533:(phosphatidylinositol-4,5-bisphosphate) in the cell membrane and facilitate actin assembly near the membrane. More recently, annexin scaffolding functions have been linked to medical applications. These medical implications have been uncovered with in vivo studies where the path of a fertilized egg is tracked to the uterus. After fertilization, the egg must enter a canal for which the opening is up to five times smaller than the diameter of the egg. Once the fertilized egg has passed through the opening, annexins are believed to promote membrane folding in an accordion-like fashion to return the stretched membrane back to its original form. Though this was discovered in the
658:. Like other annexin types, annexin A-V can also be expressed on the cell surface and can function to form 2-dimensional crystals to protect the lipids of the cell membrane from involvement in coagulation mechanisms. Medically speaking, phospholipids can often be recruited in autoimmune responses, most commonly observed in cases of fetal loss during pregnancy. In such cases, antibodies against annexin A-V destroy its 2-dimensional crystal structure and uncover the phospholipids in the membrane, making them available for contribution to various coagulation mechanisms.
29:
362:, while the convex side of the annexin contains calcium binding sites. Each annexin core contains one type II, also known as an annexin type, calcium binding site; these binding sites are the typical location of ionic membrane interactions. However, other methods of membrane connections are possible. For example, A-V exposes a
382:. Short N-termini are thought to stabilize the annexin complex in order to increase calcium binding and can be the sites for post-translational modifications. Long N-termini can contain up to 40 residues and have a more complex role in annexin signaling. For example, in A-I the N-terminus folds into an
285:
The basic structure of an annexin is composed of two major domains. The first is located at the COOH terminal and is called the “core” region. The second is located at the NH2 terminal and is called the “head” region. The core region consists of an alpha helical disk. The convex side of this disk has
377:
The diverse structure of the N-terminus confers specificity to annexin intracellular signaling. In all annexins the N-terminus is thought to sit inside the concave side of the annexin core and folds separately from the rest of the protein. The structure of this region can be divided into two broad
357:
The 310 amino acid annexin core has four annexin repeats, each composed of 5 alpha-helices. The exception is annexin A-VI that has two annexin core domains connected by a flexible linker. A-VI was produced via duplication and fusion of the genes for A-V and A-X and therefore will not be discussed
513:
Annexins can function as scaffolding proteins to anchor other proteins to the cell membrane. Annexins assemble as trimers, where this trimer formation is facilitated by calcium influx and efficient membrane binding. This trimer assembly is often stabilized by other membrane-bound annexin cores in
265:
family of annexins has continued to grow since their association with intracellular membranes was first reported in 1977. The recognition that these proteins were members of a broad family first came from protein sequence comparisons and their cross-reactivity with antibodies. One of these workers
349:
Several subfamilies of annexins have been identified based on structural and functional differences. However, all annexins share a common organizational theme that involves two distinct regions, an annexin core and an amino (N)-terminus. The annexin core is highly conserved across the annexin
290:. The N terminal region is located on the concave side of the core region and is important for providing a binding site for cytoplasmic proteins. In some annexins it can become phosphorylated and can cause affinity changes for calcium in the core region or alter cytoplasmic protein interaction.
626:
Annexin A-I has also been implicated in apoptotic mechanisms in the cell. When expressed on the surface of neutrophils, annexin A-I promotes pro-apoptotic mechanisms. Alternatively, when expressed on the cell surface, annexin A-I promotes the removal of cells that have undergone apoptosis.
409:
Annexins are characterized by their calcium dependent ability to bind to negatively charged phospholipids (i.e. membrane walls). They are located in some but not all of the membranous surfaces within a cell, which would be evidence of a heterogeneous distribution of Ca within the cell.
386:
alpha-helix and inserts into the protein core, displacing helix D of annexin repeat III. However, when calcium binds, the N-terminus is pushed from the annexin core by conformational changes within the protein. Therefore, the N-terminus can interact with other proteins, notably the
395:
sites which allow for further signaling. A-II can also use its long N-terminal to form a heterotrimer between a S100 protein and two peripheral annexins. The structural diversity of annexins is the grounds for the functional range of these complex, intracellular messengers.
569:
assembly. In fact, annexin A-II is itself an actin-binding protein and therefore it can form a region of interaction with actin by means of its filamentous actin properties. In turn, this allows for further cell-cell interactions between monolayers of cells like
586:. It is in this stage that daughter cells separate from one another because annexin A-XI inserts a new membrane that is believed to be required for abscission. Without annexin A-XI, it is believed that the daughter cells with not fully separate and may undergo
1279:
Oling F, Santos JS, Govorukhina N, Mazères-Dubut C, Bergsma-Schutter W, Oostergetel G, Keegstra W, Lambert O, Lewit-Bentley A, Brisson A (December 2000). "Structure of membrane-bound annexin A5 trimers: a hybrid cryo-EM – X-ray crystallography study".
514:
the vicinity. Eventually, enough annexin trimers will assemble and bind the cell membrane. This will induce the formation of membrane-bound annexin networks. These networks can induce the indentation and vesicle budding during an exocytosis event.
422:
activity has been shown to increase the concentrations of
Annexins II,V within the nucleus. Annexin XI is predominantly located within the nucleus, and absent from the nucleoli. During prophase, annexin XI will translocate to the nuclear envelope.
293:
Annexins are important in various cellular and physiological processes such as providing a membrane scaffold, which is relevant to changes in the cell's shape. Also, annexins have been shown to be involved in trafficking and organization of
623:) extravasation and down regulates the magnitude of the inflammatory response. Without annexin A-I in mediating this response, neutrophil extravasation is highly active and worsens the inflammatory response in damaged or infected tissues.
496:
targeting sequences have been found in the N terminus of annexins I and II, which would be useful in sorting of endocytotic vesicles. Annexins are present in several different endocytotic processes. Annexin VI is thought to be involved in
545:
Several annexins have been shown to have active roles in the organization of the membrane. Annexin A-II has been extensively studied in this aspect of annexin function and is noted to be heavily involved in the organization of
521:
unit of the membrane. Annexin A-V is effective in stabilizing changes in cell shape during endocytosis and exocytosis, as well as other cell membrane processes. Alternatively, annexins A-I and A-II bind phosphatidylserine and
358:
in length. The four annexin repeats produce a curved protein and allow functional differences based on the structure of the curve. The concave side of the annexin core interacts with the N-terminus and cytosolic
273:
As of 2002 160 annexin proteins have been identified in 65 different species. The criteria that a protein has to meet to be classified as an annexin are: it has to be capable of binding negatively charged
2872:
619:. In turn, the activation of these receptors functions to send the leukocytes to the site of infection and target the source of inflammation directly. As a result, this inhibits leukocyte (specifically
2186:
Oh P, Li Y, Yu J, Durr E, Krasinska KM, Carver LA, Testa JE, Schnitzer JE (June 2004). "Subtractive proteomic mapping of the endothelial surface in lung and solid tumours for tissue-specific therapy".
