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       ÓÉÉúÎïѧÁìÓò¶¥¼âµÄ¿ÆÑ§¼ÒȺÌ壨Faculty 1000£©³ÉÔ±ÆÀÑ¡³ö2010ÄêÉúÎïѧÁìÓò×îÖØÒªµÄÎåÏ×÷¡£ÈëÑ¡µÄÂÛÎÄ£¬¶¼ÊÇÔ¶À빫ÖÚÊÓÒ°¡¢¾²ÇÄÇĽøÐеÄһЩÕë¶ÔÉúÃü»î¶¯·Ö×Ó»ù´¡µÄÑо¿¡£¶øÇÒ¶¼ÊÇЩ³¤ÆÚÁ¬ÐøµÄ¹¤×÷¡£

No. 5 ·¢ÏÖ»úеÁ¦´«µ¼µ°°× (Mechanotransduction proteins)

ÂÛÎÄ£º B. Coste, et al., "Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels," Science, 330:55-60, 2010.

    ÎÒÃÇÒªÈÏʶÊÀ½çÊ×ÏȵÃÒª½èÖúÓÚ¸÷Öָоõϵͳ£¬°üÀ¨ÊÓ¾õ¡¢Ìý¾õ¡¢´¥¾õºÍζ¾õµÈ»ñµÃÍâ½çµÄÐźš£Î¶¾õÊÇ»¯Ñ§´Ì¼¤£¬ÊÓ¾õ¹âѧÐźŴ̼¤£¬¸ÐÊÜÕâЩ´Ì¼¤ÐźŲ¢½«Æäת»¯³Éϸ°ûÄÚ¿É´«µ¼ÐźŵÄÊÜÌå·Ö×Ó¶¼µÃµ½Á˼ø¶¨ºÍ²ûÃ÷¡£µ«ÊÇ£¬»¹ÓÐÒ»Àà¸Ð¾õ£¬´¥¾õ¡¢Ìý¾õ£¨ÉùÒôÕð¶¯Í¨¹ý¹ÄĤ¡¢ÌýС¹ÇÒÔ¼°¶úÎÏ×îÖÕ´«µ¼µ½Ìý¾õëϸ°û°Ú¶¯£©ºÍһЩÎïÀí´Ì¼¤ÒýÆðµÄÍ´¾õ£¨Èç´ÌÍ´£©£¬¶¼ÊÇһЩ»úеÁ¦´Ì¼¤£¬¶ø¸ÐÊÜÆ÷ϸ°ûÊÇÈçºÎ½«Á¦Ñ§ÐźÅת»¯³Éϸ°û¿É´«µ¼µÄÐźŵ쬳¤ÆÚÒÔÀ´Ò»Ö±ÊǸöÃÕ¡£¸Ã¹¤×÷ÔÚСÊóϸ°ûϵ·¢ÏÖ¼ø¶¨ÁËÕâÖÖ»úеÁ¦´«µ¼µ°°×·Ö×Ó£¬Piezo1 and Piezo2£¬ÖÕÓÚ½Ò¿ªÁËÕâ¸öÃյס£

5. Mechanotransduction proteins found

        The paper: B. Coste, et al., "Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels," Science, 330:55-60, 2010.

        A new family of proteins, characterized in a mouse cell line, shines new light on the previously mysterious molecular basis of mechanosensation in mammals. Called Piezos, these proteins have been identified as a critical molecular component in mechanically activated ion channels, which make possible several sensations, such as hearing, touch and pain.


Á¬½Ó£ºhttp://www.ncbi.nlm.nih.gov/pubm ... ted+cation+channels

No. 4 Ñ×Ö¢·´Ó¦µÄ·Å´ó»úÖÆ (Inflammation amplification )

ÂÛÎÄ: E. Boilard, et al., "Platelets amplify inflammation in arthritis via collagen-dependent microparticle production," Science, 327:580-83, 2010.


    Ñ×Ö¢·´Ó¦ÊÇ»úÌå¶Ô¸¶ËðÉË¡¢¸ÐȾºÍÒìÎïÈëÇֵȵÄÒ»ÖÖ±£»¤ÐÔ·´Ó¦£¬ÌåÄÚµÄÑ×Ö¢·´Ó¦ÊÇÒ»¸ö¼¶Áª·Å´óµÄ·´Ó¦¹ý³Ì¡£´óÌå±íÏÖÊǾֲ¿ºì¡¢Öס¢ÈÈ¡¢Í´£¬Æäϸ°ûѧ»úÀíÊǾֲ¿Ñª¹ÜÀ©ÕÅ¡¢Ñª¹Üͨ͸ÐÔÔö¼Ó£¬Ñª½¬Ïò×é֝ɸ³ö£¬Ñ×֢ϸ°ûÏò×éÖ¯¾Ö²¿¾Û¼¯£¬²ÎÓëÇå³ý²¡Ô­¡¢´Ù½ø×éÖ¯ÐÞ¸´¡£²¡ÀíÐÔÑ×Ö¢·´Ó¦Ò²ºÍÐí¶à²¡Àí¹ý³ÌÃÜÇÐÏà¹Ø£¬Èç¹Ø½ÚÑס¢Àà·çʪ¡¢ÒҸεĸÉϸ°ûËðÉ˵ȣ¬¶¼ÊÇÑ×Ö¢·´Ó¦¹ý¶È»òʧȥ¿ØÖÆÒýÆðµÄ¶ÔÕý³£×éÖ¯µÄÆÆ»µ¡£ÑªÐ¡°åÊÇѪҺÖеÄÒ»ÖÖ΢С¿ÅÁ£×´µÄ·Çϸ°ûÐԽṹ£¬ÔÚÄýѪ×÷ÓÃÖз¢»ÓÖØÒª×÷Ó㬵«ÔÚÑ×Ö¢·´Ó¦ÖеÄ×÷Óû¹Ã»Óеĵ½ÈÏʶ¡£¸ÃÂÛÎļø¶¨ÁËѪС°åĤÉϵÄ΢С¿ÅÁ£½á¹¹ÔÚÑ×Ö¢·´Ó¦µÄ·Å´óÖеÄ×÷Óã¬ÎªÑ×ÐÔ¼²²¡µÄÖÎÁÆÌṩÁËеÄÏßË÷¡£

