| ²é¿´: 1888 | »Ø¸´: 10 | |||
[½»Á÷]
ÈÈÐݿ˵°°×90¦Á ֪ʶÆÕ¼°
|
|
ÖÐÑëÐÂÎű¨µÀÁËÇ廪¿ÎÌâ×éÊ×´ÎÔÚ¹ú¼ÊÉÏÖ¤Ã÷£¬ÈËÈÈÐݿ˵°°×Hsp90¦Á£¨ÒÔϼò³ÆÈË90¦Á£©ÎªÒ»¸öȫеÄÖ×Áö±êÖ¾Î²¢Ñз¢³ö¶¨Á¿¼ì²âÊÔ¼ÁºÐ¡£Ä¿Ç°£¬¸ÃÊÔ¼ÁºÐÒÑ»ñµÃ¹ú¼ÒµÚÈýÀࣨ×î¸ßÀà±ð£©Ò½ÁÆÆ÷е֤Ê飬²¢Í¨¹ýÅ·ÃËÈÏÖ¤¡£ ½¨Òé´ó¼ÒºÏÁ¦ÆÕ¼°Ò»ÏÂÕâ·½ÃæµÄ֪ʶ£¡£¡ |
» ±¾Ìû¸½¼þ×ÊÔ´Áбí
-
»¶Ó¼à¶½ºÍ·´À¡£ºÐ¡Ä¾³æ½öÌṩ½»Á÷ƽ̨£¬²»¶Ô¸ÃÄÚÈݸºÔð¡£
±¾ÄÚÈÝÓÉÓû§×ÔÖ÷·¢²¼£¬Èç¹ûÆäÄÚÈÝÉæ¼°µ½ÖªÊ¶²úȨÎÊÌ⣬ÆäÔðÈÎÔÚÓÚÓû§±¾ÈË£¬Èç¶Ô°æÈ¨ÓÐÒìÒ飬ÇëÁªÏµÓÊÏ䣺xiaomuchong@tal.com - ¸½¼þ 1 : PNAS-2009-Wang-21288-93__HSP_90a.pdf
- ¸½¼þ 2 : J_Immunol-2009-Houlihan-7451-8__HSP_90a.pdf
2013-11-21 15:13:45, 1.81 M
2013-11-21 15:14:25, 2.72 M
» ²ÂÄãϲ»¶
ÆÖ½È˲żƻ®
ÒѾÓÐ14È˻ظ´
ÇóÖú£¡ëè¹Ç¡¢Íâõ×½âÆÊÊý¾Ý²âÁ¿--½Ç¶È£¬¾¶Ïß
ÒѾÓÐ0È˻ظ´
ÃÚÄòϵͳÂÛÎÄÈóÉ«/·ÒëÔõôÊÕ·Ñ?
ÒѾÓÐ188È˻ظ´
½»²æÑ§¿ÆÔõô½»Á÷£¿
ÒѾÓÐ0È˻ظ´
ͶÁ˸öÐÐÒµÄÚ¶¥¿¯
ÒѾÓÐ7È˻ظ´
ÖØ×éµ°°×ÄÜÖ±½ÓËÇι¶¯Îïô
ÒѾÓÐ3È˻ظ´
ÃÀ¹úÓÌËû´óѧ£¨University of Utah£©Ò½Ñ§Ôº ¹ùºê³¬ÊµÑéÊÒÕÐÆ¸1-2Ãû²©Ê¿ºó
ÒѾÓÐ1È˻ظ´
ÃÀ¹úÓÌËû´óѧ£¨University of Utah£©Ò½Ñ§Ôº ¹ùºê³¬(Hongchao Guo)ʵÑéÊÒÕÐÆ¸²©Ê¿ºó
ÒѾÓÐ0È˻ظ´
» ±¾Ö÷ÌâÏà¹ØÉ̼ÒÍÆ¼ö: (ÎÒÒ²ÒªÔÚÕâÀïÍÆ¹ã)
» ÇÀ½ð±ÒÀ²£¡»ØÌû¾Í¿ÉÒԵõ½:
×ø±êÎÞÎý£¬³ÏÕ÷Å®ÓÑ
+3/892
´óÁ¬Àí¹¤´óѧ´óÁ¬Êи´ÔÓ¹¤Òµ³¡¾°¾ßÉíÖÇÄÜÖØµãʵÑéÊÒ¿ÆÑÐÖúÀíÕÐÆ¸ÆôÊÂ
+2/188
´óÁ¬Àí¹¤´óѧ¿ØÖÆ¿ÆÑ§Ó빤³ÌѧԺŷÓÂÊ¢½ÌÊÚ¿ÎÌâ×é2026Äê¿ÆÑÐÖúÀíÕÐÆ¸ÆôÊÂ
+2/182
ÔÚÖ°²©Ê¿ÊDz»ÊÇûϷÁË£¬Ïë¶Á£¬Ã»ÕÐ
+1/175
ʯºÓ×Ó´óѧÄÜÔ´Óë²ÄÁÏѧԺÀ¸±½ÌÊÚ¿ÎÌâ×éÕÐÊÕ˶¡¢²©Ê¿
+1/78
±±¾©Àí¹¤´óѧ»úеÓë³µÁ¾Ñ§ÔºÌØÖÖ³µÁ¾Ñо¿Ëù²©Ê¿ºóÕÐÆ¸£¬µçÇý¶¯¿ØÖÆ¡¢ÊÔÑé²âÊÔ·½Ïò
+1/67
ÊÂÒµ±àÖÆ£¡Ìì½òʦ·¶´óѧ³ÏƸ¸±¸ß/½²Ê¦Ö°Î»
+2/48
ͬ¼Ã´óѧ»·¾³Ñ§ÔºÐ¤Ù»¿ÎÌâ×éÕÐÊÕ²©Ê¿Ñо¿Éú£¨×ʸñÉóºËÖÆ£©
+1/43
ÇóÖúÐÏÆäÒãµÚËİæ»ù´¡Óлú»¯Ñ§PDF°æ