517:
While different types of annexins can function as membrane scaffolds, annexin A-V is the most abundant membrane-bound annexin scaffold. Annexin A-V can form 2-dimensional networks when bound to the
452:
pathway, specifically in the later stages, near or at the plasma membrane. Evidence of annexins or annexin-like proteins are involved in exocytosis has been found in lower organisms, such as the
565:, where this binding is made possible by the influx of calcium ions. The binding of Annexin A-II to lipids in the bilayer orchestrates the organization of lipid rafts in the bilayer at sites of
435:
formation. The subject area has not been thoroughly studied, however it has been speculated that annexins may be involved in closing the neck of the matrix vesicle as it is endocytosed.
1711:
Pigault C, Follenius-Wund A, Schmutz M, Freyssinet JM, Brisson A (February 1994). "Formation of two-dimensional arrays of annexin V on phosphatidylserine-containing liposomes".
2237:
Rand JH (September 2000). "Antiphospholipid antibody-mediated disruption of the annexin-V antithrombotic shield: a thrombogenic mechanism for the antiphospholipid syndrome".
378:
categories, short and long N-termini. A short N-terminus, as seen in A-III, can consist of 16 or less amino acids and travels along the concave protein core interacting via
578:. In addition to annexin A-II, annexin A-XI has also been shown to organize cell membrane properties. Annexin A-XI is believed to be highly involved in the last stage of
337:
and identified a calcium dependent protein that was responsible for aggregation of granules amongst each other and the plasma membrane. This protein was given the name
1097:
Geisow MJ, Fritsche U, Hexham JM, Dash B, Johnson T (April 1986). "A consensus sequence repeat in
Torpedo and mammalian calcium-dependent membrane binding proteins".
176:
1015:
2412:
282:
dependent manner and must contain a 70 amino acid repeat sequence called an annexin repeat. Several proteins consist of annexin with other domains like gelsolin.
132:
120:
2857:
670:, annexin A-II is the most prominent in mediating these responses. The expression of annexin A-II on the cell surface is believed to serve as a receptor for
2454:
1439:"Identification and purification of an adrenal medullary protein (synexin) that causes calcium-dependent aggregation of isolated chromaffin granules"
2325:
Bauer B, Engelbrecht S, Bakker-Grunwald T, Scholze H (April 1999). "Functional identification of alpha 1-giardin as an annexin of
Giardia lamblia".
2053:
Hannon R, Croxtall JD, Getting SJ, Roviezzo F, Yona S, Paul-Clark MJ, Gavins FN, Perretti M, Morris JF, Buckingham JC, Flower RJ (February 2003).
1481:
Concha NO, Head JF, Kaetzel MA, Dedman JR, Seaton BA (September 1993). "Rat annexin V crystal structure: Ca(2+)-induced conformational changes".
2952:
3572:
458:. Through antibody recognition, there is evidence of the annexin like proteins being involved in the positioning and attachment of secretory
88:
2672:
476:. In Vitro studies however have shown that annexin VII does not promote the fusion of membranes, only the close attachment to one another.
1746:
Janshoff A, Ross M, Gerke V, Steinem C (August 2001). "Visualization of annexin I binding to calcium-induced phosphatidylserine domains".
1631:"Differential fractionation of matrix vesicle proteins. Further characterization of the acidic phospholipid-dependent Ca–binding proteins"
484:
Annexins have been found to be involved in the transport and also sorting of endocytotic events. Annexin one is a substrate of the EGF (
2018:
Prossnitz ER, Ye RD (1997). "The N-formyl peptide receptor: a model for the study of chemoattractant receptor structure and function".
1140:
Geisow MJ, Walker JH, Boustead C, Taylor W (April 1987). "Annexins – a new family of Ca -regulated phospholipid-binding protein".
1233:
Ghoshdastider, U; Popp, D; Burtnick, L. D.; Robinson, R. C. (2013). "The expanding superfamily of gelsolin homology domain proteins".
1759:
682:. The destruction of fibrin is a natural preventative measure because it prevents the formation of blood clots by fibrin networks.
1840:"Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes"
2890:
2880:
2447:
196:
2640:
2611:
1019:
1670:
Kenis H, van
Genderen H, Bennaghmouch A, Rinia HA, Frederik P, Narula J, Hofstra L, Reutelingsperger CP (December 2004).
469:
Annexin VII was the first annexin to be discovered while searching for proteins that promote the contact and fusion of
3222:
3031:
2272:
Ling Q, Jacovina AT, Deora A, Febbraio M, Simantov R, Silverstein RL, Hempstead B, Mark WH, Hajjar KA (January 2004).
3468:
2440:
431:
Annexins are abundant in bone matrix vesicles, and are speculated to play a role in Ca entry into vesicles during
3567:
3562:
2930:
2737:
2707:
2601:
1002:
838:
184:
310:
formation. Annexins have also been found outside the cell in the extracellular space and have been linked to
3016:
686:
485:
2432:
2665:
2660:
2655:
2650:
2645:
894:
473:
852:
526:
units in the cell membrane, and are often found forming monolayered clusters that lack a definite shape.
2852:
866:
824:
810:
286:
type 2 calcium-binding sites. They are important for allowing interaction with the phospholipids at the
1395:"Extracellular annexin A5: functions of phosphatidylserine-binding and two-dimensional crystallization"
880:
726:
180:
768:
740:
3397:
2195:
1490:
796:
101:
3363:
3180:
2835:
1350:
Gerke V, Creutz CE, Moss SE (June 2005). "Annexins: linking Ca2+ signalling to membrane dynamics".
782:
523:
1971:"Annexin 11 is required for midbody formation and completion of the terminal phase of cytokinesis"
3443:
2885:
2815:
2805:
2677:
2633:
2488:
2471:
2219:
2084:
1951:
1771:
1375:
1258:
1165:
1122:
1079:
518:
2790:
908:
537:
annexin NEX-1, it is believed that a similar mechanism takes place in humans and other mammals.
1630:
3458:
2862:
2844:
2467:
2387:
2342:
2303:
2254:
2211:
2168:
2125:
2076:
2035:
2000:
1943:
1902:
1861:
1820:
1763:
1728:
1693:
1652:
1611:
1556:
1506:
1460:
1438:
1416:
1367:
1297:
1250:
1215:
1157:
1114:
1071:
604:
575:
502:
359:
295:
171:
972:
338:
3453:
3271:
2621:
2423:
2377:
2367:
2334:
2293:
2285:
2246:
2203:
2158:
2115:
2066:
2027:
1990:
1982:
1933:
1892:
1851:
1810:
1802:
1755:
1720:
1683:
1672:"Cell surface-expressed phosphatidylserine and annexin A5 open a novel portal of cell entry"
1642:
1601:
1591:
1546:
1498:
1450:
1406:
1359:
1289:
1242:
1207:
1149:
1106:
1061:
1053:
932:
470:
238:
3325:
2566:
1791:"Identification, localization, and functional implications of an abundant nematode annexin"
968:
685:
Annexin A-II has medical implications because it can be utilized in treatments for various
163:
3536:
2699:
2593:
2531:
1041:
489:
419:
392:
287:
241:. Increased expression of the gene coding for annexin-1 is one of the mechanisms by which
492:
which becomes phosphorylated on its N terminus when the receptor is internalized. Unique
2416:
2199:
2102:
Arur S, Uche UE, Rezaul K, Fong M, Scranton V, Cowan AE, Mohler W, Han DK (April 2003).
