (70W) steel. This paper will discuss lessons learned in the process and present optimization techniques employed.     

Single copy Babesia microti hsp70

The glucose-6-phosphate dehydrogenase-encoding gene (G6PD) belongs to a group with constitutive expression in all tissues. The regulation of these housekeeping genes is poorly understood, as compared to what is known about many genes whose expression is restricted to a particular tissue or stage of development, and which are often regulated by locus control regions (LCR) able to act over wide distances. In order to identify sequences in human G6PD which are necessary for its expression, we have generated transgenic mice carrying a 20-kb G6PD construct, including only 2.5 kb of upstream and 2.0 kb of downstream flanking sequence. All mice which carried the transgene (TG) expressed it, and the levels of expression detected in a range of tissues from three independent lines of mice were comparable to that of the endogenous murine G6PD. The variation in enzyme activity from tissue to tissue was remarkably similar for both the TG and the endogenous gene, and was shown to be due in both cases to variations in the steady-state mRNA levels.     

Interdomain B in ZAP-70 regulates but is not required for ZAP-70 signaling function in lymphocytes

The protein tyrosine kinase ZAP-70 plays an important role in T-cell activation and development. After T-cell receptor stimulation, ZAP-70 associates with the receptor and is phosphorylated on many tyrosines, including Y292, Y315, and Y319 within interdomain B. Previously, we demonstrated that Y292 negatively regulates ZAP-70 function and that Y315 positively regulates ZAP-70 function by interacting with Vav. Recent studies have suggested that Y319 also positively regulate ZAP-70 function. Paradoxically, removal of interdomain B (to create the construct designated Delta), containing the Y292, Y315, and Y319 sites, did not eliminate the ability of ZAP-70 to induce multiple gene reporters in Syk-deficient DT-40 B cells and ZAP-70/Syk-deficient Jurkat cells. Here we show that Delta still utilizes the same pathways as wild-type ZAP-70 to mediate NF-AT induction. This is manifested by the ability of Delta to restore induction of calcium fluxes and mitogen-activated protein kinase activation and by the ability of dominant negative Ras and FK506 to block the induction of NF-AT activity mediated by Delta. Biochemically we show that the stimulated tyrosine phosphorylation of Vav, Shc, and ZAP-70 itself is diminished, whereas that of Slp-76 is increased in cells reconstituted with Delta. Deletion of interdomain B did not affect the ability of ZAP-70 to bind to the receptor. The in vitro kinase activity of ZAP-70 lacking interdomain B was markedly reduced, but the kinase activity was still required for the protein's in vivo activity. Based on these data, we concluded that interdomain B regulates but is not required for ZAP-70 signaling function leading to cellular responses.