4. Inflammation amplification

The paper: E. Boilard, et al., "Platelets amplify inflammation in arthritis via collagen-dependent microparticle production," Science, 327:580-83, 2010.

Researchers identify platelet "microparticles" -- tiny vesicles that bud from the membranes of activated platelets -- in the fluid of inflamed joints, which rarely contain blood. Importantly, depleting the microparticles using an antibody seemed to cure arthritis in mice.

The discovery, published in a January issue of Science, demonstrates the previously unappreciated role of platelets in inflammatory arthritis.

Read the full story here.


Á¬½Ó£ºhttp://www.ncbi.nlm.nih.gov/pubmed


No.3.  ½âÎöºôÎüÁ´Ã¸¸´ºÏÌåIµÄ½á¹¹£¨Complex I enzyme £©

ÂÛÎÄ: R.G. Efremov, et al., "The architecture of respiratory complex I," Nature, 465:441-5, 2010.


ÉúÎïÌåËùÐèÒªµÄÄÜÁ¿´ÓÄĶùÀ´£¿´ÓÎïÖÊ´úлÖлñµÃ¡£¶ÔÓÚ¾ø´ó¶àÊýÐèÒªÑõÆøµÄÉúÎÑõ»¯ºôÎüÊǽ«´úлÖмä²úÎï¾­¹ýÑõ»¯ºôÎüÁ´°Ñ´úлÎïÖд¢´æµÄ»¯Ñ§ÄÜ×ªÒÆµ½ATPÉÏ£¨ÉúÎïµÄÄÜÁ¿Í¨Óûõ±Ò£©¡£Ñõ»¯ºôÎüÁ´ÊÇÓÉһϵÁÐø×é³ÉµÄ½á¹¹¸´Ôӵĸ´ºÏÌ壬¾ÍÏñÉú²úÁ÷Ë®ÏßÒ»Ñù£¬µ«ÊÇÔ¶±È¹¤³§Á÷Ë®Ïß¾«ÇÉ¡¢½ô´ÕºÍ¸ßЧ¡£Ñõ»¯ºôÎüÁ´ÓÉI¡¢II¡¢IIIºÍIVÕâËĸö¸´ºÏÌå×é³É£¬ÆäÖи´ºÏÌåIµÄ½á¹¹Ò»Ö±Î´Äܵõ½½âÎö¡££¨¼ÇµÃ2005Ä꣬ÈÄ×ÓºÍÁìµ¼µÄʵÑéÊÒºÍÆäËü¼¸¼ÒʵÑéÊÒºÏ×÷½âÎöÁËÑõ»¯ºôÎüÁ´Ã¸¸´ºÏÌåIIµÄ½á¹¹£¬½á¹û·¢±íÔÚCellÉÏ£¬³ÉΪ¹úÄÚÖØÒª¿Æ¼¼ÐÂÎÅ£©¡£ÕâÆªÂÛÎijɹ¦½âÎöÁËø¸´ºÏÌåIµÄ½á¹¹£¬½â¾öÁË´ó¼ÒÆÚ´ýÒѾõÄÎÊÌâ¡£

3. Complex I enzyme revealed

The paper: R.G. Efremov, et al., "The architecture of respiratory complex I," Nature, 465:441-5, 2010.

The long-awaited structure of a bacterial complex I enzyme -- first in line in the energy-producing respiratory chain -- reveals important mechanics of this ubiquitous protein. Specifically, the structure shows how the enzyme hustles electrons and protons across membranes.

The structure, published by Nature in May, is one of the largest protein membrane complexes ever solved.


Á¬½Ó£ºhttp://www.ncbi.nlm.nih.gov/pubmed/20505720

No. 2. ÏËëÊÇÈçºÎ¡°½»Ì¸¡±µÄ£¿£¨ How cilia talk£©

ÂÛÎÄ: Q. Hu, et al., "A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution," Science, 329:436-39, 2010.