1494:
1066:
3508:
2606:
2463:
2338:
1995:
1970:
1815:
1790:
1583:
1579:"Calcium- and Cell Cycle-dependent Association of Annexin 11 with the Nuclear Envelope"
432:
379:
334:
242:
219:
2382:
2355:
2298:
2273:
2163:
2144:
2120:
2103:
2031:
1647:
1551:
1534:
1455:
125:
3556:
3526:
3085:
3075:
3001:
2626:
2616:
2479:
1938:
1921:
1262:
639:
388:
371:
275:
93:
2088:
1955:
1775:
1379:
1169:
1083:
998:
57:
3438:
3188:
3147:
3080:
2420:- Calculated spatial positions of annexins in membranes (the initially bound state)
2223:
1126:
667:
612:
551:
319:
311:
250:
159:
137:
113:
1411:
1394:
916:
902:
888:
874:
860:
846:
832:
818:
804:
790:
776:
762:
748:
734:
720:
706:
69:
3493:
3473:
3448:
3070:
3053:
3048:
2820:
2810:
2511:
2501:
1393:
van
Genderen HO, Kenis H, Hofstra L, Narula J, Reutelingsperger CP (June 2008).
671:
655:
620:
583:
562:
383:
367:
315:
307:
303:
2055:"Aberrant inflammation and resistance to glucocorticoids in annexin 1-/- mouse"
1211:
3541:
3358:
3157:
3021:
3006:
2969:
2800:
2785:
2780:
2775:
2770:
2765:
2760:
2755:
754:
712:
698:
643:
616:
571:
459:
454:
449:
363:
351:
299:
3516:
3388:
3373:
3368:
3058:
3026:
2964:
2372:
2149:
1502:
608:
587:
323:
227:
223:
2391:
2346:
2307:
2258:
2250:
2215:
2172:
2145:"Annexin I is an endogenous ligand that mediates apoptotic cell engulfment"
2129:
2104:"Annexin I is an endogenous ligand that mediates apoptotic cell engulfment"
2080:
2004:
1947:
1906:
1865:
1806:
1767:
1724:
1697:
1688:
1671:
1615:
1606:
1596:
1578:
1420:
1371:
1301:
1293:
1254:
1219:
630:
Moreover, annexin A-I has further medical implications in the treatment of
215:. They are mostly found in eukaryotic organisms (animal, plant and fungi).
2071:
2054:
2039:
1986:
1824:
1732:
1656:
1560:
1510:
1161:
1118:
1075:
1057:
634:. Annexin A-I can be used as a cell surface protein to mark some forms of
97:
3521:
3282:
3193:
3011:
2956:
2496:
1464:
911:
897:
883:
869:
855:
841:
827:
813:
799:
785:
771:
757:
743:
729:
715:
701:
534:
498:
493:
246:
64:
2207:
1760:
10.1002/1439-7633(20010803)2:7/8<587::AID-CBIC587>3.0.CO;2-Q
1437:
Creutz Carl E.; Pazoles
Christopher J.; Pollard Harvey B. (April 1978).
222:. However some annexins (Annexin A1, Annexin A2, and Annexin A5) can be
3531:
3485:
3406:
3290:
3203:
2940:
2795:
2427:
1153:
976:
675:
579:
354:
is a physical construct for variation between subfamilies of annexins.
279:
262:
212:
81:
76:
1897:
1880:
1856:
1839:
558:
in the cell membrane in vivo with a relatively high binding affinity.
3340:
3310:
3252:
3247:
3242:
3237:
3232:
3214:
3041:
3036:
2994:
2989:
2935:
2923:
2918:
2913:
2717:
2712:
2289:
2274:"Annexin II regulates fibrin homeostasis and neoangiogenesis in vivo"
1246:
1110:
940:
936:
679:
635:
631:
603:
Annexin A-I seems to be one of the most heavily involved annexins in
547:
191:
1363:
1881:"Annexins--unique membrane binding proteins with diverse functions"
28:
3431:
3426:
3421:
3416:
3411:
3335:
3330:
3320:
3315:
3305:
3300:
3295:
3264:
3259:
3227:
3198:
3167:
3162:
3152:
3140:
3135:
3130:
3063:
2984:
2979:
2974:
2908:
2581:
2576:
2571:
2561:
2556:
2551:
2546:
980:
964:
960:
956:
952:
948:
944:
928:
566:
350:
family and the N-terminus varies greatly. The variability of the
561:
In addition, Annexin A-II can bind other membrane lipids such as
505:
internalization and the biogenesis of multi-vesicular endosomes.
3463:
3125:
3120:
3115:
3110:
3105:
3100:
3095:
3090:
2729:
2687:
2682:
2541:
2536:
2526:
2521:
2516:
2506:
1198:
Gerke V, Moss S (2002). "Annexins: form structure to function".
555:
530:
418:
Annexin species (II,V,XI) have been found within the membranes.
153:
108:
52:
2436:
654:
Annexin A-V is the major player when it comes to mechanisms of
341:, which comes from the Greek word “synexis” meaning “meeting”.
1838:
Rescher U, Ruhe D, Ludwig C, Zobiack N, Gerke V (July 2004).
501:
coated budding events, while annexin II participates in both
329:
The first study to identify annexins was published by Creutz
529:
In addition, annexins A-I and A-II have been shown to bind
366:
residue, upon calcium binding, which can interact with the
2406:
1789:
Creutz CE, Snyder SL, Daigle SN, Redick J (March 1996).
666:
While several annexins may be involved in mechanisms of
615:
of tissues by interacting with annexin A-I receptors on
611:
or damage to tissues, annexin A-I is believed to reduce
689:
that thrive on blood clotting through fibrin networks.
1920:
Hayes MJ, Rescher U, Gerke V, Moss SE (August 2004).
448:
Annexins have been observed to play a role along the
3506:
3484:
3396:
3386:
3351:
3280:
3212:
3178:
2951:
2901:
2871:
2843:
2833:
2746:
2728:
2698:
2592:
2487:
2478:
190:
170:
152:
147:
131:
119:
107:
87:
75:
63:
51:
43:
38:
21:
230:to outside cellular environments, such as blood.
678:. Plasmin initiates fibrinolysis by degrading
2448:
1193:
1191:
1189:
1187:
1185:
1183:
1181:
1179:
218:In humans, the annexins are found inside the
8:
1528:
1526:
1524:
1522:
1520:
1476:
1474:
1432:
1430:
1572:
1570:
3393:
2840:
2484:
2455:
2441:
2433:
2413:UMich Orientation of Proteins in Membranes
1629:Genge BR, Wu LN, Wuthier RE (March 1990).
144:
2381:
2371:
2297:
2162:
2119:
2070:
1994:
1937:
1896:
1855:
1814:
1687:
1646:
1605:
1595:
1550:
1454:
1410:
1065:
1001:at the U.S. National Library of Medicine
211:is a common name for a group of cellular
1345:
1343:
1341:
1339:
1337:
1335:
1333:
1331:
991:
1329:
1327:
1325:
1323:
1321:
1319:
1317:
1315:
1313:
1311:
18:
1274:
1272:
924:Human proteins containing this domain
541:Membrane organization and trafficking
7:
1969:Tomas A, Futter C, Moss SE (2004).