+1/34
°Ä´óÀûÑǻʼÒÄ«¶û±¾Àí¹¤´óѧ£¨RMIT University£©ÕÐÊÕ²©Ê¿Éú¼° CSC ÁªºÏÅàÑø²©Ê¿Éú
+1/17
ÓлúºÏ³ÉÒÔºó»á²»»á±»AI¸Ä±ä£¿×ö¿ÆÑеijæÓÑÔõô¿´
+2/16
ÍÆ¼öÒ»¸ö±È½ÏʵÓõÄÉúÎïÐÅÏ¢Ñ§Ñ§Ï°ÍøÕ¾¡ª¡ªThe Omics Hub
+1/11
¡¾ÍÆÃâÕÐÉú¡¿ÕÐÊÕ²ÄÁÏ¡¢»¯¹¤¡¢»·¾³¡¢Ò±½ðÀàÍÆÃâÉú
+1/10
¾ÉºÅδ°ó¶¨ÊÖ»ú»òÍü¼ÇÊÖ»úºÅÂ룬Ôõô°ó¶¨ÐÂÊÖ»úºÅ
+1/10
¹óÖÝ´óѧ2027Óлú»¯Ñ§ÉêÇ뿼ºËÖÆ²©Ê¿ÕÐÉú
+1/8
ÃÀ¹úWashington University in St. Louis »¯¹¤×¨ÒµÕÐÊÕ²©Ê¿ºóºÍ²©Ê¿Ñо¿Éú
+1/4
ÈáÐÔÆ÷¼þ¶àÎïÀí³¡·ÂÕæ£ºCOMSOLÈÈ-Á¦-µçñîºÏÓë´úÀíÄ£ÐÍ
+1/2
ËéËéÄî
+1/2
ÃÀ¹úOhio UniversityҽѧԺ¹ÇÐԹؽÚÑ×ʵÑéÊÒÕÐÊÕÉúÎïҽѧȫ½±²©Ê¿Éú-2027ÄêÇïÈëѧ
+1/2
¹ã¶«¹¤Òµ´óѧÖÇÄܹⳡ¸ÐÖªÓëµ÷¿Ø¿ÎÌâ×飨IOSC Lab£©³ÏƸÇàÄê½Ìʦ¼°²©Ê¿ºó ½Ìʦ¸ÚλÓб
+1/2
2Â¥2013-11-19 15:10:29
3Â¥2013-11-19 17:50:33
4Â¥2013-11-19 18:38:09
5Â¥2013-11-19 19:43:05
mlanqiang
ľ³æÖ®Íõ (ÎÄѧ̩¶·)
- Ó¦Öú: 3409 (¸±½ÌÊÚ)
- ½ð±Ò: 55278.8
- Ìû×Ó: 73916
- ÔÚÏß: 730.8Сʱ
- ³æºÅ: 302202
6Â¥2013-11-19 20:03:30
7Â¥2013-11-19 20:25:27
¡ï
Сľ³æ: ½ð±Ò+0.5, ¸ø¸öºì°ü£¬Ð»Ð»»ØÌû
Сľ³æ: ½ð±Ò+0.5, ¸ø¸öºì°ü£¬Ð»Ð»»ØÌû
| The molecular acclimation of intertidal green macroalga Ulva fasciata Delile to high salinity stress were examined by the construction of a forward cDNA library via the suppressive subtractive hybridization between 30¡ë and 90¡ë (24 h) and by the time course dynamics of several abundantly expressed genes. Among the genes with known sequences, the expressed sequence tags are abundant in the function of protein synthesis (ribosomal protein) and destination. The cDNAs of ATP-dependent Clp protease (UfClpC), 20S proteasome ¦Â-subunit type 1 domain (UfPbf1), ubiquitin-conjugating enzyme E2 I (UfUbc9), and heat shock protein 90A (UfHsp90A) were cloned. UfClpC transcript increased 3 h after 90¡ë treatment, followed by a decrease, while UfPbf1 and UfUbc9 transcripts increased after 12 h and decreased at 48 h. The transcripts of UfHsp90A increased 1 h after 90¡ë treatment, followed by a drop and to the control level at 48 h. Protease activity increased 3 h after 90¡ë treatment and decreased to the control level at 48 h. H₂O₂ contents increased 1 h after 90¡ë treatment and then remained unchanged, but protein carbonyl group contents increased after 48 h. The treatments of reactive oxygen species scavengers partially alleviated 90¡ë damage (partial growth rescue) and suppressed the increases in H₂O₂ content, protein carbonyl group content, protease activity, and UfClpC, UfPbf1, UfUbc9, and UfHsp90A transcripts by 90¡ë. The induction of specific chaperones and proteases at the molecular level for protein quality control can be considered as one of the molecular mechanisms of hypersalinity acclimation in U. fasciata. |
8Â¥2013-11-21 11:02:02
|
¡¾°Ù¶È¡¿ ÈÈÐݿ˵°°× Heat Shock Proteins (HSPs),ÊÇÔÚ´Óϸ¾úµ½²¸È鶯ÎïÖй㷺´æÔÚÒ»ÀàÈÈÓ¦¼±µ°°×ÖÊ¡£µ±ÓлúÌ屩¶ÓÚ¸ßεÄʱºò£¬¾Í»áÓÉÈȼ¤·¢ºÏ³É´ËÖÖµ°°×£¬À´±£»¤ÓлúÌå×ÔÉí¡£Ðí¶àÈÈÐݿ˵°°×¾ßÓзÖ×Ó°é»îÐÔ¡£°´ÕÕµ°°×µÄ´óС£¬ÈÈÐݿ˵°°×¹²·ÖΪÎåÀ࣬·Ö±ðΪHSP100£¬HSP90£¬HSP70£¬HSP60 ÒÔ¼°Ð¡·Ö×ÓÈÈÐݿ˵°°× small Heat Shock Proteins (sHSPs)( Kyeong et al., 1998)¡£ |
9Â¥2013-11-21 14:13:31
10Â¥2013-11-21 15:11:44
11Â¥2014-06-05 08:42:58










»Ø¸´´ËÂ¥