Ç¡ÈçÀ¥³æµÄ´¥½ÇÒ»Ñù£¬³õ¼¶ÏËëÊÇÕæºËµ¥Ï¸°ûµÄ¸ÐÊÜÆ÷£¬Ëü½ÓÊÜϸ°ûÍâÐźŲ¢Í¨¹ýϸ°ûĤµ°°×Ïòϸ°ûÄÚ´«µÝ£¬µ«ÊÇ£¬ÄÇЩÐźŵ°°×¾¿¾¹ÊÇÔõô¡°¹´´î¡±Éϳõ¼¶ÏËë²¢¹ÒÔÚÉÏÃæµÄ£¿ ³¤ÆÚÒÔÀ´Ò»Ö±ÊǸöÃÔ¡£ÕâÆªÂÛÎĵÄÑо¿·¢ÏÖ֤ʵ£ºÔÚ³õ¼¶ÏËëµÄ»ùµ×²¿ÓÐÒ»¸öÓɶà¸öseptin·Ö×Ó×é³ÉµÄ¡°À¸¸Ë¡±£¬ÕâÒ»½á¹¹¿ÉÒԹ̶¨ÏË룬²¢¿ØÖÆÄ¤µ°°×µÄ¶¨Î»ºÍ·Ö²¼¡£

2. How cilia talk

The paper: Q. Hu, et al., "A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution," Science, 329:436-39, 2010.

Primary (nonmotile) cilia -- sensory organelles in eukaryotic cells that act as antennae -- rely on membrane proteins to send and receive extracellular signals. New findings, published in the July issue of Science, show how cilia retain those membrane proteins -- a barrier at the base of cilia made up of proteins called septins.

Septins, originally identified as cell division mutants in yeast, localize at the base of the cilium where they maintain a barrier to control the localization of membrane proteins. The discovery solves the long-standing mystery of how signaling proteins are retained in the primary cilium.

One of the paper's corresponding authors, Elias Spiliotis, is this month's Scientist to Watch. You can read more about septins, and how they may also help protect yeast from the effects of aging, in our October cover story by Yves Barral.


Á¬½Ó£ºhttp://www.ncbi.nlm.nih.gov/pubmed

No. 1. Ñ×Ö¢·´Ó¦Îª¼ÄÉúÎïιʳ £¨Immune response feeds parasite£©

ÂÛÎÄ: S.E. Winter, et al., "Gut inflammation provides a respiratory electron acceptor for Salmonella," Nature, 467:426-9, 2010.


¶¯ÎïµÄÏû»¯µÀ·Ö²¼×Å´óÁ¿µÄ΢ÉúÎï¾úÀ࣬ÎÒÃdzÆÖ®Îª³£×¤Õý³£¾úȺ£¬²»½ö¶ÔÏû»¯¹¦ÄÜÊ®·Ö±ØÒª£¬»¹¿ÉÒÔ¶Ô»úÌåÐγɱ£»¤£¬µÖÖÆ/ÒÖÖÆÍâÀ´Ö²¡£¨Óк¦£©Î¢ÉúÎïµÄ¶¨¾ÓºÍ·±Ö³¡£É³ÃÅÊϾúÊÇÒ»ÀàÖ²¡¾ú£¬¸Ã¾úÊÇÔõÑùÔÚÓ볫µ¼ÓÅÊÆ¾úȺµÄ¾ºÕùÖÐʤ³ö²¢Ö²¡µÄÄØ£¿ ¸ÃÂÛÎÄ·¢ÏÖ£¬ ɳÞúͨ¹ý¶ÀÌØµÄÄÜÁ¿»ñȡ;¾¶ÔÚͬ³¦µÀµÄ¾úȺ¾ºÕùÖÐʤ³ö¡£³¦µÀµÄÑ×Ö¢·´Ó¦±¾À´ÊÇÓÃÀ´¶Ô¸¶³¦µÀ²¡Ô­µÄ£¬µ«ÊÇÆä¸±²úÎïÁ¬ËÄÁòËáÑÎÈ´¿ÉÒÔ±»É³ÃÅÊϾúÓÃ×÷ΪÄÜÔ´ÎïÖÊ£¬²¢Í¨¹ýÑõ»¯ºôÎüÁ´»ñµÃÄÜÁ¿£¬Ôöǿϸ¾úÉú³¤£¬Õâ½Ð¡°½èÁ¦´òÁ¦¡±£¬ÕæÊÇ¡°µÀ¸ßÒ»³ß£¬Ä§¸ßÒ»ÕÉ¡±£¡

1. Immune response feeds parasite

The paper: S.E. Winter, et al., "Gut inflammation provides a respiratory electron acceptor for Salmonella," Nature, 467:426-9, 2010.

Salmonella is able to out-compete resident gut microbes by deriving energy from the immune response that is supposed to combat the pathogen, according to a study published in September in Nature. Inflammation in a mouse gut generates a sulfur-based molecule called tetrathionate, which Salmonella uses during respiration for enhanced growth.

Á¬½Ó£ºhttp://www.ncbi.nlm.nih.gov/pubmed


ת×Ôhttp://www.bioon.com

[ Last edited by rainwander on 2010-12-17 at 19:59 ]
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