1042:"Annexins in the secretory pathway"
550:in the bilayer near sites of actin
2339:10.1111/j.1574-6968.1999.tb13496.x
1040:Donnelly SR, Moss SE (June 1997).
333:(1978). These authors used bovine
14:
1939:10.1111/j.1600-0854.2004.00210.x
1879:Rescher U, Gerke V (June 2004).
1535:"Annexins and membrane dynamics"
638:that can be targeted by various
554:assembly. Annexin A-II can bind
27:
2891:Calcium-induced calcium release
1443:Journal of Biological Chemistry
33:Structure of human annexin III.
2612:Ionotropic glutamate receptors
2143:Arur, S.; et al. (2003).
1533:Gerke V, Moss SE (June 1997).
1:
2164:10.1016/S1534-5807(03)00090-X
2121:10.1016/S1534-5807(03)00090-X
2032:10.1016/S0163-7258(96)00203-3
1648:10.1016/S0021-9258(19)39619-X
1552:10.1016/S0167-4889(97)00038-4
1456:10.1016/S0021-9258(17)40901-X
674:, which functions to produce
148:Available protein structures:
3573:Peripheral membrane proteins
3464:Dentin matrix phosphoprotein
2409:, acquired on 20 August 2005
1922:"Annexin-actin interactions"
1412:10.1016/j.bbamcr.2008.01.030
2354:Moss SE, Morgan RO (2004).
3589:
3469:Dentin sialophosphoprotein
1212:10.1152/physrev.00030.2001
599:Apoptosis and inflammation
2931:Sodium-calcium exchangers
2708:Sodium-calcium exchangers
2407:European Annexin Homepage
439:Role in vesicle transport
266:(Geisow) coined the name
233:Annexin is also known as
143:
26:
3017:Neuronal calcium sensors
2738:Calcium-sensing receptor
2424:Annexins repeated domain
1577:Tomas A, Moss S (2003).
1352:Nat. Rev. Mol. Cell Biol
1003:Medical Subject Headings
839:Annexin, type fungal XIV
2417:families/superfamily-43
2373:10.1186/gb-2004-5-4-219
1503:10.1126/science.8362244
1016:"lipocortin definition"
687:cardiovascular diseases
486:epidermal growth factor
237:. Lipocortins suppress
2873:Intracellular channels
2251:10.1006/jaut.2000.0410
1807:10.1083/jcb.132.6.1079
1725:10.1006/jmbi.1994.1129
1689:10.1074/jbc.M409009200
1597:10.1074/jbc.M212669200
1539:Biochim. Biophys. Acta
1399:Biochim. Biophys. Acta
1294:10.1006/jmbi.2000.4183
2072:10.1096/fj.02-0239fje
1987:10.1083/jcb.200311054
1058:10.1007/s000180050068
646:against annexin A-I.
594:Clinical significance
400:Cellular localization
391:family, and includes
3398:Extracellular matrix
2327:FEMS Microbiol. Lett
895:Annexin like protein
509:Membrane scaffolding
3364:Parathyroid hormone
3352:Indirect regulators
2902:Intracellular pumps
2208:10.1038/nature02580
2200:2004Natur.429..629O
1590:(22): 20210–20216.
1495:1993Sci...261.1321C
1046:Cell. Mol. Life Sci
853:Annexin, type plant
524:phosphatidylcholine
3444:Matrix gla protein
3281:Calcium-dependent
3213:Calcium-dependent
3179:Calcium-dependent
2886:Ryanodine receptor
2489:Adhesion molecules
2472:calcium metabolism
1850:(Pt 16): 3473–80.
1154:10.1007/BF01121450
867:Annexin, type XIII
825:Annexin, type XXXI
811:Annexin, type VIII
519:phosphatidylserine
3550:
3549:
3502:
3501:
3486:Secreted hormones
3459:Bone sialoprotein
3382:
3381:
2845:Second messengers
2829:
2828:
2622:Kainate receptors
2468:calcium signaling
1898:10.1242/jcs.01245
1891:(Pt 13): 2631–9.
1857:10.1242/jcs.01208
881:Annexin, type VII
727:Annexin, type III
693:Types/subfamilies
605:anti-inflammatory
576:endothelial cells
503:cholesteryl ester
360:second messengers
306:and also calcium
206:
205:
202:
201:
197:structure summary
3580:
3568:Protein families
3507:Calcium-binding
3394:
3272:Protein kinase C
2841:
2594:Calcium channels
2485:
2457:
2450:
2443:
2434:
2395:
2385:
2375:
2350:
2312:
2311:
2301:
2290:10.1172/JCI19684
2269:
2263:
2262:
2234:
2228:
2227:
2194:(6992): 629–35.
2183:
2177:
2176:
2166:
2140:
2134:
2133:
2123:
2099:
2093:
2092:
2074:
2050:
2044:
2043:
2015:
2009:
2008:
1998:
1966:
1960:
1959:
1941:
1917:
1911:
1910:
1900:
1876:
1870:
1869:
1859:
1835:
1829:
1828:
1818:
1786:
1780:
1779:
1743:
1737:
1736:
1708:
1702:
1701:
1691:
1667:
1661:
1660:
1650:
1626:
1620:
1619:
1609:
1599:
1574:
1565:
1564:
1554:
1530:
1515:
1514:
1489:(5126): 1321–4.
1478:
1469:
1468:
1458:
1434:
1425:
1424:
1414:
1390:
1384:
1383:
1347:
1306:
1305:
1276:
1267:
1266:
1247:10.1002/cm.21149
1230:
1224:
1223:
1195:
1174:
1173:
1137:
1131:
1130:
1111:10.1038/320636a0
1105:(6063): 636–38.
1094:
1088:
1087:
1069:
1037:
1031:
1030:
1028:
1027:
1018:. Archived from
1012:
1006:
996:
769:Annexin, type VI
741:Annexin, type IV
713:Annexin, type II
607:responses. Upon
462:in the organism
239:phospholipase A2
145:
31:
19:
3588:
3587:
3583:
3582:
3581:
3579:
3578:
3577:
3563:Protein domains
3553:
3552:
3551:
3546:
3537:EGF-like domain
3498:
3480:
3378:
3347:
3276:
3208:
3174:
2947:
2897:
2867:
2825:
2742:
2724:
2694:
2588:
2474:
2461:
2403:
2398:
2353:
2324:
2320:
2318:Further reading
2315:
2278:J. Clin. Invest
2271:
2270:
2266:
2236:
2235:
2231:
2185:
2184:
2180:
2142:
2141:
2137:
2101:
2100:
2096:
2052:
2051:
2047:
2020:Pharmacol. Ther
2017:
2016:
2012:
1968:
1967:
1963:
1919:
1918:
1914:
1878:
1877:
1873:
1837:
1836:
1832:
1788:
1787:
1783:
1754:(7–8): 587–90.
1745:
1744:
1740:
1710:
1709:
1705:
1682:(50): 52623–9.
1669:
1668:
1664:
1628:
1627:
1623:
1576:
1575:
1568:
1532:
1531:
1518:
1480:
1479:
1472:
1436:
1435:
1428:
1392:
1391:
1387:
1364:10.1038/nrm1661
1349:
1348:
1309:
1278:
1277:
1270:
1232:
1231:
1227:
1197:
1196:
1177:
1139:
1138:
1134:
1096:
1095:
1091:
1039:
1038:
1034:
1025:
1023:
1014:
1013:
1009:
997:
993:
989:
926:
797:Annexin, type X
755:Annexin, type V
699:Annexin, type I
695:
664:
652:
640:immunotherapies
601:
596:
543:
511:
490:tyrosine kinase
482:
446:
441:
429:
420:Tyrosine kinase
416:
407:
402:
393:phosphorylation
347:
288:plasma membrane
270:shortly after.
259:
243:glucocorticoids
121:OPM superfamily
34:
17:
12:
11:
5:
3586:
3584:
3576:
3575:
3570:
3565:
3555:
3554:
3548:
3547:
3545:
3544:
3539:
3534:
3529:
3524:
3519:
3513:
3511:
3504:
3503:
3500:
3499:
3497:
3496:
3490:
3488:
3482:
3481:
3479:
3478:
3477:
3476:
3471:
3466:
3461:
3451:
3446:
3441:
3436:
3435:
3434:
3429:
3424:
3419:
3414:
3403:
3401:
3391:
3387:Extracellular
3384:
3383:
3380:
3379:
3377:
3376:
3371:
3366:
3361:
3355:
3353:
3349:
3348:
3346:
3345:
3344:
3343:
3338:
3333:
3328:
3323:
3318:
3313:
3308:
3303:
3298:
3287:
3285:
3278:
3277:
3275:
3274:
3269:
3268:
3267:
3262:
3257:
3256:
3255:
3250:
3245:
3240:
3230:
3219:
3217:
3210:
3209:
3207:
3206:
3201:
3196:
3191:
3185:
3183:
3176:
3175:
3173:
3172:
3171:
3170:
3165:
3155:
3150:
3145:
3144:
3143:
3138:
3133:
3128:
3123:
3118:
3113:
3108:
3103:
3098:
3093:
3086:Synaptotagmins
3083:
3078:
3073:
3068:
3067:
3066:
3061:
3056:
3051:
3046:
3045:
3044:
3039:
3029:
3024:
3014:
3009:
3004:
2999:
2998:
2997:
2992:
2987:
2982:
2977:
2967:
2961:
2959:
2949:
2948:
2946:
2945:
2944:
2943:
2938:
2928:
2927:
2926:
2921:
2916:
2905:
2903:
2899:
2898:
2896:
2895:
2894:
2893:
2883:
2877:
2875:
2869:
2868:
2866:
2865:
2860:
2855:
2849:
2847:
2838:
2834:Intracellular
2831:
2830:
2827:
2826:
2824:
2823:
2818:
2813:
2808:
2803:
2798:
2793:
2788:
2783:
2778:
2773:
2768:
2763:
2758:
2752:
2750:
2744:
2743:
2741:
2740:
2734:
2732:
2726:
2725:
2723:
2722:
2721:
2720:
2715:
2704:
2702:
2696:
2695:
2693:
2692:
2691:
2690:
2685:
2680:
2670:
2669:
2668:
2663:
2658:
2653:
2648:
2638:
2637:
2636:
2631:
2630:
2629:
2627:NMDA receptors
2624:
2619:
2617:AMPA receptors
2609:
2607:5-HT3 receptor
2598:
2596:
2590:
2589:
2587:
2586:
2585:
2584:
2579:
2574:
2569:
2564:
2559:
2554:
2549:
2544:
2539:
2534:
2529:
2524:
2519:
2514:
2509:
2504:
2493:
2491:
2482:
2476:
2475:
2464:Cell signaling
2462:
2460:
2459:
2452:
2445:
2437:
2431:
2430:
2421:
2410:
2402:
2401:External links
2399:
2397:
2396:
2356:"The annexins"
2351:
2321:
2319:
2316:
2314:
2313:
2264:
2229:
2178:
2157:(4): 587–598.
2135:
2094:
2045:
2010:
1981:(6): 813–822.
1961:
1912:
1871:
1830:
1801:(6): 1079–92.
1781:
1738:
1719:(1): 199–208.
1703:
1662:
1641:(8): 4703–10.
1621:
1584:J. Biol. Chem.
1566:
1516:
1470:
1449:(8): 2858–66.
1426:
1385:
1307:
1268:
1241:(11): 775–95.
1225:
1175:
1132:
1089:
1032:
1007:
990:
988:
985:
925:
922:
921:
920:
906:
892:
878:
864:
850:
836:
822:
808:
794:
780:
766:
752:
738:
724:
710:
694:
691:
663:
660:
651:
648:
600:
597:
595:
592:
542:
539:
510:
507:
481:
478:
445:
442:
440:
437:
433:hydroxyapatite
428:
425:
415:
412:
406:
403:
401:
398:
380:hydrogen bonds
370:chains of the
346:
343:
335:adrenal glands
258:
255:
204:
203:
200:
199:
194:
188:
187:
174:
168:
167:
157:
150:
149:
141:
140:
135:
129:
128:
123:
117:
116:
111:
105:
104:
91:
85:
84:
79:
73:
72:
67:
61:
60:
55:
49:
48:
45:
41:
40:
36:
35:
32:
24:
23:
16:Protein family
15:
13:
10:
9:
6:
4:
3:
2:
3585:
3574:
3571:
3569:
3566:
3564:
3561:
3560:
3558:
3543:
3540:
3538:
3535:
3533:
3530:
3528:
3527:C-type lectin
3525:
3523:
3520:
3518:
3515:
3514:
3512:
3510:
3505:
3495:
3492:
3491:
3489:
3487:
3483:
3475:
3472:
3470:
3467:
3465:
3462:
3460:
3457:
3456:
3455:
3452:
3450:
3447:
3445:
3442:
3440:
3437:
3433:
3430:
3428:
3425:
3423:
3420:
3418:
3415:
3413:
3410:
3409:
3408:
3405:
3404:
3402:
3399:
3395:
3392:
3390:
3385:
3375:
3372:
3370:
3367:
3365:
3362:
3360:
3357:
3356:
3354:
3350:
3342:
3339:
3337:
3334:
3332:
3329:
3327:
3324:
3322:
3319:
3317:
3314:
3312:
3309:
3307:
3304:
3302:
3299:
3297:
3294:
3293:
3292:
3289:
3288:
3286:
3284:
3279:
3273:
3270:
3266:
3263:
3261:
3258:
3254:
3251:
3249:
3246:
3244:
3241:
3239:
3236:
3235:
3234:
3231:
3229:
3226:
3225:
3224:
3221:
3220:
3218:
3216:
3211:
3205:
3202:
3200:
3197:
3195:
3192:
3190:
3187:
3186:
3184:
3182:
3177:
3169:
3166:
3164:
3161:
3160:
3159:
3156:
3154:
3151:
3149:
3146:
3142:
3139:
3137:
3134:
3132:
3129:
3127:
3124:
3122:
3119:
3117:
3114:
3112:
3109:
3107:
3104:
3102:
3099:
3097:
3094:
3092:
3089:
3088:
3087:
3084:
3082:
3079:
3077:
3076:Phospholamban
3074:
3072:
3069:
3065:
3062:
3060:
3057:
3055:
3052:
3050:
3047:
3043:
3040:
3038:
3035:
3034:
3033:
3030:
3028:
3025:
3023:
3020:
3019:
3018:
3015:
3013:
3010:
3008:
3005:
3003:
3002:Calsequestrin
3000:
2996:
2993:
2991:
2988:
2986:
2983:
2981:
2978:
2976:
2973:
2972:
2971:
2968:
2966:
2963:
2962:
2960:
2958:
2954:
2950:
2942:
2939:
2937:
2934:
2933:
2932:
2929:
2925:
2922:
2920:
2917:
2915:
2912:
2911:
2910:
2907:
2906:
2904:
2900:
2892:
2889:
2888:
2887:
2884:
2882:
2879:
2878:
2876:
2874:
2870:
2864:
2861:
2859:
2856:
2854:
2851:
2850:
2848:
2846:
2842:
2839:
2837:
2832:
2822:
2819:
2817:
2814:
2812:
2809:
2807:
2804:
2802:
2799:
2797:
2794:
2792:
2789:
2787:
2784:
2782:
2779:
2777:
2774:
2772:
2769:
2767:
2764:
2762:
2759:
2757:
2754:
2753:
2751:
2749:
2745:
2739:
2736:
2735:
2733:
2731:
2727:
2719:
2716:
2714:
2711:
2710:
2709:
2706:
2705:
2703:
2701:
2700:Calcium pumps
2697:
2689:
2686:
2684:
2681:
2679:
2676:
2675:
2674:
2671:
2667:
2664:
2662:
2659:
2657:
2654:
2652:
2649:
2647:
2644:
2643:
2642:
2641:Voltage-gated
2639:
2635:
2634:P2X receptors
2632:
2628:
2625:
2623:
2620:
2618:
2615:
2614:
2613:
2610:
2608:
2605:
2604:
2603:
2600:
2599:
2597:
2595:
2591:
2583:
2580:
2578:
2575:
2573:
2570:
2568:
2565:
2563:
2560:
2558:
2555:
2553:
2550:
2548:
2545:
2543:
2540:
2538:
2535:
2533:
2530:
2528:
2525:
2523:
2520:
2518:
2515:
2513:
2510:
2508:
2505:
2503:
2500:
2499:
2498:
2495:
2494:
2492:
2490:
2486:
2483:
2481:
2480:Cell membrane
2477:
2473:
2469:
2465:
2458:
2453:
2451:
2446:
2444:
2439:
2438:
2435:
2429:
2425:
2422:
2419:
2418:
2414:
2411:
2408:
2405:
2404:
2400:
2393:
2389:
2384:
2379:
2374:
2369:
2365:
2361:
2357:
2352:
2348:
2344:
2340:
2336:
2333:(1): 147–53.
2332:
2328:
2323:
2322:
2317:
2309:
2305:
2300:
2295:
2291:
2287:
2283:
2279:
2275:
2268:
2265:
2260:
2256:
2252:
2248:
2245:(2): 107–11.
2244:
2240:
2233:
2230:
2225:
2221:
2217:
2213:
2209:
2205:
2201:
2197:
2193:
2189:
2182:
2179:
2174:
2170:
2165:
2160:
2156:
2152:
2151:
2146:
2139:
2136:
2131:
2127:
2122:
2117:
2114:(4): 587–98.
2113:
2109:
2105:
2098:
2095:
2090:
2086:
2082:
2078:
2073:
2068:
2064:
2060:
2056:
2049:
2046:
2041:
2037:
2033:
2029:
2026:(1): 73–102.
2025:
2021:
2014:
2011:
2006:
2002:
1997:
1992:
1988:
1984:
1980:
1976:
1972:
1965:
1962:
1957:
1953:
1949:
1945:
1940:
1935:
1931:
1927:
1923:
1916:
1913:
1908:
1904:
1899:
1894:
1890:
1886:
1882:
1875:
1872:
1867:
1863:
1858:
1853:
1849:
1845:
1841:
1834:
1831:
1826:
1822:
1817:
1812:
1808:
1804:
1800:
1796:
1792:
1785:
1782:
1777:
1773:
1769:
1765:
1761:
1757:
1753:
1749:
1742:
1739:
1734:
1730:
1726:
1722:
1718:
1714:
1707:
1704:
1699:
1695:
1690:
1685:
1681:
1677:
1676:J. Biol. Chem
1673:
1666:
1663:
1658:
1654:
1649:
1644:
1640:
1636:
1635:J. Biol. Chem
1632:
1625:
1622:
1617:
1613:
1608:
1607:10044/1/42329
1603:
1598:
1593:
1589:
1586:
1585:
1580:
1573:
1571:
1567:
1562:
1558:
1553:
1548:
1545:(2): 129–54.
1544:
1540:
1536:
1529:
1527:
1525:
1523:
1521:
1517:
1512:
1508:
1504:
1500:
1496:
1492:
1488:
1484:
1477:
1475:
1471:
1466:
1462:
1457:
1452:
1448:
1444:
1440:
1433:
1431:
1427:
1422:
1418:
1413:
1408:
1405:(6): 953–63.
1404:
1400:
1396:
1389:
1386:
1381:
1377:
1373:
1369:
1365:
1361:
1358:(6): 449–61.
1357:
1353:
1346:
1344:
1342:
1340:
1338:
1336:
1334:
1332:
1330:
1328:
1326:
1324:
1322:
1320:
1318:
1316:
1314:
1312:
1308:
1303:
1299:
1295:
1291:
1288:(4): 561–73.
1287:
1283:
1275:
1273:
1269:
1264:
1260:
1256:
1252:
1248:
1244:
1240:
1236:
1229:
1226:
1221:
1217:
1213:
1209:
1206:(2): 331–71.
1205:
1201:
1194:
1192:
1190:
1188:
1186:
1184:
1182:
1180:
1176:
1171:
1167:
1163:
1159:
1155:
1151:
1148:(4): 289–98.
1147:
1143:
1136:
1133:
1128:
1124:
1120:
1116:
1112:
1108:
1104:
1100:
1093:
1090:
1085:
1081:
1077:
1073:
1068:
1063:
1059:
1055:
1051:
1047:
1043:
1036:
1033:
1022:on 2007-06-14
1021:
1017:
1011:
1008:
1004:
1000:
995:
992:
986:
984:
982:
978:
974:
970:
966:
962:
958:
954:
950:
946:
942:
938:
934:
930:
923:
919:
918:
913:
910:
907:
905:
904:
899:
896:
893:
891:
890:
885:
882:
879:
877:
876:
871:
868:
865:
863:
862:
857:
854:
851:
849:
848:
843:
840:
837:
835:
834:
829:
826:
823:
821:
820:
815:
812:
809:
807:
806:
801:
798:
795:
793:
792:
787:
784:
783:Alpha giardin
781:
779:
778:
773:
770:
767:
765:
764:
759:
756:
753:
751:
750:
745:
742:
739:
737:
736:
731:
728:
725:
723:
722:
717:
714:
711:
709:
708:
703:
700:
697:
696:
692:
690:
688:
683:
681:
677:
673:
669:
661:
659:
657:
649:
647:
645:
641:
637:
633:
628:
624:
622:
618:
614:
610:
606:
598:
593:
591:
589:
585:
581:
577:
573:
568:
564:
559:
557:
553:
549:
540:
538:
536:
532:
527:
525:
520:
515:
508:
506:
504:
500:
495:
491:
487:
479:
477:
475:
472:
467:
465:
461:
457:
456:
451:
443:
438:
436:
434:
426:
424:
421:
413:
411:
404:
399:
397:
394:
390:
389:S-100 protein
385:
381:
375:
373:
372:lipid bilayer
369:
365:
361:
355:
353:
344:
342:
340:
336:
332:
327:
325:
321:
317:
313:
309:
305:
301:
297:
291:
289:
283:
281:
277:
276:phospholipids
271:
269:
264:
256:
254:
252:
248:
244:
240:
236:
231:
229:
225:
221:
216:
214:
210:
198:
195:
193:
189:
186:
182:
178:
175:
173:
169:
165:
161:
158:
155:
151:
146:
142:
139:
136:
134:
130:
127:
124:
122:
118:
115:
112:
110:
106:
103:
99:
95:
92:
90:
86:
83:
80:
78:
74:
71:
68:
66:
62:
59:
56:
54:
50:
46:
42:
37:
30:
25:
20:
3439:Hemicentin 1
3189:Calreticulin
3081:Sarcalumenin
2881:IP3 receptor
2747:
2673:TRP channels
2602:Ligand-gated
2415:
2363:
2359:
2330:
2326:
2284:(1): 38–48.
2281:
2277:
2267:
2242:
2239:J. Autoimmun
2238:
2232:
2191:
2187:
2181:
2154:
2148:
2138:
2111:
2107:
2097:
2065:(2): 253–5.
2062:
2058:
2048:
2023:
2019:
2013:
1978:
1975:J. Cell Biol
1974:
1964:
1932:(8): 571–6.
1929:
1925:
1915:
1888:
1884:
1874:
1847:
1843:
1833:
1798:
1795:J. Cell Biol
1794:
1784:
1751:
1747:
1741:
1716:
1713:J. Mol. Biol
1712:
1706:
1679:
1675:
1665:
1638:
1634:
1624:
1587:
1582:
1542:
1538:
1486:
1482:
1446:
1442:
1402:
1398:
1388:
1355:
1351:
1285:
1282:J. Mol. Biol
1281:
1238:
1235:Cytoskeleton
1234:
1228:
1203:
1200:Physiol. Rev
1199:
1145:
1141:
1135:
1102:
1098:
1092:
1052:(6): 533–8.
1049:
1045:
1035:
1024:. Retrieved
1020:the original
1010:
994:
927:
915:
901:
887:
873:
859:
845:
831:
817:
803:
789:
775:
761:
747:
733:
719:
705:
684:
668:fibrinolysis
665:
662:Fibrinolysis
653:
629:
625:
613:inflammation
602:
560:
552:cytoskeleton
544:
528:
516:
512:
483:
468:
463:
453:
447:
430:
417:
408:
376:
356:
348:
330:
328:
320:inflammation
312:fibrinolysis
292:
284:
272:
267:
260:
257:Introduction
251:inflammation
234:
232:
217:
208:
207:
3494:Osteocalcin
3474:Osteopontin
3449:Osteonectin
3223:CaM kinases
3071:Parvalbumin
3054:Neurocalcin
3049:Hippocalcin
2360:Genome Biol
1885:J. Cell Sci
1844:J. Cell Sci
1748:ChemBioChem
1142:Biosci. Rep
672:plasminogen
656:coagulation
650:Coagulation
621:neutrophils
584:cytokinesis
563:cholesterol
480:Endocytosis
384:amphipathic
368:hydrocarbon
316:coagulation
308:ion channel
304:endocytosis
133:OPM protein
39:Identifiers
3557:Categories
3542:Gla domain
3359:Calcitonin
3181:chaperones
3158:Troponin C
3022:Calsenilin
3007:Calretinin
2970:Calmodulin
2366:(4): 219.
1026:2007-03-10
987:References
909:Annexin XI
644:antibodies
617:leukocytes
572:epithelial
471:chromaffin
464:Paramecium
460:organelles
455:Paramecium
450:exocytotic
444:Exocytosis
364:tryptophan
352:N-terminus
300:exocytosis
249:) inhibit
235:lipocortin
160:structures
3517:C2 domain
3389:chelators
3374:Vitamin K
3369:Vitamin D
3283:proteases
3059:Recoverin
3027:Frequenin
2965:Calbindin
2957:chelators
2836:signaling
2497:Cadherins
2150:Dev. Cell
2108:Dev. Cell
1263:205643538
917:IPR015475
903:IPR015472
889:IPR013286
875:IPR009166
861:IPR009118
847:IPR009117
833:IPR009116
819:IPR009115
805:IPR008156
791:IPR008088
777:IPR002393
763:IPR002392
749:IPR002391
735:IPR002390
721:IPR002389
707:IPR002388
609:infection
588:apoptosis
345:Structure
324:apoptosis
245:(such as
228:cytoplasm
226:from the
82:PDOC00195
70:IPR001464
3522:Cadherin
3454:SIBLINGs
3407:Fibulins
3400:proteins
3291:Calpains
3194:Calnexin
3012:Gelsolin
2748:Annexins
2392:15059252
2347:10220891
2308:14702107
2259:10968894
2216:15190345
2173:12689596
2130:12689596
2089:18895764
2081:12475898
2005:15197175
1956:11551148
1948:15260827
1907:15169834
1866:15226372
1776:23310803
1768:11828493
1698:15381697
1616:12601007
1421:18334229
1380:37526262
1372:15928709
1302:11099380
1255:24155256
1220:11917092
1170:20709760
1084:36108081
1067:11147375
999:Annexins
912:InterPro
898:InterPro
884:InterPro
870:InterPro
856:InterPro
842:InterPro
828:InterPro
814:InterPro
800:InterPro
786:InterPro
772:InterPro
758:InterPro
744:InterPro
730:InterPro
716:InterPro
702:InterPro
535:nematode
499:clathrin
494:endosome
474:granules
405:Membrane
296:vesicles
247:cortisol
224:secreted
213:proteins
177:RCSB PDB
65:InterPro
3532:EF hand
3509:domains
3215:kinases
3204:HSP90B1
3064:Visinin
2953:Sensors
2941:SLC24A5
2428:PROSITE
2224:4386303
2196:Bibcode
2059:FASEB J
2040:9336017
1996:2172404
1926:Traffic
1825:8601586
1816:2120750
1733:8107105
1657:2155235
1561:9223619
1511:8362244
1491:Bibcode
1483:Science
1162:2960386
1127:4361070
1119:2422556
1076:9230932
977:ANXA8L2
973:ANXA8L1
914::
900::
886::
872::
858::
844::
830::
816::
802::
788::
774::
760::
746::
732::
718::
704::
676:plasmin
580:mitosis
339:synexin
280:calcium
268:Annexin
263:protein
209:Annexin
77:PROSITE
58:PF00191
47:Annexin
22:Annexin
3341:CAPN10
2995:CALML5
2990:CALML3
2936:SLC8B1
2924:ATP2A3
2919:ATP2A2
2914:ATP2A1
2718:SLC8A1
2713:SLC3A2
2390:
2383:395778
2380:
2345:
2306:
2299:300771
2296:
2257:
2222:
2214:
2188:Nature
2171:
2128:
2087:
2079:
2038:
2003:
1993:
1954:
1946:
1905:
1864:
1823:
1813:
1774:
1766:
1731:
1696:
1655:
1614:
1559:
1509:
1465:632306
1463:
1419:
1378:
1370:
1300:
1261:
1253:
1218:
1168:
1160:
1125:
1117:
1099:Nature
1082:
1074:
1064:
1005:(MeSH)
971:;
967:;
963:;
955:;
951:;
947:;
941:ANXA13
937:ANXA11
933:ANXA10
931:;
680:fibrin
636:tumors
632:cancer
548:lipids
414:Nuclei
331:et al.
192:PDBsum
166:
156:
114:1.A.31
102:SUPFAM
44:Symbol
3432:FBLN5
3427:FBLN4
3422:FBLN3
3417:FBLN2
3412:FBLN1
3336:CAPN9
3331:CAPN8
3326:CAPN7
3321:CAPN6
3316:CAPN5
3311:CAPN4
3306:CAPN3
3301:CAPN2
3296:CAPN1
3265:CAMK4
3260:CAMK3
3233:CAMK2
3228:CAMK1
3199:HSPA5
3168:TNNC2
3163:TNNC1
3153:S100P
3141:SYT14
3136:SYT13
3131:SYT11
2985:CALM3
2980:CALM2
2975:CALM1
2909:SERCA
2863:cADPR
2858:NAADP
2796:A8-L2
2730:GPCRs
2582:CDH17
2577:CDH16
2572:CDH15
2567:CDH14
2562:CDH13
2557:CDH12
2552:CDH11
2547:CDH10
2220:S2CID
2085:S2CID
1952:S2CID
1772:S2CID
1376:S2CID
1259:S2CID
1166:S2CID
1123:S2CID
1080:S2CID
981:ANXA9
969:ANXA8
965:ANXA7
961:ANXA6
957:ANXA5
953:ANXA4
949:ANXA3
945:ANXA2
943:;
939:;
935:;
929:ANXA1
642:with
567:actin
278:in a
98:SCOPe
89:SCOP2
3148:S100
3126:SYT9
3121:SYT7
3116:SYT6
3111:SYT5
3106:SYT4
3101:SYT3
3096:SYT2
3091:SYT1
3032:GUCA
2955:and
2688:TRPV
2683:TRPC
2678:TRPA
2542:CDH9
2537:CDH8
2532:CDH7
2527:CDH6
2522:CDH5
2517:CDH4
2512:CDH3
2507:CDH2
2502:CDH1
2470:and
2388:PMID
2343:PMID
2304:PMID
2255:PMID
2212:PMID
2169:PMID
2126:PMID
2077:PMID
2036:PMID
2001:PMID
1944:PMID
1903:PMID
1862:PMID
1821:PMID
1764:PMID
1729:PMID
1694:PMID
1653:PMID
1612:PMID
1557:PMID
1543:1357
1507:PMID
1461:PMID
1417:PMID
1403:1783
1368:PMID
1298:PMID
1251:PMID
1216:PMID
1158:PMID
1115:PMID
1072:PMID
979:;
975:;
574:and
556:PIP2
531:PIP2
427:Bone
322:and
261:The
220:cell
185:PDBj
181:PDBe
164:ECOD
154:Pfam
138:1w3w
109:TCDB
94:2ran
53:Pfam
2853:IP3
2821:A13
2816:A12
2811:A11
2806:A10
2426:in
2378:PMC
2368:doi
2335:doi
2331:173
2294:PMC
2286:doi
2282:113
2247:doi
2204:doi
2192:429
2159:doi
2116:doi
2067:doi
2028:doi
1991:PMC
1983:doi
1979:165
1934:doi
1893:doi
1889:117
1852:doi
1848:117
1811:PMC
1803:doi
1799:132
1756:doi
1721:doi
1717:236
1684:doi
1680:279
1643:doi
1639:265
1602:hdl
1592:doi
1588:278
1547:doi
1499:doi
1487:261
1451:doi
1447:253
1407:doi
1360:doi
1290:doi
1286:304
1243:doi
1208:doi
1150:doi
1107:doi
1103:320
1062:PMC
1054:doi
172:PDB
3559::
3042:1B
3037:1A
2801:A9
2791:A8
2786:A7
2781:A6
2776:A5
2771:A4
2766:A3
2761:A2
2756:A1
2466::
2386:.
2376:.
2362:.
2358:.
2341:.
2329:.
2302:.
2292:.
2280:.
2276:.
2253:.
2243:15
2241:.
2218:.
2210:.
2202:.
2190:.
2167:.
2153:.
2147:.
2124:.
2110:.
2106:.
2083:.
2075:.
2063:17
2061:.
2057:.
2034:.
2024:74
2022:.
1999:.
1989:.
1977:.
1973:.
1950:.
1942:.
1928:.
1924:.
1901:.
1887:.
1883:.
1860:.
1846:.
1842:.
1819:.
1809:.
1797:.
1793:.
1770:.
1762:.
1750:.
1727:.
1715:.
1692:.
1678:.
1674:.
1651:.
1637:.
1633:.
1610:.
1600:.
1581:.
1569:^
1555:.
1541:.
1537:.
1519:^
1505:.
1497:.
1485:.
1473:^
1459:.
1445:.
1441:.
1429:^
1415:.
1401:.
1397:.
1374:.
1366:.
1354:.
1310:^
1296:.
1284:.
1271:^
1257:.
1249:.
1239:70
1237:.
1214:.
1204:82
1202:.
1178:^
1164:.
1156:.
1144:.
1121:.
1113:.
1101:.
1078:.
1070:.
1060:.
1050:53
1048:.
1044:.
983:;
959:;
590:.
582::
488:)
466:.
374:.
326:.
318:,
314:,
302:,
298:,
253:.
183:;
179:;
162:/
126:41
100:/
96:/
3253:G
3248:D
3243:B
3238:A
2666:T
2661:R
2656:P
2651:N
2646:L
2456:e
2449:t
2442:v
2394:.
2370::
2364:5
2349:.
2337::
2310:.
2288::
2261:.
2249::
2226:.
2206::
2198::
2175:.
2161::
2155:4
2132:.
2118::
2112:4
2091:.
2069::
2042:.
2030::
2007:.
1985::
1958:.
1936::
1930:5
1909:.
1895::
1868:.
1854::
1827:.
1805::
1778:.
1758::
1752:2
1735:.
1723::
1700:.
1686::
1659:.
1645::
1618:.
1604::
1594::
1563:.
1549::
1513:.
1501::
1493::
1467:.
1453::
1423:.
1409::
1382:.
1362::
1356:6
1304:.
1292::
1265:.
1245::
1222:.
1210::
1172:.
1152::
1146:7
1129:.
1109::
1086:.
1056::
1029:.
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
